eF-site ID 5dgy-ABCD
PDB Code 5dgy
Chain A, B, C, D

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Title Crystal structure of rhodopsin bound to visual arrestin
Classification SIGNALING PROTEIN
Compound Endolysin,Rhodopsin,S-arrestin
Source (ARRS_MOUSE)
Sequence A:  NIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNA
AKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRN
AKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRML
QQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAY
MCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQFSML
AAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLA
VADLFMVLGGFTSTLYTSLHGYFVFGPTGCNLQGFFATLG
GEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFT
WVMALACAAPPLAGWSRYIPEGLQCSCGIDYYTLKPEVNN
ESFVIYMFVVHFTIPMIIIFFCYGQLVFTVKEAAAQQQES
ATTQKAEKEVTRMVIIYVIAFLICWVPYASVAFYIFTHQG
SCFGPIFMTIPAFFAKSAAIYNPVIYIMMNKQFRNCMLTT
ICCGKNVIFKKVSRDKSVTIYLGKRDYVDHVSQVEPVDGV
VLVDPELVKGKKVYVTLTCAFRYGQEDIDVMGLTFRRDLY
FSRVQVYPPVGAMSVLTQLQESLLKKLGDNTYPFLLTFPD
YLPCSVMLQPAPQDVGKSCGVDFEVKAFASDITDPEEDKI
PKKSSVRLLIRKVQHAPPEMGPQPSAEASWQFFMSDKPLN
LSVSLSKEIYFHGEPIPVTVTVTNNTDKVVKKIKVSVEQI
ANVVLYSSDYYVKPVASEETQEKVQPNSTLTKTLVLVPLL
ANNRERRGIALDGKIKHEDTNLASSTIIKEGIDRTVMGIL
VSYHIKVKLTVSGFLTSSEVATEVPFRLMHPQP
B:  MCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQFSML
AAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLA
VADLFMVLGGFTSTLYTSLHGYFVFGPTGCNLQGFFATLG
GEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFT
WVMALACAAPPLAGWSRYIPEGLQCSCGIDYYTLKPEVNN
ESFVIYMFVVHFTIPMIIIFFCYGQLVFTVKEAAAQQQES
ATTQKAEKEVTRMVIIYVIAFLICWVPYASVAFYIFTHQG
SCFGPIFMTIPAFFAKSAAIYNPVIYIMMNKQFRNCMLTT
ICCGKNVIFKKVSRDKSVTIYLGKRDYVDHVSQVEPVDGV
VLVDPELVKGKKVYVTLTCAFRYGQEDIDVMGLTFRRDLY
FSRVQVYPPVGAMSVLTQLQESLLKKLGDNTYPFLLTFPD
YLPCSVMLQPAPQDVGKSCGVDFEVKAFASDITDPEEDKI
PKKSSVRLLIRKVQHAPPEMGPQPSAEASWQFFMSDKPLN
LSVSLSKEIYFHGEPIPVTVTVTNNTDKVVKKIKVSVEQI
ANVVLYSSDYYVKPVASEETQEKVQPNSTLTKTLVLVPLL
ANNRERRGIALDGKIKHEDTNLASSTIIKEGIDRTVMGIL
VSYHIKVKLTVSGFLTSSEVATEVPFRLMHPQP
C:  NIFEMLRIDEGVITKDEAEKLFNQDVDAAVRGILRNAKLK
PVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKR
WDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYMCGT
EGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQFSMLAAYM
FLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADL
FMVLGGFTSTLYTSLHGYFVFGPTGCNLQGFFATLGGEIA
LWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMA
LACAAPPLAGWSRYIPEGLQCSCGIDYYTLKPEVNNESFV
IYMFVVHFTIPMIIIFFCYGQLVFTVKEAAAQQQESATTQ
KAEKEVTRMVIIYVIAFLICWVPYASVAFYIFTHQGSCFG
PIFMTIPAFFAKSAAIYNPVIYIMMNKQFRNCMLTTICCG
KNVIFKKVSRDKSVTIYLGKRDYVDHVSQVEPVDGVVLVD
PELVKGKKVYVTLTCAFRYGQEDIDVMGLTFRRDLYFSRV
QVYPPVGAMSVLTQLQESLLKKLGDNTYPFLLTFPDYLPC
SVMLQPAPQDVGKSCGVDFEVKAFASDITDPEEDKIPKKS
SVRLLIRKVQHAPPEMGPQPSAEASWQFFMSDKPLNLSVS
LSKEIYFHGEPIPVTVTVTNNTDKVVKKIKVSVEQIANVV
LYSSDYYVKPVASEETQEKVQPNSTLTKTLVLVPLLANNR
ERRGIALDGKIKHEDTNLASSTIIKEGIDRTVMGILVSYH
IKVKLTVSGFLTSSEVATEVPFRLMHPQP
D:  NIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNA
AKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRN
AKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRML
QQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAY
MCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQFSML
AAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLA
VADLFMVLGGFTSTLYTSLHGYFVFGPTGCNLQGFFATLG
GEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFT
WVMALACAAPPLAGWSRYIPEGLQCSCGIDYYTLKPEVNN
ESFVIYMFVVHFTIPMIIIFFCYGQLVFTVKEAAAQQQES
ATTQKAEKEVTRMVIIYVIAFLICWVPYASVAFYIFTHQG
SCFGPIFMTIPAFFAKSAAIYNPVIYIMMNKQFRNCMLTT
ICCGKNVIFKKVSRDKSVTIYLGKRDYVDHVSQVEPVDGV
VLVDPELVKGKKVYVTLTCAFRYGQEDIDVMGLTFRRDLY
FSRVQVYPPVGAMSVLTQLQESLLKKLGDNTYPFLLTFPD
YLPCSVMLQPAPQDVGKSCGVDFEVKAFASDITDPEEDKI
PKKSSVRLLIRKVQHAPPEMGPQPSAEASWQFFMSDKPLN
LSVSLSKEIYFHGEPIPVTVTVTNNTDKVVKKIKVSVEQI
ANVVLYSSDYYVKPVASEETQEKVQPNSTLTKTLVLVPLL
ANNRERRGIALDGKIKHEDTNLASSTIIKEGIDRTVMGIL
VSYHIKVKLTVSGFLTSSEVATEVPFRLMHPQP
Description


Functional site

1) chain A
residue -150
type catalytic
sequence E
description 921
source MCSA : MCSA1

2) chain A
residue -141
type catalytic
sequence D
description 921
source MCSA : MCSA1

3) chain C
residue -150
type catalytic
sequence E
description 921
source MCSA : MCSA3

4) chain D
residue -150
type catalytic
sequence E
description 921
source MCSA : MCSA4

5) chain D
residue -141
type catalytic
sequence D
description 921
source MCSA : MCSA4

6) chain A
residue 123-139
type prosite
sequence IALWSLVVLAIERYVVV
description G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. IALwSLVVLAIERYVvV
source prosite : PS00237

7) chain A
residue 290-306
type prosite
sequence IPAFFAKSAAIYNPVIY
description OPSIN Visual pigments (opsins) retinal binding site. IPaFfAKSAAiyNPviY
source prosite : PS00238

8) chain A
residue 1066-1084
type prosite
sequence FRYGQEDIDVMGLTFRRDL
description ARRESTINS Arrestins signature. FRYGqEDiDVMGLtFrRDL
source prosite : PS00295

9) chain A
residue -150
type ACT_SITE
sequence E
description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI1

10) chain C
residue -150
type ACT_SITE
sequence E
description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI1

11) chain D
residue -150
type ACT_SITE
sequence E
description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI1

12) chain A
residue 153-173
type TRANSMEM
sequence AIMGVAFTWVMALACAAPPLA
description Helical; Name=4 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI10

13) chain B
residue 153-173
type TRANSMEM
sequence AIMGVAFTWVMALACAAPPLA
description Helical; Name=4 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI10

14) chain C
residue 153-173
type TRANSMEM
sequence AIMGVAFTWVMALACAAPPLA
description Helical; Name=4 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI10

15) chain D
residue 153-173
type TRANSMEM
sequence AIMGVAFTWVMALACAAPPLA
description Helical; Name=4 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI10

16) chain A
residue 203-224
type TRANSMEM
sequence FVIYMFVVHFTIPMIIIFFCYG
description Helical; Name=5 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI11

17) chain B
residue 203-224
type TRANSMEM
sequence FVIYMFVVHFTIPMIIIFFCYG
description Helical; Name=5 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI11

18) chain C
residue 203-224
type TRANSMEM
sequence FVIYMFVVHFTIPMIIIFFCYG
description Helical; Name=5 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI11

19) chain D
residue 203-224
type TRANSMEM
sequence FVIYMFVVHFTIPMIIIFFCYG
description Helical; Name=5 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI11

20) chain A
residue 253-274
type TRANSMEM
sequence MVIIYVIAFLICWVPYASVAFY
description Helical; Name=6 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI12

21) chain B
residue 253-274
type TRANSMEM
sequence MVIIYVIAFLICWVPYASVAFY
description Helical; Name=6 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI12

22) chain C
residue 253-274
type TRANSMEM
sequence MVIIYVIAFLICWVPYASVAFY
description Helical; Name=6 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI12

23) chain D
residue 253-274
type TRANSMEM
sequence MVIIYVIAFLICWVPYASVAFY
description Helical; Name=6 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI12

24) chain A
residue 285-309
type TRANSMEM
sequence PIFMTIPAFFAKSAAIYNPVIYIMM
description Helical; Name=7 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI13

25) chain B
residue 285-309
type TRANSMEM
sequence PIFMTIPAFFAKSAAIYNPVIYIMM
description Helical; Name=7 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI13

26) chain C
residue 285-309
type TRANSMEM
sequence PIFMTIPAFFAKSAAIYNPVIYIMM
description Helical; Name=7 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI13

27) chain D
residue 285-309
type TRANSMEM
sequence PIFMTIPAFFAKSAAIYNPVIYIMM
description Helical; Name=7 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI13

28) chain A
residue 201
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI14

29) chain A
residue 279
type BINDING
sequence Q
description BINDING => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI14

30) chain B
residue 201
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI14

31) chain B
residue 279
type BINDING
sequence Q
description BINDING => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI14

32) chain C
residue 201
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI14

33) chain C
residue 279
type BINDING
sequence Q
description BINDING => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI14

34) chain D
residue 201
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI14

35) chain D
residue 279
type BINDING
sequence Q
description BINDING => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI14

36) chain A
residue 113
type SITE
sequence Q
description Plays an important role in the conformation switch to the active conformation => ECO:0000269|PubMed:26200343
source Swiss-Prot : SWS_FT_FI15

37) chain B
residue 113
type SITE
sequence Q
description Plays an important role in the conformation switch to the active conformation => ECO:0000269|PubMed:26200343
source Swiss-Prot : SWS_FT_FI15

38) chain C
residue 113
type SITE
sequence Q
description Plays an important role in the conformation switch to the active conformation => ECO:0000269|PubMed:26200343
source Swiss-Prot : SWS_FT_FI15

39) chain D
residue 113
type SITE
sequence Q
description Plays an important role in the conformation switch to the active conformation => ECO:0000269|PubMed:26200343
source Swiss-Prot : SWS_FT_FI15

40) chain A
residue 1
type MOD_RES
sequence M
description N-acetylmethionine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI16

41) chain B
residue 1
type MOD_RES
sequence M
description N-acetylmethionine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI16

42) chain C
residue 1
type MOD_RES
sequence M
description N-acetylmethionine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI16

43) chain D
residue 1
type MOD_RES
sequence M
description N-acetylmethionine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI16

44) chain A
residue 296
type MOD_RES
sequence K
description N6-(retinylidene)lysine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI17

45) chain B
residue 296
type MOD_RES
sequence K
description N6-(retinylidene)lysine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI17

46) chain C
residue 296
type MOD_RES
sequence K
description N6-(retinylidene)lysine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI17

47) chain D
residue 296
type MOD_RES
sequence K
description N6-(retinylidene)lysine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI17

48) chain A
residue -141
type ACT_SITE
sequence D
description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI2

49) chain D
residue -141
type ACT_SITE
sequence D
description Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04110, ECO:0000269|PubMed:1892846, ECO:0000269|PubMed:3382407, ECO:0000269|PubMed:7831309, ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI2

50) chain A
residue 322
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI22

51) chain A
residue 323
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI22

52) chain B
residue 322
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI22

53) chain B
residue 323
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI22

54) chain C
residue 322
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI22

55) chain C
residue 323
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI22

56) chain D
residue 322
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI22

57) chain D
residue 323
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI22

58) chain A
residue 2
type CARBOHYD
sequence C
description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI23

59) chain B
residue 2
type CARBOHYD
sequence C
description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI23

60) chain C
residue 2
type CARBOHYD
sequence C
description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI23

61) chain D
residue 2
type CARBOHYD
sequence C
description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI23

62) chain A
residue 15
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI24

63) chain B
residue 15
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI24

64) chain C
residue 15
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI24

65) chain D
residue 15
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI24

66) chain A
residue 1231
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P15887
source Swiss-Prot : SWS_FT_FI25

67) chain B
residue 1231
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P15887
source Swiss-Prot : SWS_FT_FI25

68) chain C
residue 1231
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P15887
source Swiss-Prot : SWS_FT_FI25

69) chain D
residue 1231
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P15887
source Swiss-Prot : SWS_FT_FI25

70) chain A
residue -129
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI3

71) chain A
residue -57
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI3

72) chain C
residue -57
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI3

73) chain D
residue -129
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI3

74) chain D
residue -57
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI3

75) chain A
residue -44
type BINDING
sequence S
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI4

76) chain A
residue -29
type BINDING
sequence N
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI4

77) chain C
residue -44
type BINDING
sequence S
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI4

78) chain C
residue -29
type BINDING
sequence N
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI4

79) chain D
residue -44
type BINDING
sequence S
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI4

80) chain D
residue -29
type BINDING
sequence N
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI4

81) chain A
residue 1-36
type TOPO_DOM
sequence MCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQ
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI5

82) chain C
residue 97-110
type TOPO_DOM
sequence TSLHGYFVFGPTGC
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI5

83) chain C
residue 174-202
type TOPO_DOM
sequence GWSRYIPEGLQCSCGIDYYTLKPEVNNES
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI5

84) chain C
residue 275-284
type TOPO_DOM
sequence IFTHQGSCFG
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI5

85) chain D
residue 1-36
type TOPO_DOM
sequence MCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQ
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI5

86) chain D
residue 97-110
type TOPO_DOM
sequence TSLHGYFVFGPTGC
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI5

87) chain D
residue 174-202
type TOPO_DOM
sequence GWSRYIPEGLQCSCGIDYYTLKPEVNNES
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI5

88) chain D
residue 275-284
type TOPO_DOM
sequence IFTHQGSCFG
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI5

89) chain A
residue 97-110
type TOPO_DOM
sequence TSLHGYFVFGPTGC
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI5

90) chain A
residue 174-202
type TOPO_DOM
sequence GWSRYIPEGLQCSCGIDYYTLKPEVNNES
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI5

91) chain A
residue 275-284
type TOPO_DOM
sequence IFTHQGSCFG
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI5

92) chain B
residue 1-36
type TOPO_DOM
sequence MCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQ
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI5

93) chain B
residue 97-110
type TOPO_DOM
sequence TSLHGYFVFGPTGC
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI5

94) chain B
residue 174-202
type TOPO_DOM
sequence GWSRYIPEGLQCSCGIDYYTLKPEVNNES
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI5

95) chain B
residue 275-284
type TOPO_DOM
sequence IFTHQGSCFG
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI5

96) chain C
residue 1-36
type TOPO_DOM
sequence MCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQ
description Extracellular => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI5

97) chain A
residue 37-61
type TRANSMEM
sequence FSMLAAYMFLLIVLGFPINFLTLYV
description Helical; Name=1 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI6

98) chain B
residue 37-61
type TRANSMEM
sequence FSMLAAYMFLLIVLGFPINFLTLYV
description Helical; Name=1 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI6

99) chain C
residue 37-61
type TRANSMEM
sequence FSMLAAYMFLLIVLGFPINFLTLYV
description Helical; Name=1 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI6

100) chain D
residue 37-61
type TRANSMEM
sequence FSMLAAYMFLLIVLGFPINFLTLYV
description Helical; Name=1 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI6

101) chain A
residue 62-73
type TOPO_DOM
sequence TVQHKKLRTPLN
description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI7

102) chain C
residue 134-152
type TOPO_DOM
sequence ERYVVVCKPMSNFRFGENH
description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI7

103) chain C
residue 225-252
type TOPO_DOM
sequence QLVFTVKEAAAQQQESATTQKAEKEVTR
description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI7

104) chain D
residue 62-73
type TOPO_DOM
sequence TVQHKKLRTPLN
description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI7

105) chain D
residue 134-152
type TOPO_DOM
sequence ERYVVVCKPMSNFRFGENH
description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI7

106) chain D
residue 225-252
type TOPO_DOM
sequence QLVFTVKEAAAQQQESATTQKAEKEVTR
description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI7

107) chain A
residue 134-152
type TOPO_DOM
sequence ERYVVVCKPMSNFRFGENH
description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI7

108) chain A
residue 225-252
type TOPO_DOM
sequence QLVFTVKEAAAQQQESATTQKAEKEVTR
description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI7

109) chain B
residue 62-73
type TOPO_DOM
sequence TVQHKKLRTPLN
description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI7

110) chain B
residue 134-152
type TOPO_DOM
sequence ERYVVVCKPMSNFRFGENH
description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI7

111) chain B
residue 225-252
type TOPO_DOM
sequence QLVFTVKEAAAQQQESATTQKAEKEVTR
description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI7

112) chain C
residue 62-73
type TOPO_DOM
sequence TVQHKKLRTPLN
description Cytoplasmic => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI7

113) chain A
residue 74-96
type TRANSMEM
sequence YILLNLAVADLFMVLGGFTSTLY
description Helical; Name=2 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI8

114) chain B
residue 74-96
type TRANSMEM
sequence YILLNLAVADLFMVLGGFTSTLY
description Helical; Name=2 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI8

115) chain C
residue 74-96
type TRANSMEM
sequence YILLNLAVADLFMVLGGFTSTLY
description Helical; Name=2 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI8

116) chain D
residue 74-96
type TRANSMEM
sequence YILLNLAVADLFMVLGGFTSTLY
description Helical; Name=2 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI8

117) chain A
residue 111-133
type TRANSMEM
sequence NLQGFFATLGGEIALWSLVVLAI
description Helical; Name=3 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI9

118) chain B
residue 111-133
type TRANSMEM
sequence NLQGFFATLGGEIALWSLVVLAI
description Helical; Name=3 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI9

119) chain C
residue 111-133
type TRANSMEM
sequence NLQGFFATLGGEIALWSLVVLAI
description Helical; Name=3 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI9

120) chain D
residue 111-133
type TRANSMEM
sequence NLQGFFATLGGEIALWSLVVLAI
description Helical; Name=3 => ECO:0000269|PubMed:26200343, ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI9


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