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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