eF-site ID 5w0p-ABCD
PDB Code 5w0p
Chain A, B, C, D

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Title Crystal structure of rhodopsin bound to visual arrestin determined by X-ray free electron laser
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
ICCGDDEASAXVXKTETSVIFKKVSRDKSVTIYLGKRDYV
DHVSQVEPVDGVVLVDPELVKGKKVYVTLTCAFRYGQEDI
DVMGLTFRRDLYFSRVQVYPPVGAMSVLTQLQESLLKKLG
DNTYPFLLTFPDYLPCSVMLQPAPQDVGKSCGVDFEVKAF
ASDITDPEEDKIPKKSSVRLLIRKVQHAPPEMGPQPSAEA
SWQFFMSDKPLNLSVSLSKEIYFHGEPIPVTVTVTNNTDK
VVKKIKVSVEQIANVVLYSSDYYVKPVASEETQEKVQPNS
TLTKTLVLVPLLANNRERRGIALDGKIKHEDTNLASSTII
KEGIDRTVMGILVSYHIKVKLTVSGFLGELTSSEVATEVP
FRLMHPQPE
B:  NIFEMLRIDEGVITKDEAEKLFNQDVDAAVRGILRNAKLK
PVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKR
WDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYMCGT
EGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQFSMLAAYM
FLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADL
FMVLGGFTSTLYTSLHGYFVFGPTGCNLQGFFATLGGEIA
LWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFTWVMA
LACAAPPLAGWSRYIPEGLQCSCGIDYYTLKPEVNNESFV
IYMFVVHFTIPMIIIFFCYGQLVFTVKEAAAQQQESATTQ
KAEKEVTRMVIIYVIAFLICWVPYASVAFYIFTHQGSCFG
PIFMTIPAFFAKSAAIYNPVIYIMMNKQFRNCMLTTICCG
DDEASAXVXKTETSVIFKKVSRDKSVTIYLGKRDYVDHVS
QVEPVDGVVLVDPELVKGKKVYVTLTCAFRYGQEDIDVMG
LTFRRDLYFSRVQVYPPVGAMSVLTQLQESLLKKLGDNTY
PFLLTFPDYLPCSVMLQPAPQDVGKSCGVDFEVKAFASDI
TDPEEDKIPKKSSVRLLIRKVQHAPPEMGPQPSAEASWQF
FMSDKPLNLSVSLSKEIYFHGEPIPVTVTVTNNTDKVVKK
IKVSVEQIANVVLYSSDYYVKPVASEETQEKVQPNSTLTK
TLVLVPLLANNRERRGIALDGKIKHEDTNLASSTIIKEGI
DRTVMGILVSYHIKVKLTVSGFLGELTSSEVATEVPFRLM
HPQP
C:  NIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNA
AKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRN
AKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRML
QQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAY
MCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEPWQFSML
AAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLA
VADLFMVLGGFTSTLYTSLHGYFVFGPTGCNLQGFFATLG
GEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVAFT
WVMALACAAPPLAGWSRYIPEGLQCSCGIDYYTLKPEVNN
ESFVIYMFVVHFTIPMIIIFFCYGQLVFTVKEAAAQQQES
ATTQKAEKEVTRMVIIYVIAFLICWVPYASVAFYIFTHQG
SCFGPIFMTIPAFFAKSAAIYNPVIYIMMNKQFRNCMLTT
ICCGGDDEASATVXKTETSHVIFKKVSRDKSVTIYLGKRD
YVDHVSQVEPVDGVVLVDPELVKGKKVYVTLTCAFRYGQE
DIDVMGLTFRRDLYFSRVQVYPPVGAMSVLTQLQESLLKK
LGDNTYPFLLTFPDYLPCSVMLQPAPQDVGKSCGVDFEVK
AFASDITDPEEDKIPKKSSVRLLIRKVQHAPPEMGPQPSA
EASWQFFMSDKPLNLSVSLSKEIYFHGEPIPVTVTVTNNT
DKVVKKIKVSVEQIANVVLYSSDYYVKPVASEETQEKVQP
NSTLTKTLVLVPLLANNRERRGIALDGKIKHEDTNLASST
IIKEGIDRTVMGILVSYHIKVKLTVSGFLGELTSSEVATE
VPFRLMHPQP
D:  RGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFT
NSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRT
GTWDAYMCGTEGPNFYVPFSNATGVVRSPFEYPQYYLAEP
WQFSMLAAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNY
ILLNLAVADLFMVLGGFTSTLYTSLHGYFVFGPTGCNLQG
FFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAI
MGVAFTWVMALACAAPPLAGWSRYIPEGLQCSCGIDYYTL
KPEVNNESFVIYMFVVHFTIPMIIIFFCYGQLVFTVKEAA
AQQQESATTQKAEKEVTRMVIIYVIAFLICWVPYASVAFY
IFTHQGSCFGPIFMTIPAFFAKSAAIYNPVIYIMMNKQFR
NCMLTTICCGDDEASATVXKTETSVIFKKVSRDKSVTIYL
GKRDYVDHVSQVEPVDGVVLVDPELVKGKKVYVTLTCAFR
YGQEDIDVMGLTFRRDLYFSRVQVYPPVGAMSVLTQLQES
LLKKLGDNTYPFLLTFPDYLPCSVMLQPAPQDVGKSCGVD
FEVKAFASDITDPEEDKIPKKSSVRLLIRKVQHAPPEMGP
QPSAEASWQFFMSDKPLNLSVSLSKEIYFHGEPIPVTVTV
TNNTDKVVKKIKVSVEQIANVVLYSSDYYVKPVASEETQE
KVQPNSTLTKTLVLVPLLANNRERRGIALDGKIKHEDTNL
ASSTIIKEGIDRTVMGILVSYHIKVKLTVSGFLGELTSSE
VATEVPFRLMHPQP
Description


Functional site
1) chain C
residue -150
type catalytic
sequence E
description 921
source MCSA : MCSA1
2) chain C
residue -141
type catalytic
sequence D
description 921
source MCSA : MCSA1
3) 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
4) chain C
residue 123-139
type prosite
sequence IALWSLVVLAIERYVVV
description G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. IALwSLVVLAIERYVvV
source prosite : PS00237
5) chain A
residue 290-306
type prosite
sequence IPAFFAKSAAIYNPVIY
description OPSIN Visual pigments (opsins) retinal binding site. IPaFfAKSAAiyNPviY
source prosite : PS00238
6) chain C
residue 290-306
type prosite
sequence IPAFFAKSAAIYNPVIY
description OPSIN Visual pigments (opsins) retinal binding site. IPaFfAKSAAiyNPviY
source prosite : PS00238
7) chain A
residue 2066-2084
type prosite
sequence FRYGQEDIDVMGLTFRRDL
description ARRESTINS Arrestins signature. FRYGqEDiDVMGLtFrRDL
source prosite : PS00295
8) chain C
residue 2066-2084
type prosite
sequence FRYGQEDIDVMGLTFRRDL
description ARRESTINS Arrestins signature. FRYGqEDiDVMGLtFrRDL
source prosite : PS00295
9) 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_FI1
10) 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_FI1
11) 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_FI1
12) 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_FI1
13) 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_FI1
14) 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_FI1
15) 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_FI1
16) 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_FI1
17) chain C
residue 201
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI10
18) chain C
residue 279
type BINDING
sequence Q
description BINDING => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI10
19) chain D
residue 201
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI10
20) chain D
residue 279
type BINDING
sequence Q
description BINDING => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI10
21) 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_FI11
22) 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_FI11
23) chain C
residue 1
type MOD_RES
sequence M
description N-acetylmethionine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI12
24) chain D
residue 1
type MOD_RES
sequence M
description N-acetylmethionine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI12
25) chain C
residue 296
type MOD_RES
sequence K
description N6-(retinylidene)lysine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI13
26) chain D
residue 296
type MOD_RES
sequence K
description N6-(retinylidene)lysine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI13
27) chain C
residue 334
type MOD_RES
sequence S
description Phosphoserine => ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI14
28) chain C
residue 338
type MOD_RES
sequence X
description Phosphoserine => ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI14
29) chain D
residue 334
type MOD_RES
sequence S
description Phosphoserine => ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI14
30) chain D
residue 338
type MOD_RES
sequence X
description Phosphoserine => ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI14
31) chain C
residue 336
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI15
32) chain D
residue 336
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI15
33) chain C
residue 340
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI16
34) chain C
residue 342
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI16
35) chain D
residue 340
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI16
36) chain D
residue 342
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI16
37) chain C
residue 343
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI17
38) chain D
residue 343
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI17
39) chain C
residue 322
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI18
40) chain C
residue 323
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI18
41) chain D
residue 322
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI18
42) chain D
residue 323
type LIPID
sequence C
description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI18
43) chain C
residue 2
type CARBOHYD
sequence C
description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI19
44) chain D
residue 2
type CARBOHYD
sequence C
description N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:P02699
source Swiss-Prot : SWS_FT_FI19
45) 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_FI2
46) 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_FI2
47) chain C
residue 15
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI20
48) chain D
residue 15
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:28753425
source Swiss-Prot : SWS_FT_FI20
49) chain C
residue 2231
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P15887
source Swiss-Prot : SWS_FT_FI21
50) chain D
residue 2231
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000250|UniProtKB:P15887
source Swiss-Prot : SWS_FT_FI21
51) 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_FI22
52) chain C
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_FI23
53) chain C
residue -129
type BINDING
sequence L
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI24
54) chain C
residue -57
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI24
55) chain D
residue -57
type BINDING
sequence F
description BINDING => ECO:0000269|PubMed:8266098
source Swiss-Prot : SWS_FT_FI24
56) chain C
residue -44
type BINDING
sequence S
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI25
57) chain C
residue -29
type BINDING
sequence N
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI25
58) chain D
residue -44
type BINDING
sequence S
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI25
59) chain D
residue -29
type BINDING
sequence N
description BINDING => ECO:0000303|PubMed:7831309
source Swiss-Prot : SWS_FT_FI25
60) 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_FI3
61) 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_FI3
62) 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_FI3
63) 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_FI3
64) 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_FI3
65) 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_FI3
66) 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_FI4
67) 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_FI4
68) 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_FI5
69) 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_FI5
70) 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_FI6
71) 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_FI6
72) 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_FI7
73) 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_FI7
74) 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_FI8
75) 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_FI8
76) 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_FI9
77) 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_FI9

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