OPSD_MOUSE
ID OPSD_MOUSE Reviewed; 348 AA.
AC P15409; Q8K0D8; Q96DZ2;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Rhodopsin;
GN Name=Rho;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2844600; DOI=10.1016/0014-5793(88)80490-3;
RA Baehr W., Falk J.D., Bugra K., Triantafyllos J.T., McGinnis J.F.;
RT "Isolation and analysis of the mouse opsin gene.";
RL FEBS Lett. 238:253-256(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1978723; DOI=10.1016/s0021-9258(17)30539-2;
RA Al-Ubaidi M.R., Pittler S.J., Champagne M.S., Triantafyllos J.T.,
RA McGinnis J.F., Baehr W.;
RT "Mouse opsin. Gene structure and molecular basis of multiple transcripts.";
RL J. Biol. Chem. 265:20563-20569(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9020854; DOI=10.1038/ng0297-216;
RA Humphries M.M., Rancourt D., Farrar G.J., Kenna P., Hazel M., Bush R.A.,
RA Sieving P.A., Sheils D.M., McNally N., Creighton P., Erven A., Boros A.,
RA Gulya K., Capecchi M.R., Humphries P.;
RT "Retinopathy induced in mice by targeted disruption of the rhodopsin
RT gene.";
RL Nat. Genet. 15:216-219(1997).
RN [7]
RP PHOSPHORYLATION AT SER-334; SER-338 AND SER-343, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=11910029; DOI=10.1110/ps.3870102;
RA Lee K.A., Craven K.B., Niemi G.A., Hurley J.B.;
RT "Mass spectrometric analysis of the kinetics of in vivo rhodopsin
RT phosphorylation.";
RL Protein Sci. 11:862-874(2002).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15961391; DOI=10.1074/jbc.m501789200;
RA Strissel K.J., Lishko P.V., Trieu L.H., Kennedy M.J., Hurley J.B.,
RA Arshavsky V.Y.;
RT "Recoverin undergoes light-dependent intracellular translocation in rod
RT photoreceptors.";
RL J. Biol. Chem. 280:29250-29255(2005).
RN [9]
RP INTERACTION WITH PRCD.
RX PubMed=27509380; DOI=10.1021/acs.biochem.6b00489;
RA Spencer W.J., Pearring J.N., Salinas R.Y., Loiselle D.R., Skiba N.P.,
RA Arshavsky V.Y.;
RT "Progressive Rod-Cone Degeneration (PRCD) Protein Requires N-Terminal S-
RT Acylation and Rhodopsin Binding for Photoreceptor Outer Segment
RT Localization and Maintaining Intracellular Stability.";
RL Biochemistry 55:5028-5037(2016).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=27353443; DOI=10.1085/jgp.201511538;
RA Frederiksen R., Nymark S., Kolesnikov A.V., Berry J.D., Adler L. IV,
RA Koutalos Y., Kefalov V.J., Cornwall M.C.;
RT "Rhodopsin kinase and arrestin binding control the decay of photoactivated
RT rhodopsin and dark adaptation of mouse rods.";
RL J. Gen. Physiol. 148:1-11(2016).
RN [11]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=28151698; DOI=10.1369/0022155416689675;
RA Zalis M.C., Johansson S., Englund-Johansson U.;
RT "Immunocytochemical Profiling of Cultured Mouse Primary Retinal Cells.";
RL J. Histochem. Cytochem. 65:223-239(2017).
RN [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=32312889; DOI=10.26508/lsa.201900618;
RA Ozaki E., Gibbons L., Neto N.G., Kenna P., Carty M., Humphries M.,
RA Humphries P., Campbell M., Monaghan M., Bowie A., Doyle S.L.;
RT "SARM1 deficiency promotes rod and cone photoreceptor cell survival in a
RT model of retinal degeneration.";
RL Life. Sci Alliance 3:0-0(2020).
CC -!- FUNCTION: Photoreceptor required for image-forming vision at low light
CC intensity. Required for photoreceptor cell viability after birth
CC (PubMed:9020854). Light-induced isomerization of 11-cis to all-trans
CC retinal triggers a conformational change that activates signaling via
CC G-proteins. Subsequent receptor phosphorylation mediates displacement
CC of the bound G-protein alpha subunit by the arrestin SAG and terminates
CC signaling (PubMed:27353443). {ECO:0000269|PubMed:27353443,
CC ECO:0000269|PubMed:9020854}.
CC -!- SUBUNIT: Homodimer (By similarity). May form a complex composed of RHO,
CC GRK1 and RCVRN in a Ca(2+)-dependent manner; RCVRN prevents the
CC interaction between GRK1 and RHO (By similarity). Interacts with GRK1
CC (By similarity). Interacts (phosphorylated form) with SAG (By
CC similarity). Interacts with GNAT1 (By similarity). Interacts with
CC GNAT3. SAG and G-proteins compete for a common binding site (By
CC similarity). Interacts with PRCD; the interaction promotes PRCD
CC stability (PubMed:27509380). {ECO:0000250|UniProtKB:P02699,
CC ECO:0000250|UniProtKB:P08100, ECO:0000269|PubMed:27509380}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P02699}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:P02699}. Cell projection,
CC cilium, photoreceptor outer segment {ECO:0000269|PubMed:15961391,
CC ECO:0000269|PubMed:27353443, ECO:0000269|PubMed:28151698}.
CC Note=Synthesized in the inner segment (IS) of rod photoreceptor cells
CC before vectorial transport to disk membranes in the rod outer segment
CC (OS) photosensory cilia. {ECO:0000250|UniProtKB:P08100}.
CC -!- TISSUE SPECIFICITY: Rod-shaped photoreceptor cells in the retina (at
CC protein level). {ECO:0000269|PubMed:15961391,
CC ECO:0000269|PubMed:27353443}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the outer segment of retinal
CC photoreceptors at postnatal days 11 and 22.
CC {ECO:0000269|PubMed:28151698}.
CC -!- PTM: Phosphorylated on some or all of the serine and threonine residues
CC present in the C-terminal region. {ECO:0000269|PubMed:11910029}.
CC -!- PTM: Contains one covalently linked retinal chromophore. Upon light
CC absorption, the covalently bound 11-cis-retinal is converted to all-
CC trans-retinal. After hydrolysis of the Schiff base and release of the
CC covalently bound all-trans-retinal, active rhodopsin is regenerated by
CC binding of a fresh molecule of 11-cis-retinal.
CC {ECO:0000250|UniProtKB:P02699}.
CC -!- DISRUPTION PHENOTYPE: Mice show no response in electroretinograms at
CC low light intensity (PubMed:9020854). They fail to form rod outer
CC segments leading to degeneration of photoreceptor cells within 3 months
CC of birth (PubMed:9020854, PubMed:32312889).
CC {ECO:0000269|PubMed:32312889, ECO:0000269|PubMed:9020854}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. Opsin
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; M36699; AAA39861.1; -; Genomic_DNA.
DR EMBL; M36695; AAA39861.1; JOINED; Genomic_DNA.
DR EMBL; M36696; AAA39861.1; JOINED; Genomic_DNA.
DR EMBL; M36697; AAA39861.1; JOINED; Genomic_DNA.
DR EMBL; M36698; AAA39861.1; JOINED; Genomic_DNA.
DR EMBL; M55171; AAA63392.1; -; Genomic_DNA.
DR EMBL; AK044333; BAC31871.1; -; mRNA.
DR EMBL; AK044412; BAC31908.1; -; mRNA.
DR EMBL; CH466523; EDK99545.1; -; Genomic_DNA.
DR EMBL; BC013125; AAH13125.1; -; mRNA.
DR EMBL; BC031766; AAH31766.1; -; mRNA.
DR CCDS; CCDS20446.1; -.
DR PIR; A23665; A23665.
DR RefSeq; NP_663358.1; NM_145383.1.
DR AlphaFoldDB; P15409; -.
DR SMR; P15409; -.
DR IntAct; P15409; 3.
DR MINT; P15409; -.
DR STRING; 10090.ENSMUSP00000032471; -.
DR GlyGen; P15409; 2 sites.
DR iPTMnet; P15409; -.
DR PhosphoSitePlus; P15409; -.
DR SwissPalm; P15409; -.
DR MaxQB; P15409; -.
DR PaxDb; P15409; -.
DR PRIDE; P15409; -.
DR ProteomicsDB; 293847; -.
DR Antibodypedia; 17456; 527 antibodies from 38 providers.
DR DNASU; 212541; -.
DR Ensembl; ENSMUST00000032471; ENSMUSP00000032471; ENSMUSG00000030324.
DR GeneID; 212541; -.
DR KEGG; mmu:212541; -.
DR UCSC; uc009djk.1; mouse.
DR CTD; 6010; -.
DR MGI; MGI:97914; Rho.
DR VEuPathDB; HostDB:ENSMUSG00000030324; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01030000234549; -.
DR HOGENOM; CLU_009579_3_0_1; -.
DR InParanoid; P15409; -.
DR OMA; QYYLVNP; -.
DR OrthoDB; 940057at2759; -.
DR PhylomeDB; P15409; -.
DR TreeFam; TF324998; -.
DR Reactome; R-MMU-2453902; The canonical retinoid cycle in rods (twilight vision).
DR Reactome; R-MMU-2485179; Activation of the phototransduction cascade.
DR Reactome; R-MMU-2514859; Inactivation, recovery and regulation of the phototransduction cascade.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-419771; Opsins.
DR Reactome; R-MMU-5620916; VxPx cargo-targeting to cilium.
DR BioGRID-ORCS; 212541; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Rho; mouse.
DR PRO; PR:P15409; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; P15409; protein.
DR Bgee; ENSMUSG00000030324; Expressed in retinal neural layer and 55 other tissues.
DR ExpressionAtlas; P15409; baseline and differential.
DR Genevisible; P15409; MM.
DR GO; GO:0005911; C:cell-cell junction; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0097381; C:photoreceptor disc membrane; ISS:UniProtKB.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
DR GO; GO:0060342; C:photoreceptor inner segment membrane; ISS:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
DR GO; GO:0042622; C:photoreceptor outer segment membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0120200; C:rod photoreceptor outer segment; IDA:MGI.
DR GO; GO:0030867; C:rough endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:1990913; C:sperm head plasma membrane; IDA:MGI.
DR GO; GO:0097225; C:sperm midpiece; IDA:MGI.
DR GO; GO:0005502; F:11-cis retinal binding; ISS:UniProtKB.
DR GO; GO:0008020; F:G protein-coupled photoreceptor activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016918; F:retinal binding; ISO:MGI.
DR GO; GO:0030507; F:spectrin binding; ISO:MGI.
DR GO; GO:0016038; P:absorption of visible light; ISS:AgBase.
DR GO; GO:0071482; P:cellular response to light stimulus; IMP:MGI.
DR GO; GO:0009583; P:detection of light stimulus; IMP:MGI.
DR GO; GO:0050960; P:detection of temperature stimulus involved in thermoception; IGI:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0045494; P:photoreceptor cell maintenance; IMP:UniProtKB.
DR GO; GO:0007602; P:phototransduction; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0009585; P:red, far-red light phototransduction; ISO:MGI.
DR GO; GO:0009416; P:response to light stimulus; IMP:MGI.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0016056; P:rhodopsin mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0050953; P:sensory perception of light stimulus; IMP:MGI.
DR GO; GO:0043052; P:thermotaxis; IGI:MGI.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001760; Opsin.
DR InterPro; IPR027430; Retinal_BS.
DR InterPro; IPR000732; Rhodopsin.
DR InterPro; IPR019477; Rhodopsin_N.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF10413; Rhodopsin_N; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00238; OPSIN.
DR PRINTS; PR00579; RHODOPSIN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR PROSITE; PS00238; OPSIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell projection; Chromophore; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
KW Metal-binding; Palmitate; Phosphoprotein; Photoreceptor protein; Receptor;
KW Reference proteome; Retinal protein; Sensory transduction; Transducer;
KW Transmembrane; Transmembrane helix; Vision; Zinc.
FT CHAIN 1..348
FT /note="Rhodopsin"
FT /id="PRO_0000197687"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 37..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 62..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 74..96
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 97..110
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 111..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 134..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 153..173
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 174..202
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 203..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 225..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 253..274
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 275..286
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 287..308
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT TOPO_DOM 309..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 330..348
FT /note="Interaction with SAG"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOTIF 134..136
FT /note="'Ionic lock' involved in activated form
FT stabilization"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT SITE 113
FT /note="Plays an important role in the conformation switch
FT to the active conformation"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 296
FT /note="N6-(retinylidene)lysine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11910029"
FT MOD_RES 336
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02700"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11910029"
FT MOD_RES 340
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 342
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11910029"
FT LIPID 322
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT LIPID 323
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P02699"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 110..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 20
FT /note="V -> G (in Ref. 1; AAA39861 and 2; AAA63392)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 39070 MW; B336C04B699AFF75 CRC64;
MNGTEGPNFY VPFSNVTGVV RSPFEQPQYY LAEPWQFSML AAYMFLLIVL GFPINFLTLY
VTVQHKKLRT PLNYILLNLA VADLFMVFGG FTTTLYTSLH GYFVFGPTGC NLEGFFATLG
GEIALWSLVV LAIERYVVVC KPMSNFRFGE NHAIMGVVFT WIMALACAAP PLVGWSRYIP
EGMQCSCGID YYTLKPEVNN ESFVIYMFVV HFTIPMIVIF FCYGQLVFTV KEAAAQQQES
ATTQKAEKEV TRMVIIMVIF FLICWLPYAS VAFYIFTHQG SNFGPIFMTL PAFFAKSSSI
YNPVIYIMLN KQFRNCMLTT LCCGKNPLGD DDASATASKT ETSQVAPA
