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SEM4A_HUMAN
ID   SEM4A_HUMAN             Reviewed;         761 AA.
AC   Q9H3S1; B2RDH8; B3KR76; Q5TCI5; Q5TCJ6; Q8WUA9;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   11-APR-2003, sequence version 2.
DT   03-AUG-2022, entry version 186.
DE   RecName: Full=Semaphorin-4A;
DE   AltName: Full=Semaphorin-B;
DE            Short=Sema B;
DE   Flags: Precursor;
GN   Name=SEMA4A; Synonyms=SEMAB, SEMB; ORFNames=UNQ783/PRO1317;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Miyajima N.,
RA   Saito T.;
RT   "Human semaphorin B.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Placenta, and Tongue;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon;
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   SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT GLN-713, AND
RP   CHARACTERIZATION OF VARIANTS RP35 HIS-345 AND CYS-350.
RX   PubMed=22956603; DOI=10.1167/iovs.11-9378;
RA   Tsuruma K., Nishimura Y., Kishi S., Shimazawa M., Tanaka T., Hara H.;
RT   "SEMA4A mutations lead to susceptibility to light irradiation, oxidative
RT   stress, and ER stress in retinal pigment epithelial cells.";
RL   Invest. Ophthalmol. Vis. Sci. 53:6729-6737(2012).
RN   [7]
RP   VARIANTS RP35 HIS-345 AND CYS-350, VARIANTS CORD10 HIS-345 AND CYS-350, AND
RP   VARIANT GLN-713.
RX   PubMed=16199541; DOI=10.1136/jmg.2005.035055;
RA   Abid A., Ismail M., Mehdi S.Q., Khaliq S.;
RT   "Identification of novel mutations in the SEMA4A gene associated with
RT   retinal degenerative diseases.";
RL   J. Med. Genet. 43:378-381(2006).
RN   [8]
RP   VARIANT GLN-713.
RX   PubMed=28805479; DOI=10.1080/13816810.2017.1354384;
RA   Bryant L., Lozynska O., Han G., Morgan J.I.W., Gai X., Maguire A.M.,
RA   Aleman T., Bennett J.;
RT   "On variants and disease-causing mutations: Case studies of a SEMA4A
RT   variant identified in inherited blindness.";
RL   Ophthalmic Genet. 39:144-146(2018).
CC   -!- FUNCTION: Cell surface receptor for PLXNB1, PLXNB2, PLXNB3 and PLXND1
CC       that plays an important role in cell-cell signaling (By similarity).
CC       Regulates glutamatergic and GABAergic synapse development (By
CC       similarity). Promotes the development of inhibitory synapses in a
CC       PLXNB1-dependent manner and promotes the development of excitatory
CC       synapses in a PLXNB2-dependent manner (By similarity). Plays a role in
CC       priming antigen-specific T-cells, promotes differentiation of Th1 T-
CC       helper cells, and thereby contributes to adaptive immunity (By
CC       similarity). Promotes phosphorylation of TIMD2 (By similarity).
CC       Inhibits angiogenesis (By similarity). Promotes axon growth cone
CC       collapse (By similarity). Inhibits axonal extension by providing local
CC       signals to specify territories inaccessible for growing axons (By
CC       similarity). {ECO:0000250|UniProtKB:Q62178}.
CC   -!- SUBUNIT: Interacts with PLXNB1, PLXNB2, PLXNB3, PLXND1 and TIMD2 (By
CC       similarity). {ECO:0000250|UniProtKB:Q62178}.
CC   -!- INTERACTION:
CC       Q9H3S1; Q9Y4D7: PLXND1; NbExp=2; IntAct=EBI-3924922, EBI-310731;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22956603};
CC       Single-pass type I membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9H3S1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9H3S1-2; Sequence=VSP_046381, VSP_046382;
CC   -!- DISEASE: Retinitis pigmentosa 35 (RP35) [MIM:610282]: A retinal
CC       dystrophy belonging to the group of pigmentary retinopathies. Retinitis
CC       pigmentosa is characterized by retinal pigment deposits visible on
CC       fundus examination and primary loss of rod photoreceptor cells followed
CC       by secondary loss of cone photoreceptors. Patients typically have night
CC       vision blindness and loss of midperipheral visual field. As their
CC       condition progresses, they lose their far peripheral visual field and
CC       eventually central vision as well. {ECO:0000269|PubMed:16199541,
CC       ECO:0000269|PubMed:22956603}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Cone-rod dystrophy 10 (CORD10) [MIM:610283]: An inherited
CC       retinal dystrophy characterized by retinal pigment deposits visible on
CC       fundus examination, predominantly in the macular region, and initial
CC       loss of cone photoreceptors followed by rod degeneration. This leads to
CC       decreased visual acuity and sensitivity in the central visual field,
CC       followed by loss of peripheral vision. Severe loss of vision occurs
CC       earlier than in retinitis pigmentosa, due to cone photoreceptors
CC       degenerating at a higher rate than rod photoreceptors.
CC       {ECO:0000269|PubMed:16199541}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the semaphorin family. {ECO:0000305}.
CC   -!- CAUTION: Variant Gln-713 was originally reported as mutation causing
CC       retinitis pigmentosa (PubMed:16199541). Subsequently, it has been shown
CC       to be a likely benign variant (PubMed:22956603, PubMed:28805479).
CC       {ECO:0000269|PubMed:16199541, ECO:0000269|PubMed:22956603,
CC       ECO:0000269|PubMed:28805479}.
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DR   EMBL; AB029394; BAB20087.1; -; mRNA.
DR   EMBL; AY358531; AAQ88895.1; -; mRNA.
DR   EMBL; AK091127; BAG52288.1; -; mRNA.
DR   EMBL; AK315547; BAG37925.1; -; mRNA.
DR   EMBL; AL135927; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC020974; AAH20974.1; -; mRNA.
DR   CCDS; CCDS1132.1; -. [Q9H3S1-1]
DR   CCDS; CCDS53378.1; -. [Q9H3S1-2]
DR   RefSeq; NP_001180229.1; NM_001193300.1. [Q9H3S1-1]
DR   RefSeq; NP_001180230.1; NM_001193301.1. [Q9H3S1-1]
DR   RefSeq; NP_001180231.1; NM_001193302.1. [Q9H3S1-2]
DR   RefSeq; NP_071762.2; NM_022367.3. [Q9H3S1-1]
DR   RefSeq; XP_011508174.1; XM_011509872.2. [Q9H3S1-1]
DR   RefSeq; XP_011508175.1; XM_011509873.2.
DR   RefSeq; XP_016857545.1; XM_017002056.1.
DR   AlphaFoldDB; Q9H3S1; -.
DR   SMR; Q9H3S1; -.
DR   BioGRID; 122108; 13.
DR   CORUM; Q9H3S1; -.
DR   IntAct; Q9H3S1; 5.
DR   MINT; Q9H3S1; -.
DR   STRING; 9606.ENSP00000357268; -.
DR   GlyGen; Q9H3S1; 4 sites.
DR   iPTMnet; Q9H3S1; -.
DR   PhosphoSitePlus; Q9H3S1; -.
DR   BioMuta; SEMA4A; -.
DR   DMDM; 29840871; -.
DR   EPD; Q9H3S1; -.
DR   jPOST; Q9H3S1; -.
DR   MassIVE; Q9H3S1; -.
DR   MaxQB; Q9H3S1; -.
DR   PaxDb; Q9H3S1; -.
DR   PeptideAtlas; Q9H3S1; -.
DR   PRIDE; Q9H3S1; -.
DR   ProteomicsDB; 64964; -.
DR   ProteomicsDB; 80746; -. [Q9H3S1-1]
DR   Antibodypedia; 20428; 350 antibodies from 33 providers.
DR   DNASU; 64218; -.
DR   Ensembl; ENST00000355014.6; ENSP00000347117.2; ENSG00000196189.14. [Q9H3S1-1]
DR   Ensembl; ENST00000368282.1; ENSP00000357265.1; ENSG00000196189.14. [Q9H3S1-1]
DR   Ensembl; ENST00000368284.5; ENSP00000357267.1; ENSG00000196189.14. [Q9H3S1-2]
DR   Ensembl; ENST00000368285.8; ENSP00000357268.3; ENSG00000196189.14. [Q9H3S1-1]
DR   GeneID; 64218; -.
DR   KEGG; hsa:64218; -.
DR   MANE-Select; ENST00000368285.8; ENSP00000357268.3; NM_022367.4; NP_071762.2.
DR   UCSC; uc001fnl.4; human. [Q9H3S1-1]
DR   CTD; 64218; -.
DR   DisGeNET; 64218; -.
DR   GeneCards; SEMA4A; -.
DR   GeneReviews; SEMA4A; -.
DR   HGNC; HGNC:10729; SEMA4A.
DR   HPA; ENSG00000196189; Tissue enhanced (epididymis).
DR   MalaCards; SEMA4A; -.
DR   MIM; 607292; gene.
DR   MIM; 610282; phenotype.
DR   MIM; 610283; phenotype.
DR   neXtProt; NX_Q9H3S1; -.
DR   OpenTargets; ENSG00000196189; -.
DR   Orphanet; 1872; Cone rod dystrophy.
DR   Orphanet; 440437; Familial colorectal cancer Type X.
DR   Orphanet; 791; Retinitis pigmentosa.
DR   PharmGKB; PA35651; -.
DR   VEuPathDB; HostDB:ENSG00000196189; -.
DR   eggNOG; KOG3611; Eukaryota.
DR   GeneTree; ENSGT00940000161509; -.
DR   InParanoid; Q9H3S1; -.
DR   OMA; KYYAGDG; -.
DR   OrthoDB; 64683at2759; -.
DR   PhylomeDB; Q9H3S1; -.
DR   TreeFam; TF316102; -.
DR   PathwayCommons; Q9H3S1; -.
DR   Reactome; R-HSA-416700; Other semaphorin interactions.
DR   SignaLink; Q9H3S1; -.
DR   BioGRID-ORCS; 64218; 7 hits in 1067 CRISPR screens.
DR   ChiTaRS; SEMA4A; human.
DR   GeneWiki; SEMA4A; -.
DR   GenomeRNAi; 64218; -.
DR   Pharos; Q9H3S1; Tbio.
DR   PRO; PR:Q9H3S1; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9H3S1; protein.
DR   Bgee; ENSG00000196189; Expressed in monocyte and 158 other tissues.
DR   ExpressionAtlas; Q9H3S1; baseline and differential.
DR   Genevisible; Q9H3S1; HS.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0045499; F:chemorepellent activity; IBA:GO_Central.
DR   GO; GO:0030215; F:semaphorin receptor binding; IBA:GO_Central.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR   GO; GO:0050919; P:negative chemotaxis; IBA:GO_Central.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0048843; P:negative regulation of axon extension involved in axon guidance; IBA:GO_Central.
DR   GO; GO:0001755; P:neural crest cell migration; IBA:GO_Central.
DR   GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR   GO; GO:1904891; P:positive regulation of excitatory synapse assembly; ISS:UniProtKB.
DR   GO; GO:1905704; P:positive regulation of inhibitory synapse assembly; ISS:UniProtKB.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR   GO; GO:0010594; P:regulation of endothelial cell migration; IEA:Ensembl.
DR   GO; GO:0071526; P:semaphorin-plexin signaling pathway; IBA:GO_Central.
DR   GO; GO:0045063; P:T-helper 1 cell differentiation; IEA:Ensembl.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR002165; Plexin_repeat.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR001627; Semap_dom.
DR   InterPro; IPR036352; Semap_dom_sf.
DR   InterPro; IPR027231; Semaphorin.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR11036; PTHR11036; 1.
DR   Pfam; PF01437; PSI; 1.
DR   Pfam; PF01403; Sema; 1.
DR   SMART; SM00423; PSI; 1.
DR   SMART; SM00630; Sema; 1.
DR   SUPFAM; SSF101912; SSF101912; 1.
DR   PROSITE; PS51004; SEMA; 1.
PE   1: Evidence at protein level;
KW   Adaptive immunity; Alternative splicing; Angiogenesis; Cell membrane;
KW   Cone-rod dystrophy; Developmental protein; Differentiation;
KW   Disease variant; Disulfide bond; Glycoprotein; Immunity;
KW   Immunoglobulin domain; Membrane; Neurogenesis; Reference proteome;
KW   Retinitis pigmentosa; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..761
FT                   /note="Semaphorin-4A"
FT                   /id="PRO_0000032322"
FT   TOPO_DOM        33..683
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        684..704
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        705..761
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          36..494
FT                   /note="Sema"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DOMAIN          496..548
FT                   /note="PSI"
FT   DOMAIN          573..631
FT                   /note="Ig-like C2-type"
FT   REGION          722..749
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        135
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        496
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        607
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        113..124
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        142..151
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        269..379
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        293..339
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        497..514
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        506..523
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   DISULFID        580..624
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT   VAR_SEQ         1..99
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046381"
FT   VAR_SEQ         122..154
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_046382"
FT   VARIANT         345
FT                   /note="D -> H (in RP35 and CORD10; heterozygous compound
FT                   with C-350; loss of localization to cell membrane;
FT                   dbSNP:rs267607033)"
FT                   /evidence="ECO:0000269|PubMed:16199541,
FT                   ECO:0000269|PubMed:22956603"
FT                   /id="VAR_028322"
FT   VARIANT         350
FT                   /note="F -> C (in RP35 and CORD10; heterozygous compound
FT                   with H-345; loss of localization to cell membrane;
FT                   dbSNP:rs267607034)"
FT                   /evidence="ECO:0000269|PubMed:16199541,
FT                   ECO:0000269|PubMed:22956603"
FT                   /id="VAR_028323"
FT   VARIANT         510
FT                   /note="R -> Q (in dbSNP:rs2075164)"
FT                   /id="VAR_028324"
FT   VARIANT         713
FT                   /note="R -> Q (originally reported as mutation causing
FT                   retinitis pigmentosa; no effect on localization to cell
FT                   membrane; dbSNP:rs41265017)"
FT                   /evidence="ECO:0000269|PubMed:16199541,
FT                   ECO:0000269|PubMed:22956603, ECO:0000269|PubMed:28805479"
FT                   /id="VAR_028325"
FT   CONFLICT        293..328
FT                   /note="CTQPGQLPFNVIRHAVLLPADSPTAPHIYAVFTSQW -> SAPSRGSCPSTS
FT                   SATRSCSPPILPQLPTSTQSSPPSG (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        354
FT                   /note="Y -> F (in Ref. 1; BAB20087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        641
FT                   /note="D -> G (in Ref. 3; BAG52288)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   761 AA;  83574 MW;  5BCB889AA32A2BB3 CRC64;
     MALPALGLDP WSLLGLFLFQ LLQLLLPTTT AGGGGQGPMP RVRYYAGDER RALSFFHQKG
     LQDFDTLLLS GDGNTLYVGA REAILALDIQ DPGVPRLKNM IPWPASDRKK SECAFKKKSN
     ETQCFNFIRV LVSYNVTHLY TCGTFAFSPA CTFIELQDSY LLPISEDKVM EGKGQSPFDP
     AHKHTAVLVD GMLYSGTMNN FLGSEPILMR TLGSQPVLKT DNFLRWLHHD ASFVAAIPST
     QVVYFFFEET ASEFDFFERL HTSRVARVCK NDVGGEKLLQ KKWTTFLKAQ LLCTQPGQLP
     FNVIRHAVLL PADSPTAPHI YAVFTSQWQV GGTRSSAVCA FSLLDIERVF KGKYKELNKE
     TSRWTTYRGP ETNPRPGSCS VGPSSDKALT FMKDHFLMDE QVVGTPLLVK SGVEYTRLAV
     ETAQGLDGHS HLVMYLGTTT GSLHKAVVSG DSSAHLVEEI QLFPDPEPVR NLQLAPTQGA
     VFVGFSGGVW RVPRANCSVY ESCVDCVLAR DPHCAWDPES RTCCLLSAPN LNSWKQDMER
     GNPEWACASG PMSRSLRPQS RPQIIKEVLA VPNSILELPC PHLSALASYY WSHGPAAVPE
     ASSTVYNGSL LLIVQDGVGG LYQCWATENG FSYPVISYWV DSQDQTLALD PELAGIPREH
     VKVPLTRVSG GAALAAQQSY WPHFVTVTVL FALVLSGALI ILVASPLRAL RARGKVQGCE
     TLRPGEKAPL SREQHLQSPK ECRTSASDVD ADNNCLGTEV A
 
 
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