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ARRC_PIG
ID   ARRC_PIG                Reviewed;         391 AA.
AC   Q7YS78;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Arrestin-C;
DE   AltName: Full=Cone arrestin;
DE            Short=cArr;
DE   AltName: Full=Retinal cone arrestin-3;
GN   Name=ARR3;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RX   PubMed=15623797; DOI=10.1167/iovs.04-0695;
RA   Balse E., Tessier L.H., Fuchs C., Forster V., Sahel J.A., Picaud S.;
RT   "Purification of mammalian cone photoreceptors by lectin panning and the
RT   enhancement of their survival in glia-conditioned medium.";
RL   Invest. Ophthalmol. Vis. Sci. 46:367-374(2005).
CC   -!- FUNCTION: May play a role in an as yet undefined retina-specific signal
CC       transduction. Could bind to photoactivated-phosphorylated red/green
CC       opsins (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked in response to retinal
CC       illumination (By similarity). Interacts with CXCR4; the interaction is
CC       dependent on the C-terminal phosphorylation of CXCR4 and modulates the
CC       calcium ion mobilization activity of CXCR4 (By similarity).
CC       {ECO:0000250|UniProtKB:P36575, ECO:0000250|UniProtKB:Q9N0H5}.
CC   -!- SUBCELLULAR LOCATION: Photoreceptor inner segment
CC       {ECO:0000250|UniProtKB:Q9EQP6}. Cell projection, cilium, photoreceptor
CC       outer segment {ECO:0000250|UniProtKB:Q9EQP6}.
CC   -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD92082.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ564496; CAD92082.1; ALT_INIT; mRNA.
DR   RefSeq; NP_999510.1; NM_214345.1.
DR   AlphaFoldDB; Q7YS78; -.
DR   SMR; Q7YS78; -.
DR   STRING; 9823.ENSSSCP00000013174; -.
DR   PaxDb; Q7YS78; -.
DR   PeptideAtlas; Q7YS78; -.
DR   PRIDE; Q7YS78; -.
DR   GeneID; 397622; -.
DR   KEGG; ssc:397622; -.
DR   CTD; 407; -.
DR   eggNOG; KOG3865; Eukaryota.
DR   HOGENOM; CLU_033484_1_1_1; -.
DR   InParanoid; Q7YS78; -.
DR   OrthoDB; 783081at2759; -.
DR   TreeFam; TF314260; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Genevisible; Q7YS78; SS.
DR   GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR   GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:Ensembl.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR   GO; GO:0002046; F:opsin binding; IEA:Ensembl.
DR   GO; GO:0051219; F:phosphoprotein binding; IEA:Ensembl.
DR   GO; GO:0002031; P:G protein-coupled receptor internalization; IBA:GO_Central.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0007601; P:visual perception; IBA:GO_Central.
DR   Gene3D; 2.60.40.640; -; 1.
DR   Gene3D; 2.60.40.840; -; 1.
DR   InterPro; IPR033042; ARR3.
DR   InterPro; IPR000698; Arrestin.
DR   InterPro; IPR014752; Arrestin-like_C.
DR   InterPro; IPR011021; Arrestin-like_N.
DR   InterPro; IPR011022; Arrestin_C-like.
DR   InterPro; IPR017864; Arrestin_CS.
DR   InterPro; IPR014753; Arrestin_N.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR11792; PTHR11792; 1.
DR   PANTHER; PTHR11792:SF19; PTHR11792:SF19; 1.
DR   Pfam; PF02752; Arrestin_C; 1.
DR   Pfam; PF00339; Arrestin_N; 1.
DR   PRINTS; PR00309; ARRESTIN.
DR   SMART; SM01017; Arrestin_C; 1.
DR   SUPFAM; SSF81296; SSF81296; 2.
DR   PROSITE; PS00295; ARRESTINS; 1.
PE   2: Evidence at transcript level;
KW   Cell projection; Disulfide bond; Reference proteome; Sensory transduction;
KW   Vision.
FT   CHAIN           1..391
FT                   /note="Arrestin-C"
FT                   /id="PRO_0000250487"
FT   REGION          369..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..383
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   391 AA;  43239 MW;  25A5EAAE37684A55 CRC64;
     MSRVFKKTCS NGKLSIYLGK RDFVDHVDMV EPIDGVVLVD PEYLKGRKMF VMLTCAFRYG
     HDDLDVIGLT FRKDLYVQVQ QVVPAEPTSP QVPLTVLQER LLHKLGDNAY PFNLQMVVNL
     PCSVTLQPGP DDTGKACGID FEVKSFCAEN LEEKVSKKDS VRLVIRKIQF APVEPGPGPW
     AQTVRRFLLS AQPLQLQAWM DREVHYHGKP ISVNVSINNS TNKVIKKIKI SVDQITDVVL
     YSLDKYTKTV FIQEFTETIA ANSTFSKSFE VTPLLADNCE KQGLALDGKL KHGDTNLASS
     TILRPGMDKE LLGILVSYKV RVNLMVSCGG ILGDLTASDV GVELPLILMH PKPSNEAASS
     EDIVIEEFAR QEPGGREESQ EALAAEGDEG S
 
 
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