ID   ARRC_HUMAN              Reviewed;         388 AA.
AC   P36575; B5B0B9; Q5JT23; Q5JT24; Q6IBF5; Q96EN2;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   09-DEC-2015, entry version 136.
DE   RecName: Full=Arrestin-C;
DE   AltName: Full=Cone arrestin;
DE            Short=C-arrestin;
DE            Short=cArr;
DE   AltName: Full=Retinal cone arrestin-3;
DE   AltName: Full=X-arrestin;
GN   Name=ARR3; Synonyms=ARRX, CAR;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Retina;
RX   PubMed=8224247; DOI=10.1016/0014-5793(93)81712-9;
RA   Murakami A., Yajima T., Sakuma H., McLaren M.J., Inana G.;
RT   "X-arrestin: a new retinal arrestin mapping to the X chromosome.";
RL   FEBS Lett. 334:203-209(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Retina;
RX   PubMed=8308033;
RA   Craft C.M., Whitmore D.H., Wiechmann A.F.;
RT   "Cone arrestin identified by targeting expression of a functional
RT   family.";
RL   J. Biol. Chem. 269:4613-4619(1994).
RN   [3]
RP   SEQUENCE REVISION.
RA   Craft C.M.;
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Retina;
RX   PubMed=8612728; DOI=10.1016/0014-5793(96)00163-9;
RA   Sakuma H., Inana G., Murakami A., Higashide T., McLaren M.J.;
RT   "Immunolocalization of X-arrestin in human cone photoreceptors.";
RL   FEBS Lett. 382:105-110(1996).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9931451; DOI=10.1016/S0378-1119(98)00510-1;
RA   Sakuma H., Murakami A., Fujimaki T., Inana G.;
RT   "Isolation and characterization of the human X-arrestin gene.";
RL   Gene 224:87-95(1998).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Eye;
RA   Kaighin V.A., Martin A.L., Aronstam R.S.;
RT   "Isolation of cDNA coding for human arrestin 3, retinal (X-arrestin)
RT   ARR3.";
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA   Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA   Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA   Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA   Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA   Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA   Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA   Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA   Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA   Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA   Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA   Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA   Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA   Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA   Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA   Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA   Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA   Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA   Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA   Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA   Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA   Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA   Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA   Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA   de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA   Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA   Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA   Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA   Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA   Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA   Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA   Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA   Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA   Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA   Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA   Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA   Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA   Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA   Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA   Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA   Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA   Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA   Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA   Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
RP   PHE-44.
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   INTERACTION WITH CXCR4.
RX   PubMed=20048153; DOI=10.1074/jbc.M109.091173;
RA   Busillo J.M., Armando S., Sengupta R., Meucci O., Bouvier M.,
RA   Benovic J.L.;
RT   "Site-specific phosphorylation of CXCR4 is dynamically regulated by
RT   multiple kinases and results in differential modulation of CXCR4
RT   signaling.";
RL   J. Biol. Chem. 285:7805-7817(2010).
CC   -!- FUNCTION: May play a role in an as yet undefined retina-specific
CC       signal transduction. Could binds to photoactivated-phosphorylated
CC       red/green opsins.
CC   -!- SUBUNIT: Interacts with CXCR4; the interaction is dependent on the
CC       C-terminal phosphorylation of CXCR4 and modulates the calcium ion
CC       mobilization activity of CXCR4. {ECO:0000269|PubMed:20048153}.
CC   -!- INTERACTION:
CC       O00444:PLK4; NbExp=3; IntAct=EBI-718116, EBI-746202;
CC       O43298:ZBTB43; NbExp=3; IntAct=EBI-718116, EBI-740718;
CC       Q96IT1:ZNF496; NbExp=5; IntAct=EBI-718116, EBI-743906;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P36575-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P36575-2; Sequence=VSP_017495;
CC   -!- TISSUE SPECIFICITY: Inner and outer segments, and the inner
CC       plexiform regions of the retina.
CC   -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR   EMBL; U03626; AAC78395.1; -; mRNA.
DR   EMBL; AF033105; AAB84302.1; -; mRNA.
DR   EMBL; AF076512; AAC27524.1; -; Genomic_DNA.
DR   EMBL; AF076497; AAC27524.1; JOINED; Genomic_DNA.
DR   EMBL; AF076498; AAC27524.1; JOINED; Genomic_DNA.
DR   EMBL; AF076499; AAC27524.1; JOINED; Genomic_DNA.
DR   EMBL; AF076500; AAC27524.1; JOINED; Genomic_DNA.
DR   EMBL; AF076501; AAC27524.1; JOINED; Genomic_DNA.
DR   EMBL; AF076502; AAC27524.1; JOINED; Genomic_DNA.
DR   EMBL; AF076503; AAC27524.1; JOINED; Genomic_DNA.
DR   EMBL; AF076504; AAC27524.1; JOINED; Genomic_DNA.
DR   EMBL; AF076505; AAC27524.1; JOINED; Genomic_DNA.
DR   EMBL; AF076506; AAC27524.1; JOINED; Genomic_DNA.
DR   EMBL; AF076507; AAC27524.1; JOINED; Genomic_DNA.
DR   EMBL; AF076508; AAC27524.1; JOINED; Genomic_DNA.
DR   EMBL; AF076509; AAC27524.1; JOINED; Genomic_DNA.
DR   EMBL; AF076510; AAC27524.1; JOINED; Genomic_DNA.
DR   EMBL; AF076511; AAC27524.1; JOINED; Genomic_DNA.
DR   EMBL; EU883571; ACG60645.1; -; mRNA.
DR   EMBL; CR456849; CAG33130.1; -; mRNA.
DR   EMBL; AL357752; CAI41490.1; -; Genomic_DNA.
DR   EMBL; AL357752; CAI41491.1; -; Genomic_DNA.
DR   EMBL; BC012096; AAH12096.1; -; mRNA.
DR   CCDS; CCDS14399.1; -. [P36575-1]
DR   PIR; S38943; S38943.
DR   RefSeq; NP_004303.2; NM_004312.2. [P36575-1]
DR   UniGene; Hs.308; -.
DR   PDB; 1XEH; Model; -; A=1-356.
DR   PDB; 2A34; Model; -; A=1-388.
DR   PDBsum; 1XEH; -.
DR   PDBsum; 2A34; -.
DR   ProteinModelPortal; P36575; -.
DR   SMR; P36575; 2-371.
DR   BioGrid; 106900; 23.
DR   IntAct; P36575; 11.
DR   MINT; MINT-1378211; -.
DR   STRING; 9606.ENSP00000311538; -.
DR   BioMuta; ARR3; -.
DR   DMDM; 93189450; -.
DR   MaxQB; P36575; -.
DR   PaxDb; P36575; -.
DR   PRIDE; P36575; -.
DR   DNASU; 407; -.
DR   Ensembl; ENST00000307959; ENSP00000311538; ENSG00000120500. [P36575-1]
DR   Ensembl; ENST00000374495; ENSP00000363619; ENSG00000120500. [P36575-2]
DR   GeneID; 407; -.
DR   KEGG; hsa:407; -.
DR   UCSC; uc004dya.3; human. [P36575-2]
DR   UCSC; uc004dyb.2; human. [P36575-1]
DR   CTD; 407; -.
DR   GeneCards; ARR3; -.
DR   H-InvDB; HIX0016849; -.
DR   HGNC; HGNC:710; ARR3.
DR   MIM; 301770; gene.
DR   neXtProt; NX_P36575; -.
DR   PharmGKB; PA25004; -.
DR   eggNOG; KOG3865; Eukaryota.
DR   eggNOG; ENOG410XR0F; LUCA.
DR   GeneTree; ENSGT00390000013152; -.
DR   HOGENOM; HOG000231319; -.
DR   HOVERGEN; HBG002399; -.
DR   InParanoid; P36575; -.
DR   KO; K13801; -.
DR   OrthoDB; EOG79W954; -.
DR   PhylomeDB; P36575; -.
DR   TreeFam; TF314260; -.
DR   SignaLink; P36575; -.
DR   ChiTaRS; ARR3; human.
DR   GeneWiki; ARR3; -.
DR   GenomeRNAi; 407; -.
DR   NextBio; 1709; -.
DR   PRO; PR:P36575; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   Bgee; P36575; -.
DR   CleanEx; HS_ARR3; -.
DR   ExpressionAtlas; P36575; baseline and differential.
DR   Genevisible; P36575; HS.
DR   GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR   GO; GO:0001917; C:photoreceptor inner segment; IDA:MGI.
DR   GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
DR   GO; GO:0045202; C:synapse; IEA:Ensembl.
DR   GO; GO:0006897; P:endocytosis; IEA:Ensembl.
DR   GO; GO:0001932; P:regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR   Gene3D; 2.60.40.640; -; 1.
DR   Gene3D; 2.60.40.840; -; 1.
DR   InterPro; IPR000698; Arrestin.
DR   InterPro; IPR011021; Arrestin-like_N.
DR   InterPro; IPR014752; Arrestin_C.
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   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   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Complete proteome; Polymorphism;
KW   Reference proteome; Sensory transduction; Vision.
FT   CHAIN         1    388       Arrestin-C.
FT                                /FTId=PRO_0000205203.
FT   VAR_SEQ     359    388       SSEDIVIEEFTRKGEEESQKAVEAEGDEGS -> R (in
FT                                isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_017495.
FT   VARIANT      44     44       L -> F (in dbSNP:rs17855428).
FT                                {ECO:0000269|PubMed:15489334}.
FT                                /FTId=VAR_025520.
FT   CONFLICT     19     19       G -> V (in Ref. 7; CAG33130).
FT                                {ECO:0000305}.
FT   CONFLICT     93     93       P -> A (in Ref. 1; no nucleotide entry
FT                                and 4; AAB84302/AAC27524). {ECO:0000305}.
FT   CONFLICT    217    217       I -> V (in Ref. 2; AAC78395).
FT                                {ECO:0000305}.
FT   CONFLICT    356    357       EA -> AS (in Ref. 8; CAI41490).
FT                                {ECO:0000305}.
SQ   SEQUENCE   388 AA;  42778 MW;  491F4EE4EE1ADA0D CRC64;
     MSKVFKKTSS NGKLSIYLGK RDFVDHVDTV EPIDGVVLVD PEYLKCRKLF VMLTCAFRYG
     RDDLEVIGLT FRKDLYVQTL QVVPAESSSP QGPLTVLQER LLHKLGDNAY PFTLQMVTNL
     PCSVTLQPGP EDAGKPCGID FEVKSFCAEN PEETVSKRDY VRLVVRKVQF APPEAGPGPS
     AQTIRRFLLS AQPLQLQAWM DREVHYHGEP ISVNVSINNC TNKVIKKIKI SVDQITDVVL
     YSLDKYTKTV FIQEFTETVA ANSSFSQSFA VTPILAASCQ KRGLALDGKL KHEDTNLASS
     TIIRPGMDKE LLGILVSYKV RVNLMVSCGG ILGDLTASDV GVELPLVLIH PKPSHEAASS
     EDIVIEEFTR KGEEESQKAV EAEGDEGS
//