ARRC_HUMAN
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 03-AUG-2022, entry version 178.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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; DOI=10.1016/s0021-9258(17)41820-5;
RA Craft C.M., Whitmore D.H., Wiechmann A.F.;
RT "Cone arrestin identified by targeting expression of a functional 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., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., 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., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., 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., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., 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., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., 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., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA 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 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 project:
RT 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., 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).
RN [11]
RP INVOLVEMENT IN MYP26, AND VARIANTS MYP26 PRO-80; 100-ARG--SER-388 DEL AND
RP ASP-298.
RX PubMed=27829781;
RA Xiao X., Li S., Jia X., Guo X., Zhang Q.;
RT "cause female-limited early onset high myopia.";
RL Mol. Vis. 22:1257-1266(2016).
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.
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 (PubMed:20048153).
CC {ECO:0000250|UniProtKB:Q9N0H5, ECO:0000269|PubMed:20048153}.
CC -!- INTERACTION:
CC P36575; O00444: PLK4; NbExp=3; IntAct=EBI-718116, EBI-746202;
CC P36575; O43298: ZBTB43; NbExp=3; IntAct=EBI-718116, EBI-740718;
CC P36575; Q96IT1: ZNF496; NbExp=6; IntAct=EBI-718116, EBI-743906;
CC P36575-2; Q5T0T0: MARCHF8; NbExp=3; IntAct=EBI-11977533, EBI-14061946;
CC P36575-2; Q96IT1: ZNF496; NbExp=3; IntAct=EBI-11977533, EBI-743906;
CC -!- SUBCELLULAR LOCATION: Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:Q9EQP6}. Cell projection, cilium, photoreceptor
CC outer segment {ECO:0000250|UniProtKB:Q9EQP6}.
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 plexiform
CC regions of the retina.
CC -!- DISEASE: Myopia 26, X-linked, female-limited (MYP26) [MIM:301010]: A
CC form of myopia, a refractive error of the eye, in which parallel rays
CC from a distant object come to focus in front of the retina, vision
CC being better for near objects than for far. MYP26 is characterized by
CC typical tigroid fundus changes commonly seen in early onset high
CC myopia, and an unusual pattern of X-linked female-limited inheritance.
CC {ECO:0000269|PubMed:27829781}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
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; -; NOT_ANNOTATED_CDS; 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 AlphaFoldDB; P36575; -.
DR SMR; P36575; -.
DR BioGRID; 106900; 12.
DR IntAct; P36575; 13.
DR MINT; P36575; -.
DR STRING; 9606.ENSP00000311538; -.
DR PhosphoSitePlus; P36575; -.
DR BioMuta; ARR3; -.
DR DMDM; 93189450; -.
DR EPD; P36575; -.
DR jPOST; P36575; -.
DR MassIVE; P36575; -.
DR MaxQB; P36575; -.
DR PaxDb; P36575; -.
DR PeptideAtlas; P36575; -.
DR PRIDE; P36575; -.
DR ProteomicsDB; 55214; -. [P36575-1]
DR ProteomicsDB; 55215; -. [P36575-2]
DR Antibodypedia; 27367; 243 antibodies from 33 providers.
DR DNASU; 407; -.
DR Ensembl; ENST00000307959.9; ENSP00000311538.8; ENSG00000120500.19. [P36575-1]
DR Ensembl; ENST00000374495.7; ENSP00000363619.3; ENSG00000120500.19. [P36575-2]
DR GeneID; 407; -.
DR KEGG; hsa:407; -.
DR MANE-Select; ENST00000307959.9; ENSP00000311538.8; NM_004312.3; NP_004303.2.
DR UCSC; uc004dya.4; human. [P36575-1]
DR CTD; 407; -.
DR DisGeNET; 407; -.
DR GeneCards; ARR3; -.
DR HGNC; HGNC:710; ARR3.
DR HPA; ENSG00000120500; Tissue enriched (retina).
DR MalaCards; ARR3; -.
DR MIM; 301010; phenotype.
DR MIM; 301770; gene.
DR neXtProt; NX_P36575; -.
DR OpenTargets; ENSG00000120500; -.
DR PharmGKB; PA25004; -.
DR VEuPathDB; HostDB:ENSG00000120500; -.
DR eggNOG; KOG3865; Eukaryota.
DR GeneTree; ENSGT00950000182887; -.
DR HOGENOM; CLU_033484_0_0_1; -.
DR InParanoid; P36575; -.
DR OMA; SMDREVH; -.
DR OrthoDB; 783081at2759; -.
DR PhylomeDB; P36575; -.
DR TreeFam; TF314260; -.
DR PathwayCommons; P36575; -.
DR SignaLink; P36575; -.
DR BioGRID-ORCS; 407; 8 hits in 690 CRISPR screens.
DR ChiTaRS; ARR3; human.
DR GeneWiki; ARR3; -.
DR GenomeRNAi; 407; -.
DR Pharos; P36575; Tbio.
DR PRO; PR:P36575; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P36575; protein.
DR Bgee; ENSG00000120500; Expressed in retina and 113 other tissues.
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: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; TAS:ProtInc.
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 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Disease variant; Disulfide bond;
KW Reference proteome; Sensory transduction; Vision.
FT CHAIN 1..388
FT /note="Arrestin-C"
FT /id="PRO_0000205203"
FT VAR_SEQ 359..388
FT /note="SSEDIVIEEFTRKGEEESQKAVEAEGDEGS -> R (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017495"
FT VARIANT 44
FT /note="L -> F (in dbSNP:rs11548182)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025520"
FT VARIANT 80
FT /note="L -> P (in MYP26; unknown pathological significance;
FT dbSNP:rs1555941116)"
FT /evidence="ECO:0000269|PubMed:27829781"
FT /id="VAR_080595"
FT VARIANT 100..388
FT /note="Missing (in MYP26; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:27829781"
FT /id="VAR_080596"
FT VARIANT 298
FT /note="A -> D (in MYP26; unknown pathological significance;
FT dbSNP:rs765658563)"
FT /evidence="ECO:0000269|PubMed:27829781"
FT /id="VAR_080597"
FT CONFLICT 19
FT /note="G -> V (in Ref. 7; CAG33130)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="P -> A (in Ref. 1; no nucleotide entry and 4;
FT AAB84302/AAC27524)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="I -> V (in Ref. 2; AAC78395)"
FT /evidence="ECO:0000305"
FT CONFLICT 356..357
FT /note="EA -> AS (in Ref. 8; AL357752)"
FT /evidence="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
