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P36575 (ARRC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arrestin-C
Alternative name(s):
Cone arrestin
Short name=C-arrestin
Short name=cArr
Retinal cone arrestin-3
X-arrestin
Gene names
Name:ARR3
Synonyms:ARRX, CAR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in an as yet undefined retina-specific signal transduction. Could binds to photoactivated-phosphorylated red/green opsins.

Subunit structure

Interacts with CXCR4; the interaction is dependent on the C-terminal phosphorylation of CXCR4 and modulates the calcium ion mobilization activity of CXCR4. Ref.10

Tissue specificity

Inner and outer segments, and the inner plexiform regions of the retina.

Sequence similarities

Belongs to the arrestin family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ZNF496Q96IT12EBI-718116,EBI-743906

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P36575-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P36575-2)

The sequence of this isoform differs from the canonical sequence as follows:
     359-388: SSEDIVIEEFTRKGEEESQKAVEAEGDEGS → R

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 388388Arrestin-C
PRO_0000205203

Natural variations

Alternative sequence359 – 38830SSEDI…GDEGS → R in isoform 2.
VSP_017495
Natural variant441L → F. Ref.9
Corresponds to variant rs17855428 [ dbSNP | Ensembl ].
VAR_025520

Experimental info

Sequence conflict191G → V in CAG33130. Ref.7
Sequence conflict931P → A no nucleotide entry Ref.1
Sequence conflict931P → A in AAB84302. Ref.4
Sequence conflict931P → A in AAC27524. Ref.4
Sequence conflict2171I → V in AAC78395. Ref.2
Sequence conflict356 – 3572EA → AS in CAI41490. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 7, 2006. Version 2.
Checksum: 491F4EE4EE1ADA0D

FASTA38842,778
        10         20         30         40         50         60 
MSKVFKKTSS NGKLSIYLGK RDFVDHVDTV EPIDGVVLVD PEYLKCRKLF VMLTCAFRYG 

        70         80         90        100        110        120 
RDDLEVIGLT FRKDLYVQTL QVVPAESSSP QGPLTVLQER LLHKLGDNAY PFTLQMVTNL 

       130        140        150        160        170        180 
PCSVTLQPGP EDAGKPCGID FEVKSFCAEN PEETVSKRDY VRLVVRKVQF APPEAGPGPS 

       190        200        210        220        230        240 
AQTIRRFLLS AQPLQLQAWM DREVHYHGEP ISVNVSINNC TNKVIKKIKI SVDQITDVVL 

       250        260        270        280        290        300 
YSLDKYTKTV FIQEFTETVA ANSSFSQSFA VTPILAASCQ KRGLALDGKL KHEDTNLASS 

       310        320        330        340        350        360 
TIIRPGMDKE LLGILVSYKV RVNLMVSCGG ILGDLTASDV GVELPLVLIH PKPSHEAASS 

       370        380 
EDIVIEEFTR KGEEESQKAV EAEGDEGS 

« Hide

Isoform 2 [UniParc].

Checksum: 3210415593EA6B38
Show »

FASTA35939,667

References

« Hide 'large scale' references
[1]"X-arrestin: a new retinal arrestin mapping to the X chromosome."
Murakami A., Yajima T., Sakuma H., McLaren M.J., Inana G.
FEBS Lett. 334:203-209(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Retina.
[2]"Cone arrestin identified by targeting expression of a functional family."
Craft C.M., Whitmore D.H., Wiechmann A.F.
J. Biol. Chem. 269:4613-4619(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Retina.
[3]Craft C.M.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[4]"Immunolocalization of X-arrestin in human cone photoreceptors."
Sakuma H., Inana G., Murakami A., Higashide T., McLaren M.J.
FEBS Lett. 382:105-110(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Retina.
[5]"Isolation and characterization of the human X-arrestin gene."
Sakuma H., Murakami A., Fujimaki T., Inana G.
Gene 224:87-95(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Isolation of cDNA coding for human arrestin 3, retinal (X-arrestin) ARR3."
Kaighin V.A., Martin A.L., Aronstam R.S.
Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Eye.
[7]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT PHE-44.
Tissue: Eye.
[10]"Site-specific phosphorylation of CXCR4 is dynamically regulated by multiple kinases and results in differential modulation of CXCR4 signaling."
Busillo J.M., Armando S., Sengupta R., Meucci O., Bouvier M., Benovic J.L.
J. Biol. Chem. 285:7805-7817(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CXCR4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U03626 mRNA. Translation: AAC78395.1.
AF033105 mRNA. Translation: AAB84302.1.
AF076512 expand/collapse EMBL AC list , AF076497, AF076498, AF076499, AF076500, AF076501, AF076502, AF076503, AF076504, AF076505, AF076506, AF076507, AF076508, AF076509, AF076510, AF076511 Genomic DNA. Translation: AAC27524.1.
EU883571 mRNA. Translation: ACG60645.1.
CR456849 mRNA. Translation: CAG33130.1.
AL357752 Genomic DNA. Translation: CAI41490.1.
AL357752 Genomic DNA. Translation: CAI41491.1.
BC012096 mRNA. Translation: AAH12096.1.
PIRS38943.
RefSeqNP_004303.2. NM_004312.2.
UniGeneHs.308.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XEHmodel-A1-356[»]
2A34model-A1-388[»]
ProteinModelPortalP36575.
SMRP36575. Positions 2-371.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106900. 24 interactions.
IntActP36575. 9 interactions.
MINTMINT-1378211.
STRING9606.ENSP00000311538.

Polymorphism databases

DMDM93189450.

Proteomic databases

PaxDbP36575.
PRIDEP36575.

Protocols and materials databases

DNASU407.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307959; ENSP00000311538; ENSG00000120500. [P36575-1]
ENST00000374495; ENSP00000363619; ENSG00000120500. [P36575-2]
GeneID407.
KEGGhsa:407.
UCSCuc004dya.3. human. [P36575-2]
uc004dyb.2. human. [P36575-1]

Organism-specific databases

CTD407.
GeneCardsGC0XP069488.
H-InvDBHIX0016849.
HGNCHGNC:710. ARR3.
MIM301770. gene.
neXtProtNX_P36575.
PharmGKBPA25004.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG302111.
HOGENOMHOG000231319.
HOVERGENHBG002399.
InParanoidP36575.
KOK13801.
OMAEVKSFCA.
OrthoDBEOG79W954.
PhylomeDBP36575.
TreeFamTF314260.

Enzyme and pathway databases

SignaLinkP36575.

Gene expression databases

ArrayExpressP36575.
BgeeP36575.
CleanExHS_ARR3.
GenevestigatorP36575.

Family and domain databases

Gene3D2.60.40.640. 1 hit.
2.60.40.840. 1 hit.
InterProIPR000698. Arrestin.
IPR011021. Arrestin-like_N.
IPR014752. Arrestin_C.
IPR011022. Arrestin_C-like.
IPR017864. Arrestin_CS.
IPR014753. Arrestin_N.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERPTHR11792. PTHR11792. 1 hit.
PfamPF02752. Arrestin_C. 1 hit.
PF00339. Arrestin_N. 1 hit.
[Graphical view]
PRINTSPR00309. ARRESTIN.
SMARTSM01017. Arrestin_C. 1 hit.
[Graphical view]
SUPFAMSSF81296. SSF81296. 2 hits.
PROSITEPS00295. ARRESTINS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiARR3.
GenomeRNAi407.
NextBio1709.
PROP36575.
SOURCESearch...

Entry information

Entry nameARRC_HUMAN
AccessionPrimary (citable) accession number: P36575
Secondary accession number(s): B5B0B9 expand/collapse secondary AC list , Q5JT23, Q5JT24, Q6IBF5, Q96EN2
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: March 7, 2006
Last modified: March 19, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM