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Reviewed, UniProtKB/Swiss-Prot P36575 (ARRC_HUMAN)

Last modified November 3, 2009. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Tissue specificity

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

Sequence similarities

Belongs to the arrestin family.

Ontologies

Keywords
   Biological processSensory transduction
Vision
   Coding sequence diversityAlternative splicing
Polymorphism
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processresponse to stimulus

Inferred from electronic annotation. Source: UniProtKB-KW

signal transduction Ref.1

Traceable author statement. Source: ProtInc

visual perception Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentcytoplasm Ref.1

Traceable author statement. Source: ProtInc

soluble fraction Ref.1

Traceable author statement. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARRB1P494071EBI-718116,EBI-743313
ZNF496Q96IT11EBI-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: dbSNP rs17855428. Ref.9
VAR_025520

Experimental info

Sequence conflict191G → V in CAG33130. Ref.7
Sequence conflict931P → A Ref.1
Sequence conflict931P → A Ref.3
Sequence conflict931P → A Ref.4
Sequence conflict931P → A Ref.5
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.

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: 8224247] [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: 8308033] [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: 8612728] [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: 9931451] [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: 15772651] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT PHE-44.
Tissue: Eye.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
IPIIPI00003917.
IPI00644870.
PIRS38943.
RefSeqNP_004303.2.
UniGeneHs.308

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1XEHmodel-A1-356[»]
2A34model-A1-388[»]
SMRP36575. Positions 2-371.
ModBaseSearch...

Protein-protein interaction databases

IntActP36575. 9 interactions.
STRINGP36575.

Proteomic databases

PRIDEP36575.

Genome annotation databases

EnsemblENST00000307959; ENSP00000311538; ENSG00000120500; Homo sapiens. [Genome view]
ENST00000374480; ENSP00000363604; ENSG00000120500; Homo sapiens. [Genome view]
ENST00000374495; ENSP00000363619; ENSG00000120500; Homo sapiens. [Genome view]
GeneID407.
KEGGhsa:407.
NMPDRfig|9606.3.peg.32946.
UCSCuc004dya.2. human.
uc004dyb.2. human.

Organism-specific databases

CTD407.
GeneCardsGC0XP069404.
HGNCHGNC:710. ARR3.
MIM301770. gene.
PharmGKBPA25004.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP36575.
HOVERGENP36575.
OMAIVIEEFA.

Enzyme and pathway databases

Pathway_Interaction_DBtxa2pathway. Thromboxane A2 receptor signaling.
cone_pathway. Visual signal transduction: Cones.

Gene expression databases

ArrayExpressP36575.
BgeeP36575.
CleanExHS_ARR3.
GenevestigatorP36575.
GermOnlineENSG00000120500. Homo sapiens.

Family and domain databases

InterProIPR000698. Arrestin.
IPR011022. Arrestin-like_C.
IPR011021. Arrestin-like_N.
IPR014752. Arrestin_C.
IPR017864. Arrestin_CS.
IPR014753. Arrestin_N.
[Graphical view]
Gene3DG3DSA:2.60.40.640. Arrestin_C. 1 hit.
G3DSA:2.60.40.840. Arrestin_N. 1 hit.
PANTHERPTHR11792. Arrestin. 1 hit.
PfamPF02752. Arrestin_C. 1 hit.
PF00339. Arrestin_N. 1 hit.
[Graphical view]
PRINTSPR00309. ARRESTIN.
ProDomPD002099. Arrestin. 2 hits.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00295. ARRESTINS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio1709.
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: November 3, 2009
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome X

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents