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P36575

- ARRC_HUMAN

UniProt

P36575 - ARRC_HUMAN

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Protein

Arrestin-C

Gene

ARR3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

GO - Biological processi

  1. endocytosis Source: Ensembl
  2. regulation of protein phosphorylation Source: Ensembl
  3. signal transduction Source: ProtInc
  4. visual perception Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Sensory transduction, Vision

Enzyme and pathway databases

SignaLinkiP36575.

Names & Taxonomyi

Protein namesi
Recommended name:
Arrestin-C
Alternative name(s):
Cone arrestin
Short name:
C-arrestin
Short name:
cArr
Retinal cone arrestin-3
X-arrestin
Gene namesi
Name:ARR3
Synonyms:ARRX, CAR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:710. ARR3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. photoreceptor inner segment Source: MGI
  3. photoreceptor outer segment Source: Ensembl
  4. synapse Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25004.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 388388Arrestin-CPRO_0000205203Add
BLAST

Proteomic databases

MaxQBiP36575.
PaxDbiP36575.
PRIDEiP36575.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP36575.
CleanExiHS_ARR3.
GenevestigatoriP36575.

Interactioni

Subunit structurei

Interacts with CXCR4; the interaction is dependent on the C-terminal phosphorylation of CXCR4 and modulates the calcium ion mobilization activity of CXCR4.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ZNF496Q96IT12EBI-718116,EBI-743906

Protein-protein interaction databases

BioGridi106900. 24 interactions.
IntActiP36575. 9 interactions.
MINTiMINT-1378211.
STRINGi9606.ENSP00000311538.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XEHmodel-A1-356[»]
2A34model-A1-388[»]
ProteinModelPortaliP36575.
SMRiP36575. Positions 2-371.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the arrestin family.Curated

Phylogenomic databases

eggNOGiNOG302111.
GeneTreeiENSGT00390000013152.
HOGENOMiHOG000231319.
HOVERGENiHBG002399.
InParanoidiP36575.
KOiK13801.
OMAiEIFWAGV.
OrthoDBiEOG79W954.
PhylomeDBiP36575.
TreeFamiTF314260.

Family and domain databases

Gene3Di2.60.40.640. 1 hit.
2.60.40.840. 1 hit.
InterProiIPR000698. Arrestin.
IPR011021. Arrestin-like_N.
IPR014752. Arrestin_C.
IPR011022. Arrestin_C-like.
IPR017864. Arrestin_CS.
IPR014753. Arrestin_N.
IPR014756. Ig_E-set.
[Graphical view]
PANTHERiPTHR11792. PTHR11792. 1 hit.
PfamiPF02752. Arrestin_C. 1 hit.
PF00339. Arrestin_N. 1 hit.
[Graphical view]
PRINTSiPR00309. ARRESTIN.
SMARTiSM01017. Arrestin_C. 1 hit.
[Graphical view]
SUPFAMiSSF81296. SSF81296. 2 hits.
PROSITEiPS00295. ARRESTINS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P36575-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSKVFKKTSS NGKLSIYLGK RDFVDHVDTV EPIDGVVLVD PEYLKCRKLF
60 70 80 90 100
VMLTCAFRYG RDDLEVIGLT FRKDLYVQTL QVVPAESSSP QGPLTVLQER
110 120 130 140 150
LLHKLGDNAY PFTLQMVTNL PCSVTLQPGP EDAGKPCGID FEVKSFCAEN
160 170 180 190 200
PEETVSKRDY VRLVVRKVQF APPEAGPGPS AQTIRRFLLS AQPLQLQAWM
210 220 230 240 250
DREVHYHGEP ISVNVSINNC TNKVIKKIKI SVDQITDVVL YSLDKYTKTV
260 270 280 290 300
FIQEFTETVA ANSSFSQSFA VTPILAASCQ KRGLALDGKL KHEDTNLASS
310 320 330 340 350
TIIRPGMDKE LLGILVSYKV RVNLMVSCGG ILGDLTASDV GVELPLVLIH
360 370 380
PKPSHEAASS EDIVIEEFTR KGEEESQKAV EAEGDEGS
Length:388
Mass (Da):42,778
Last modified:March 7, 2006 - v2
Checksum:i491F4EE4EE1ADA0D
GO
Isoform 2 (identifier: P36575-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:359
Mass (Da):39,667
Checksum:i3210415593EA6B38
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti19 – 191G → V in CAG33130. 1 PublicationCurated
Sequence conflicti93 – 931P → A no nucleotide entry (PubMed:8224247)Curated
Sequence conflicti93 – 931P → A in AAB84302. (PubMed:8612728)Curated
Sequence conflicti93 – 931P → A in AAC27524. (PubMed:8612728)Curated
Sequence conflicti217 – 2171I → V in AAC78395. (PubMed:8308033)Curated
Sequence conflicti356 – 3572EA → AS in CAI41490. (PubMed:15772651)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti44 – 441L → F.1 Publication
Corresponds to variant rs17855428 [ dbSNP | Ensembl ].
VAR_025520

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei359 – 38830SSEDI…GDEGS → R in isoform 2. 1 PublicationVSP_017495Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03626 mRNA. Translation: AAC78395.1.
AF033105 mRNA. Translation: AAB84302.1.
AF076512
, 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.
CCDSiCCDS14399.1. [P36575-1]
PIRiS38943.
RefSeqiNP_004303.2. NM_004312.2. [P36575-1]
UniGeneiHs.308.

Genome annotation databases

EnsembliENST00000307959; ENSP00000311538; ENSG00000120500. [P36575-1]
ENST00000374495; ENSP00000363619; ENSG00000120500. [P36575-2]
GeneIDi407.
KEGGihsa:407.
UCSCiuc004dya.3. human. [P36575-2]
uc004dyb.2. human. [P36575-1]

Polymorphism databases

DMDMi93189450.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03626 mRNA. Translation: AAC78395.1 .
AF033105 mRNA. Translation: AAB84302.1 .
AF076512
, 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 .
CCDSi CCDS14399.1. [P36575-1 ]
PIRi S38943.
RefSeqi NP_004303.2. NM_004312.2. [P36575-1 ]
UniGenei Hs.308.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1XEH model - A 1-356 [» ]
2A34 model - A 1-388 [» ]
ProteinModelPortali P36575.
SMRi P36575. Positions 2-371.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106900. 24 interactions.
IntActi P36575. 9 interactions.
MINTi MINT-1378211.
STRINGi 9606.ENSP00000311538.

Polymorphism databases

DMDMi 93189450.

Proteomic databases

MaxQBi P36575.
PaxDbi P36575.
PRIDEi P36575.

Protocols and materials databases

DNASUi 407.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000307959 ; ENSP00000311538 ; ENSG00000120500 . [P36575-1 ]
ENST00000374495 ; ENSP00000363619 ; ENSG00000120500 . [P36575-2 ]
GeneIDi 407.
KEGGi hsa:407.
UCSCi uc004dya.3. human. [P36575-2 ]
uc004dyb.2. human. [P36575-1 ]

Organism-specific databases

CTDi 407.
GeneCardsi GC0XP069488.
H-InvDB HIX0016849.
HGNCi HGNC:710. ARR3.
MIMi 301770. gene.
neXtProti NX_P36575.
PharmGKBi PA25004.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG302111.
GeneTreei ENSGT00390000013152.
HOGENOMi HOG000231319.
HOVERGENi HBG002399.
InParanoidi P36575.
KOi K13801.
OMAi EIFWAGV.
OrthoDBi EOG79W954.
PhylomeDBi P36575.
TreeFami TF314260.

Enzyme and pathway databases

SignaLinki P36575.

Miscellaneous databases

ChiTaRSi ARR3. human.
GeneWikii ARR3.
GenomeRNAii 407.
NextBioi 1709.
PROi P36575.
SOURCEi Search...

Gene expression databases

Bgeei P36575.
CleanExi HS_ARR3.
Genevestigatori P36575.

Family and domain databases

Gene3Di 2.60.40.640. 1 hit.
2.60.40.840. 1 hit.
InterProi IPR000698. Arrestin.
IPR011021. Arrestin-like_N.
IPR014752. Arrestin_C.
IPR011022. Arrestin_C-like.
IPR017864. Arrestin_CS.
IPR014753. Arrestin_N.
IPR014756. Ig_E-set.
[Graphical view ]
PANTHERi PTHR11792. PTHR11792. 1 hit.
Pfami PF02752. Arrestin_C. 1 hit.
PF00339. Arrestin_N. 1 hit.
[Graphical view ]
PRINTSi PR00309. ARRESTIN.
SMARTi SM01017. Arrestin_C. 1 hit.
[Graphical view ]
SUPFAMi SSF81296. SSF81296. 2 hits.
PROSITEi PS00295. ARRESTINS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiARRC_HUMAN
AccessioniPrimary (citable) accession number: P36575
Secondary accession number(s): B5B0B9
, Q5JT23, Q5JT24, Q6IBF5, Q96EN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: March 7, 2006
Last modified: November 26, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3