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Protein

Recoverin

Gene

RCVRN

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

Functioni

Seems to be implicated in the pathway from retinal rod guanylate cyclase to rhodopsin. May be involved in the inhibition of the phosphorylation of rhodopsin in a calcium-dependent manner. The calcium-bound recoverin prolongs the photoresponse.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi74 – 85121; low affinityPROSITE-ProRule annotationAdd
BLAST
Calcium bindingi110 – 121122; high affinityPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • calcium ion binding Source: ProtInc
  • calcium sensitive guanylate cyclase activator activity Source: ProtInc

GO - Biological processi

  • phototransduction, visible light Source: Reactome
  • positive regulation of guanylate cyclase activity Source: GOC
  • regulation of calcium ion transport Source: Ensembl
  • regulation of rhodopsin mediated signaling pathway Source: Reactome
  • rhodopsin mediated signaling pathway Source: Reactome
  • signal transduction Source: ProtInc
  • visual perception Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
SignaLinkiP35243.

Names & Taxonomyi

Protein namesi
Recommended name:
Recoverin
Alternative name(s):
Cancer-associated retinopathy protein
Short name:
Protein CAR
Gene namesi
Name:RCVRN
Synonyms:RCV1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:9937. RCVRN.

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162400987.

Polymorphism and mutation databases

BioMutaiRCVRN.
DMDMi464600.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 200199RecoverinPRO_0000073759Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity

Keywords - PTMi

Lipoprotein, Myristate

Proteomic databases

PaxDbiP35243.
PRIDEiP35243.

PTM databases

PhosphoSiteiP35243.

Expressioni

Tissue specificityi

Retina and pineal gland.

Gene expression databases

BgeeiP35243.
CleanExiHS_RCVRN.
GenevisibleiP35243. HS.

Interactioni

Protein-protein interaction databases

BioGridi111890. 14 interactions.
IntActiP35243. 5 interactions.
MINTiMINT-2862634.
STRINGi9606.ENSP00000226193.

Structurei

Secondary structure

1
200
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2010Combined sources
Helixi25 – 3814Combined sources
Beta strandi42 – 454Combined sources
Helixi46 – 5510Combined sources
Helixi63 – 7311Combined sources
Beta strandi79 – 824Combined sources
Helixi83 – 9311Combined sources
Beta strandi96 – 994Combined sources
Helixi102 – 1098Combined sources
Beta strandi114 – 1174Combined sources
Helixi119 – 13214Combined sources
Helixi135 – 1395Combined sources
Turni143 – 1453Combined sources
Helixi148 – 15811Combined sources
Helixi169 – 17810Combined sources
Helixi180 – 1867Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D8NX-ray2.20A1-200[»]
ProteinModelPortaliP35243.
SMRiP35243. Positions 1-197.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35243.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 6036EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini61 – 9636EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini97 – 13236EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini147 – 18236EF-hand 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the recoverin family.Curated
Contains 4 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0044. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000118820.
HOGENOMiHOG000233019.
HOVERGENiHBG108179.
InParanoidiP35243.
KOiK13764.
OMAiKECPSGR.
OrthoDBiEOG7GJ6F3.
PhylomeDBiP35243.
TreeFamiTF300009.

Family and domain databases

Gene3Di1.10.238.10. 3 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR028846. Recoverin.
[Graphical view]
PANTHERiPTHR23055. PTHR23055. 1 hit.
PfamiPF13499. EF-hand_7. 1 hit.
PF13833. EF-hand_8. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35243-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNSKSGALS KEILEELQLN TKFSEEELCS WYQSFLKDCP TGRITQQQFQ
60 70 80 90 100
SIYAKFFPDT DPKAYAQHVF RSFDSNLDGT LDFKEYVIAL HMTTAGKTNQ
110 120 130 140 150
KLEWAFSLYD VDGNGTISKN EVLEIVMAIF KMITPEDVKL LPDDENTPEK
160 170 180 190 200
RAEKIWKYFG KNDDDKLTEK EFIEGTLANK EILRLIQFEP QKVKEKMKNA
Length:200
Mass (Da):23,130
Last modified:January 23, 2007 - v2
Checksum:i7B1FA91EF19E6122
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S43855 mRNA. Translation: AAB23163.1.
S45545 mRNA. Translation: AAB23392.1.
S62028 mRNA. Translation: AAB26894.1.
AB001838 mRNA. Translation: BAA19460.1.
BT009838 mRNA. Translation: AAP88840.1.
AK314129 mRNA. Translation: BAG36819.1.
AB593156 mRNA. Translation: BAJ84088.1.
CH471108 Genomic DNA. Translation: EAW90014.1.
BC001720 mRNA. Translation: AAH01720.1.
CCDSiCCDS11151.1.
PIRiJC1227.
RefSeqiNP_002894.1. NM_002903.2.
UniGeneiHs.80539.

Genome annotation databases

EnsembliENST00000226193; ENSP00000226193; ENSG00000109047.
GeneIDi5957.
KEGGihsa:5957.
UCSCiuc002gme.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S43855 mRNA. Translation: AAB23163.1.
S45545 mRNA. Translation: AAB23392.1.
S62028 mRNA. Translation: AAB26894.1.
AB001838 mRNA. Translation: BAA19460.1.
BT009838 mRNA. Translation: AAP88840.1.
AK314129 mRNA. Translation: BAG36819.1.
AB593156 mRNA. Translation: BAJ84088.1.
CH471108 Genomic DNA. Translation: EAW90014.1.
BC001720 mRNA. Translation: AAH01720.1.
CCDSiCCDS11151.1.
PIRiJC1227.
RefSeqiNP_002894.1. NM_002903.2.
UniGeneiHs.80539.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D8NX-ray2.20A1-200[»]
ProteinModelPortaliP35243.
SMRiP35243. Positions 1-197.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111890. 14 interactions.
IntActiP35243. 5 interactions.
MINTiMINT-2862634.
STRINGi9606.ENSP00000226193.

PTM databases

PhosphoSiteiP35243.

Polymorphism and mutation databases

BioMutaiRCVRN.
DMDMi464600.

Proteomic databases

PaxDbiP35243.
PRIDEiP35243.

Protocols and materials databases

DNASUi5957.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000226193; ENSP00000226193; ENSG00000109047.
GeneIDi5957.
KEGGihsa:5957.
UCSCiuc002gme.2. human.

Organism-specific databases

CTDi5957.
GeneCardsiRCVRN.
HGNCiHGNC:9937. RCVRN.
MIMi179618. gene.
neXtProtiNX_P35243.
PharmGKBiPA162400987.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0044. Eukaryota.
COG5126. LUCA.
GeneTreeiENSGT00760000118820.
HOGENOMiHOG000233019.
HOVERGENiHBG108179.
InParanoidiP35243.
KOiK13764.
OMAiKECPSGR.
OrthoDBiEOG7GJ6F3.
PhylomeDBiP35243.
TreeFamiTF300009.

Enzyme and pathway databases

ReactomeiR-HSA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
SignaLinkiP35243.

Miscellaneous databases

ChiTaRSiRCVRN. human.
EvolutionaryTraceiP35243.
GenomeRNAii5957.
NextBioi23200.
PROiP35243.
SOURCEiSearch...

Gene expression databases

BgeeiP35243.
CleanExiHS_RCVRN.
GenevisibleiP35243. HS.

Family and domain databases

Gene3Di1.10.238.10. 3 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR028846. Recoverin.
[Graphical view]
PANTHERiPTHR23055. PTHR23055. 1 hit.
PfamiPF13499. EF-hand_7. 1 hit.
PF13833. EF-hand_8. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of human retinal genes: recoverin cDNA and gene."
    Murakami A., Yajima T., Inana G.
    Biochem. Biophys. Res. Commun. 187:234-244(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  2. "Molecular cloning and nucleotide sequence of a cDNA encoding recoverin from human retina."
    Wiechmann A.F., Hammarback J.A.
    Exp. Eye Res. 56:463-470(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  3. "The cancer-associated retinopathy antigen is a recoverin-like protein."
    Thirkill C.E., Tait R.C., Tyler N.K., Roth A.M., Keltner J.L.
    Invest. Ophthalmol. Vis. Sci. 33:2768-2772(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Expression of a photoreceptor protein, recoverin, as a cancer-associated retinopathy autoantigen in human lung cancer cell lines."
    Matsubara S., Yamaji Y., Sato M., Fujita J., Takahara J.
    Br. J. Cancer 74:1419-1422(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Subthalamic nucleus.
  7. "Full-length transcriptome analysis of human retina-derived cell lines ARPE-19 and Y79 using the vector-capping method."
    Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S., Usami R., Ohtoko K., Kato S.
    Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  8. 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].
    Tissue: Eye.
  10. "A photoreceptor calcium binding protein is recognized by autoantibodies obtained from patients with cancer-associated retinopathy."
    Polans A.S., Buczylko J., Crabb J., Palczewski K.
    J. Cell Biol. 112:981-989(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
  11. "Crystal structure of human recoverin at 2.2 A resolution."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

Entry informationi

Entry nameiRECO_HUMAN
AccessioniPrimary (citable) accession number: P35243
Secondary accession number(s): Q53XL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 150 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

Miscellaneous

Binds two calcium ions; one with high affinity, the other with low affinity.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.