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PRCD_MOUSE
ID   PRCD_MOUSE              Reviewed;          53 AA.
AC   Q00LT2;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Photoreceptor disk component PRCD {ECO:0000312|MGI:MGI:3649529};
DE   AltName: Full=Progressive rod-cone degeneration protein homolog {ECO:0000250|UniProtKB:Q00LT1};
GN   Name=Prcd {ECO:0000312|MGI:MGI:3649529}; Synonyms=Gm11744;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16938425; DOI=10.1016/j.ygeno.2006.07.007;
RA   Zangerl B., Goldstein O., Philp A.R., Lindauer S.J.P., Pearce-Kelling S.E.,
RA   Mullins R.F., Graphodatsky A.S., Ripoll D., Felix J.S., Stone E.M.,
RA   Acland G.M., Aguirre G.D.;
RT   "Identical mutation in a novel retinal gene causes progressive rod-cone
RT   degeneration in dogs and retinitis pigmentosa in humans.";
RL   Genomics 88:551-563(2006).
RN   [2]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=23672200; DOI=10.1021/pr4003678;
RA   Skiba N.P., Spencer W.J., Salinas R.Y., Lieu E.C., Thompson J.W.,
RA   Arshavsky V.Y.;
RT   "Proteomic identification of unique photoreceptor disc components reveals
RT   the presence of PRCD, a protein linked to retinal degeneration.";
RL   J. Proteome Res. 12:3010-3018(2013).
RN   [3]
RP   INTERACTION WITH RHO, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   PALMITOYLATION AT CYS-2, AND MUTAGENESIS OF CYS-2.
RX   PubMed=27509380; DOI=10.1021/acs.biochem.6b00489;
RA   Spencer W.J., Pearring J.N., Salinas R.Y., Loiselle D.R., Skiba N.P.,
RA   Arshavsky V.Y.;
RT   "Progressive Rod-Cone Degeneration (PRCD) Protein Requires N-Terminal S-
RT   Acylation and Rhodopsin Binding for Photoreceptor Outer Segment
RT   Localization and Maintaining Intracellular Stability.";
RL   Biochemistry 55:5028-5037(2016).
RN   [4]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=27613864; DOI=10.1074/jbc.m116.742767;
RA   Murphy J., Kolandaivelu S.;
RT   "Palmitoylation of Progressive Rod-Cone Degeneration (PRCD) Regulates
RT   Protein Stability and Localization.";
RL   J. Biol. Chem. 291:23036-23046(2016).
CC   -!- FUNCTION: Involved in vision. {ECO:0000250|UniProtKB:Q00LT1}.
CC   -!- SUBUNIT: Interacts with RHO/rhodopsin; the interaction promotes PRCD
CC       stability. {ECO:0000269|PubMed:27509380}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium, photoreceptor outer
CC       segment {ECO:0000269|PubMed:23672200, ECO:0000269|PubMed:27509380,
CC       ECO:0000269|PubMed:27613864}. Membrane {ECO:0000269|PubMed:27509380,
CC       ECO:0000269|PubMed:27613864}; Lipid-anchor
CC       {ECO:0000269|PubMed:27509380}; Cytoplasmic side
CC       {ECO:0000269|PubMed:27509380}. Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q00LT1}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:Q00LT1}. Note=Localizes to photoreceptor disk
CC       membranes in the photoreceptor outer segment.
CC       {ECO:0000269|PubMed:27509380}.
CC   -!- TISSUE SPECIFICITY: Expressed in retina, where it localizes to both rod
CC       and cone photoreceptors (at protein level).
CC       {ECO:0000269|PubMed:23672200, ECO:0000269|PubMed:27509380,
CC       ECO:0000269|PubMed:27613864}.
CC   -!- PTM: Palmitoylated at Cys-2 (PubMed:27509380). Palmitoylation is
CC       essential for protein stability and trafficking to the photoreceptor
CC       outer segment, but does not appear to be essential for membrane
CC       localization (PubMed:27509380). Probably palmitoylated by ZDHHC3 (By
CC       similarity). {ECO:0000250|UniProtKB:Q00LT1,
CC       ECO:0000269|PubMed:27509380}.
CC   -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:E1B7R9}.
CC   -!- SIMILARITY: Belongs to the PRCD family. {ECO:0000305}.
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DR   EMBL; DQ390337; ABD17428.1; -; mRNA.
DR   CCDS; CCDS48987.1; -.
DR   RefSeq; NP_001156790.1; NM_001163318.1.
DR   AlphaFoldDB; Q00LT2; -.
DR   SwissPalm; Q00LT2; -.
DR   PaxDb; Q00LT2; -.
DR   PRIDE; Q00LT2; -.
DR   Ensembl; ENSMUST00000116318; ENSMUSP00000112020; ENSMUSG00000075410.
DR   Ensembl; ENSMUST00000148484; ENSMUSP00000119671; ENSMUSG00000075410.
DR   GeneID; 100038570; -.
DR   KEGG; mmu:100038570; -.
DR   UCSC; uc007mlx.2; mouse.
DR   CTD; 768206; -.
DR   MGI; MGI:3649529; Prcd.
DR   VEuPathDB; HostDB:ENSMUSG00000075410; -.
DR   GeneTree; ENSGT00900000143652; -.
DR   HOGENOM; CLU_3175255_0_0_1; -.
DR   InParanoid; Q00LT2; -.
DR   OMA; CRRRFAN; -.
DR   OrthoDB; 1638622at2759; -.
DR   BioGRID-ORCS; 100038570; 2 hits in 59 CRISPR screens.
DR   ChiTaRS; Prcd; mouse.
DR   PRO; PR:Q00LT2; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q00LT2; protein.
DR   Bgee; ENSMUSG00000075410; Expressed in retinal neural layer and 94 other tissues.
DR   ExpressionAtlas; Q00LT2; baseline and differential.
DR   Genevisible; Q00LT2; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0001750; C:photoreceptor outer segment; IDA:HGNC.
DR   GO; GO:0042622; C:photoreceptor outer segment membrane; IDA:UniProtKB.
DR   GO; GO:0002046; F:opsin binding; IPI:UniProtKB.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   InterPro; IPR027937; PRCD.
DR   PANTHER; PTHR38501; PTHR38501; 1.
DR   Pfam; PF15201; Rod_cone_degen; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Endoplasmic reticulum; Golgi apparatus; Lipoprotein;
KW   Membrane; Palmitate; Reference proteome; Sensory transduction; Vision.
FT   CHAIN           1..53
FT                   /note="Photoreceptor disk component PRCD"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000280354"
FT   REGION          24..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           2
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000269|PubMed:27509380,
FT                   ECO:0000305|PubMed:27613864"
FT   MUTAGEN         2
FT                   /note="C->Y: Loss of N-terminal lipidation. Fails to
FT                   localize to the photoreceptor outer segment."
FT                   /evidence="ECO:0000269|PubMed:27509380"
SQ   SEQUENCE   53 AA;  5931 MW;  DE36C6262A6BC42C CRC64;
     MCTTLFLFSL AMLWRRRFTN RVEPEPSRVD GTVVGSGSDT DLQSTGREKG PVK
 
 
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