ID   OCAD1_RAT               Reviewed;         247 AA.
AC   Q5XIG4;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=OCIA domain-containing protein 1;
GN   Name=Ociad1 {ECO:0000312|RGD:1359549};
GN   Synonyms=Asrij {ECO:0000250|UniProtKB:Q9CRD0};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA   Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT   "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT   regulation of aquaporin-2 phosphorylation at two sites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193 AND SER-198, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Maintains stem cell potency (By similarity). Increases STAT3
CC       phosphorylation and controls ERK phosphorylation (By similarity). May
CC       act as a scaffold, increasing STAT3 recruitment onto endosomes (By
CC       similarity). {ECO:0000250|UniProtKB:Q9CRD0}.
CC   -!- SUBUNIT: Interacts with STAT3. {ECO:0000250|UniProtKB:Q9CRD0}.
CC   -!- SUBCELLULAR LOCATION: Endosome {ECO:0000250|UniProtKB:Q9CRD0}.
CC   -!- DOMAIN: The OCIA domain is necessary and sufficient for endosomal
CC       localization. {ECO:0000250|UniProtKB:Q9CRD0}.
CC   -!- MISCELLANEOUS: 'Asrij' stands for 'blood' in Sanskrit as this protein
CC       is strongly expressed in blood vessels.
CC   -!- SIMILARITY: Belongs to the OCIAD1 family. {ECO:0000305}.
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DR   EMBL; BC083718; AAH83718.1; -; mRNA.
DR   RefSeq; NP_001013896.1; NM_001013874.1.
DR   AlphaFoldDB; Q5XIG4; -.
DR   STRING; 10116.ENSRNOP00000002996; -.
DR   iPTMnet; Q5XIG4; -.
DR   PhosphoSitePlus; Q5XIG4; -.
DR   jPOST; Q5XIG4; -.
DR   PaxDb; Q5XIG4; -.
DR   PRIDE; Q5XIG4; -.
DR   DNASU; 289590; -.
DR   GeneID; 289590; -.
DR   KEGG; rno:289590; -.
DR   UCSC; RGD:1359549; rat.
DR   CTD; 54940; -.
DR   RGD; 1359549; Ociad1.
DR   VEuPathDB; HostDB:ENSRNOG00000002205; -.
DR   eggNOG; ENOG502RXQR; Eukaryota.
DR   HOGENOM; CLU_083038_0_0_1; -.
DR   InParanoid; Q5XIG4; -.
DR   OMA; AGKMSYM; -.
DR   OrthoDB; 1322104at2759; -.
DR   PhylomeDB; Q5XIG4; -.
DR   TreeFam; TF327106; -.
DR   PRO; PR:Q5XIG4; -.
DR   Proteomes; UP000002494; Chromosome 14.
DR   Bgee; ENSRNOG00000002205; Expressed in cerebellum and 20 other tissues.
DR   Genevisible; Q5XIG4; RN.
DR   GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR   GO; GO:2000736; P:regulation of stem cell differentiation; ISS:UniProtKB.
DR   InterPro; IPR040187; OCAD1/2.
DR   InterPro; IPR009764; OCIA_dom.
DR   PANTHER; PTHR13336; PTHR13336; 1.
DR   Pfam; PF07051; OCIA; 1.
PE   1: Evidence at protein level;
KW   Endosome; Phosphoprotein; Reference proteome.
FT   CHAIN           1..247
FT                   /note="OCIA domain-containing protein 1"
FT                   /id="PRO_0000299385"
FT   DOMAIN          1..112
FT                   /note="OCIA"
FT   REGION          116..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..214
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..247
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         108
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NX40"
FT   MOD_RES         116
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NX40"
FT   MOD_RES         193
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         198
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16641100,
FT                   ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   247 AA;  27659 MW;  DCCAC49D5FD88F1B CRC64;
     MNGRADFREP NAQVSRPIPD IGGGYIPTEE EWRLFAECHE ECFWFRSVPL AATSMLITQG
     LISKGILSSH PKYGSIPKLI FACIVGYFAG KLSYVKTCQE KFKKLENSPL GEALRSGELR
     RSLPPGHYTQ KPKYDSNVSG QSSFGTSPAA DNIEKETLPR YEPIPFSASM NESTPTGITD
     HIAQGPDPNL EDSPKRKSVT YEELRNKNRE SYGVTLSHKT DPSVRPMQER GPQKEVKVNK
     YGDTWDE