ID   OCAD1_BOVIN             Reviewed;         247 AA.
AC   Q5E948; Q3ZBB3;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=OCIA domain-containing protein 1;
GN   Name=Ociad1; Synonyms=Asrij {ECO:0000250|UniProtKB:Q9CRD0};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thymus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; BT021072; AAX09089.1; -; mRNA.
DR   EMBL; BC103460; AAI03461.1; -; mRNA.
DR   RefSeq; NP_001015648.1; NM_001015648.1.
DR   RefSeq; XP_005208017.1; XM_005207960.2.
DR   RefSeq; XP_005208022.1; XM_005207965.3.
DR   RefSeq; XP_010804434.1; XM_010806132.2.
DR   RefSeq; XP_010804435.1; XM_010806133.2.
DR   AlphaFoldDB; Q5E948; -.
DR   STRING; 9913.ENSBTAP00000014028; -.
DR   PaxDb; Q5E948; -.
DR   PRIDE; Q5E948; -.
DR   GeneID; 533520; -.
DR   KEGG; bta:533520; -.
DR   CTD; 54940; -.
DR   eggNOG; ENOG502RXQR; Eukaryota.
DR   HOGENOM; CLU_083038_0_0_1; -.
DR   InParanoid; Q5E948; -.
DR   OrthoDB; 1322104at2759; -.
DR   TreeFam; TF327106; -.
DR   Proteomes; UP000009136; Unplaced.
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   2: Evidence at transcript level;
KW   Endosome; Phosphoprotein; Reference proteome.
FT   CHAIN           1..247
FT                   /note="OCIA domain-containing protein 1"
FT                   /id="PRO_0000299381"
FT   DOMAIN          1..112
FT                   /note="OCIA"
FT   REGION          113..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          217..247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..149
FT                   /note="Polar 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         123
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NX40"
FT   MOD_RES         193
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NX40"
FT   CONFLICT        12
FT                   /note="A -> T (in Ref. 2; AAI03461)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   247 AA;  27829 MW;  DE0CFE50F4A96C3E CRC64;
     MNGRADFREP NAEVPRPIPH IGADYIPTEE ERRVFAECND ESFWFRSVPL AATSMLITQG
     LISKGILSSH PKYGSIPKLI FACIMGYFAG KLSYVKTCQE KFKNLENSPL GEALRSGQAR
     RSSPTGHYSQ RSKYDSNVSG HSSFGTSPAA DNLEKEMLPH YEPIPFSASL NESTPTGITD
     HIAQGPDPNT EESPKRKNIT YEELRNKNRE SYEVTLTHKT DPSVRPMQER MPKKEVKVNK
     YGDTWDE