OCAD1_PONAB
ID OCAD1_PONAB Reviewed; 245 AA.
AC Q5RD48;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=OCIA domain-containing protein 1;
GN Name=OCIAD1; Synonyms=Asrij {ECO:0000250|UniProtKB:Q9CRD0};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR858070; CAH90309.1; -; mRNA.
DR RefSeq; NP_001125142.1; NM_001131670.1.
DR RefSeq; XP_009238215.1; XM_009239940.1.
DR RefSeq; XP_009238216.1; XM_009239941.1.
DR RefSeq; XP_009238217.1; XM_009239942.1.
DR RefSeq; XP_009238218.1; XM_009239943.1.
DR RefSeq; XP_009238219.1; XM_009239944.1.
DR RefSeq; XP_009238220.1; XM_009239945.1.
DR RefSeq; XP_009238221.1; XM_009239946.1.
DR AlphaFoldDB; Q5RD48; -.
DR STRING; 9601.ENSPPYP00000016445; -.
DR Ensembl; ENSPPYT00000041742; ENSPPYP00000027782; ENSPPYG00000014721.
DR GeneID; 100172028; -.
DR KEGG; pon:100172028; -.
DR CTD; 54940; -.
DR eggNOG; ENOG502RXQR; Eukaryota.
DR GeneTree; ENSGT00530000063690; -.
DR HOGENOM; CLU_083038_0_0_1; -.
DR InParanoid; Q5RD48; -.
DR OMA; AGKMSYM; -.
DR OrthoDB; 1322104at2759; -.
DR TreeFam; TF327106; -.
DR Proteomes; UP000001595; Chromosome 4.
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..245
FT /note="OCIA domain-containing protein 1"
FT /id="PRO_0000299383"
FT DOMAIN 1..112
FT /note="OCIA"
FT REGION 111..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..212
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..245
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 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NX40"
SQ SEQUENCE 245 AA; 27687 MW; 0D22E52ADBB666AB CRC64;
MNGRADFREP NAEVPRPIPH IGPDYIPTEE ERRVFAECND ESFWFRSVPL AATSMLITQG
LISKGILSSH PKYGSIPKLI FACIMGYFAG KLSYVKTCQE KFKKLENSPL GEALRSGQAR
RSSPPGHYYQ KSKYDSNVSG QSSFVTSPAA DNIEMLPHYE PIPFSSSMNE SAPTGITDHI
VQGPDPNLEE SPKRKNITYE ELRNKNRESY EVSLTQKTDP SVRPMHERVP KKEVKVNKYG
DTWDE