OCAD1_MOUSE
ID OCAD1_MOUSE Reviewed; 247 AA.
AC Q9CRD0; Q3TEC2; Q3TJS3; Q7TNB3; Q922M2;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=OCIA domain-containing protein 1;
GN Name=Ociad1 {ECO:0000312|MGI:MGI:1915345}; Synonyms=Asrij;
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] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J;
RX PubMed=12889067; DOI=10.1002/dvdy.10332;
RA Mukhopadhyay A., Das D., Inamdar M.S.;
RT "Embryonic stem cell and tissue-specific expression of a novel conserved
RT gene, asrij.";
RL Dev. Dyn. 227:578-586(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Brain cortex, Cecum, Corpora quadrigemina, Medulla oblongata,
RC Pancreas, Placenta, Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108 AND SER-193, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, INDUCTION, DOMAIN, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=23972987; DOI=10.1016/j.celrep.2013.07.029;
RA Sinha A., Khadilkar R.J., Vinay K.S., Roychowdhury Sinha A., Inamdar M.S.;
RT "Conserved regulation of the Jak/STAT pathway by the endosomal protein
RT asrij maintains stem cell potency.";
RL Cell Rep. 4:649-658(2013).
CC -!- FUNCTION: Maintains stem cell potency (PubMed:23972987). Increases
CC STAT3 phosphorylation and controls ERK phosphorylation
CC (PubMed:23972987). May act as a scaffold, increasing STAT3 recruitment
CC onto endosomes (PubMed:23972987). {ECO:0000269|PubMed:23972987}.
CC -!- SUBUNIT: Interacts with STAT3. {ECO:0000269|PubMed:23972987}.
CC -!- SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:12889067,
CC ECO:0000269|PubMed:23972987}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9CRD0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CRD0-2; Sequence=VSP_027623;
CC Name=3;
CC IsoId=Q9CRD0-3; Sequence=VSP_027624, VSP_027625;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the brain and at lower
CC levels in the heart, ovary, testis and kidney. Expression is strongest
CC in embryonic stem cells and in the blood vessels.
CC {ECO:0000269|PubMed:12889067}.
CC -!- DEVELOPMENTAL STAGE: First detected at 6.5 dpc in the primitive streak
CC region of the epiblast and extraembryonic vasculature. Expression in
CC the 8.5 dpc yolk sac is seen within blood islands and the capillary
CC plexus. As embryogenesis proceeds, expression becomes prominent in the
CC blood islands and the primitive blood vessels of the yolk sac. By 8-8.5
CC dpc, a more generalized expression pattern is seen in the neural folds
CC and caudally in the presomitic mesoderm and primitive streak regions. A
CC definite increase in vascular expression is seen in the embryo by 9.5
CC dpc. Tissue-specific expression is initially seen from early 9.5 dpc in
CC the anterior-most regions of the head, mainly in the optic vesicle and
CC branchial arches. At 11.5 dpc and 13.5 dpc, strong expression is seen
CC in the embryonic stem cells of the blood vessels, especially in the
CC capillaries of the brain and in the hyaline vasculature of the eye.
CC Weak expression is also seen in the lingual vessels and in the neural
CC crest-derived regions of the jaw. A rapid increase in expression in the
CC trunk is seen between 9.5 dpc and 10.5 dpc and by 13.5 dpc, expression
CC is more localized. Expression is not detected in the embryonic heart at
CC early 9.5 dpc and from 11.5 dpc onward, increasing expression is seen
CC in the atrium, ventricle, and outflow tracts of the heart.
CC {ECO:0000269|PubMed:12889067}.
CC -!- INDUCTION: Expression is down-regulated as differentiation proceeds in
CC stem cells. {ECO:0000269|PubMed:23972987}.
CC -!- DOMAIN: The OCIA domain is necessary and sufficient for endosomal
CC localization (PubMed:23972987). {ECO:0000269|PubMed:23972987}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE39422.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF295357; AAG59858.1; -; mRNA.
DR EMBL; AF295358; AAG59859.1; -; Genomic_DNA.
DR EMBL; AY208935; AAP41523.1; -; mRNA.
DR EMBL; AK006013; BAB24366.1; -; mRNA.
DR EMBL; AK007636; BAB25152.1; -; mRNA.
DR EMBL; AK043603; BAC31593.1; -; mRNA.
DR EMBL; AK077904; BAC37055.1; -; mRNA.
DR EMBL; AK078102; BAC37125.1; -; mRNA.
DR EMBL; AK078909; BAC37453.1; -; mRNA.
DR EMBL; AK080795; BAC38024.1; -; mRNA.
DR EMBL; AK082769; BAC38610.1; -; mRNA.
DR EMBL; AK082781; BAC38616.1; -; mRNA.
DR EMBL; AK159811; BAE35391.1; -; mRNA.
DR EMBL; AK167320; BAE39422.1; ALT_FRAME; mRNA.
DR EMBL; AK169715; BAE41326.1; -; mRNA.
DR EMBL; BC006937; AAH06937.1; -; mRNA.
DR CCDS; CCDS19339.1; -. [Q9CRD0-1]
DR CCDS; CCDS51518.1; -. [Q9CRD0-3]
DR CCDS; CCDS80300.1; -. [Q9CRD0-2]
DR RefSeq; NP_001153359.1; NM_001159887.1. [Q9CRD0-2]
DR RefSeq; NP_001153360.1; NM_001159888.1. [Q9CRD0-3]
DR RefSeq; NP_001153361.1; NM_001159889.1. [Q9CRD0-3]
DR RefSeq; NP_075918.1; NM_023429.4. [Q9CRD0-1]
DR RefSeq; XP_006504138.1; XM_006504075.3. [Q9CRD0-1]
DR RefSeq; XP_006504139.1; XM_006504076.3. [Q9CRD0-1]
DR RefSeq; XP_017176571.1; XM_017321082.1. [Q9CRD0-2]
DR RefSeq; XP_017176572.1; XM_017321083.1. [Q9CRD0-3]
DR AlphaFoldDB; Q9CRD0; -.
DR BioGRID; 212653; 5.
DR STRING; 10090.ENSMUSP00000031038; -.
DR iPTMnet; Q9CRD0; -.
DR PhosphoSitePlus; Q9CRD0; -.
DR SwissPalm; Q9CRD0; -.
DR EPD; Q9CRD0; -.
DR jPOST; Q9CRD0; -.
DR MaxQB; Q9CRD0; -.
DR PaxDb; Q9CRD0; -.
DR PeptideAtlas; Q9CRD0; -.
DR PRIDE; Q9CRD0; -.
DR ProteomicsDB; 293481; -. [Q9CRD0-1]
DR ProteomicsDB; 293482; -. [Q9CRD0-2]
DR ProteomicsDB; 293483; -. [Q9CRD0-3]
DR Antibodypedia; 23858; 234 antibodies from 32 providers.
DR DNASU; 68095; -.
DR Ensembl; ENSMUST00000031038; ENSMUSP00000031038; ENSMUSG00000029152. [Q9CRD0-1]
DR Ensembl; ENSMUST00000071081; ENSMUSP00000069412; ENSMUSG00000029152. [Q9CRD0-3]
DR Ensembl; ENSMUST00000166823; ENSMUSP00000128805; ENSMUSG00000029152. [Q9CRD0-3]
DR Ensembl; ENSMUST00000200935; ENSMUSP00000144515; ENSMUSG00000029152. [Q9CRD0-2]
DR Ensembl; ENSMUST00000202250; ENSMUSP00000143799; ENSMUSG00000029152. [Q9CRD0-3]
DR GeneID; 68095; -.
DR KEGG; mmu:68095; -.
DR UCSC; uc008xss.2; mouse. [Q9CRD0-1]
DR UCSC; uc008xst.2; mouse. [Q9CRD0-3]
DR UCSC; uc008xsv.2; mouse. [Q9CRD0-2]
DR CTD; 54940; -.
DR MGI; MGI:1915345; Ociad1.
DR VEuPathDB; HostDB:ENSMUSG00000029152; -.
DR eggNOG; ENOG502RXQR; Eukaryota.
DR GeneTree; ENSGT00530000063690; -.
DR HOGENOM; CLU_083038_0_0_1; -.
DR InParanoid; Q9CRD0; -.
DR OMA; AGKMSYM; -.
DR OrthoDB; 1322104at2759; -.
DR PhylomeDB; Q9CRD0; -.
DR TreeFam; TF327106; -.
DR BioGRID-ORCS; 68095; 6 hits in 73 CRISPR screens.
DR ChiTaRS; Ociad1; mouse.
DR PRO; PR:Q9CRD0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9CRD0; protein.
DR Bgee; ENSMUSG00000029152; Expressed in primary visual cortex and 116 other tissues.
DR ExpressionAtlas; Q9CRD0; baseline and differential.
DR Genevisible; Q9CRD0; MM.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:2000736; P:regulation of stem cell differentiation; IMP: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 Alternative splicing; Endosome; Phosphoprotein; Reference proteome.
FT CHAIN 1..247
FT /note="OCIA domain-containing protein 1"
FT /id="PRO_0000299384"
FT DOMAIN 1..112
FT /note="OCIA"
FT REGION 113..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..149
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 MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
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:0007744|PubMed:21183079"
FT VAR_SEQ 185..235
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12889067"
FT /id="VSP_027623"
FT VAR_SEQ 186..189
FT /note="PEPN -> RNFS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_027624"
FT VAR_SEQ 190..247
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_027625"
FT CONFLICT 151
FT /note="D -> G (in Ref. 2; BAE41326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 247 AA; 27610 MW; 00EDDB3D12B16853 CRC64;
MNGRADFREP NAQVSRPIPD IGGGYIPTEE EWRLFAECHE ECFWFRSVPL AATSMLITQG
LISKGILSSH PKYGSIPKLL FACIVGYFAG KLSYVKTCQE KFKKLENSPL GEALRSGELR
RSSPPGHYTQ KPKFDSNVSG QSSFGTSPAA DNIEKEALPR YEPIPFSASM NESTPTGITD
HIAQGPEPNL EESPKRKGVT YEELRSKNRE SYGVTLPHKT DPSVRPMQER VPKKEVKVNK
YGDTWDE
