ITM2A_MOUSE
ID ITM2A_MOUSE Reviewed; 263 AA.
AC Q61500; Q3TJP5; Q8K0H4; Q9CRW4;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Integral membrane protein 2A;
DE AltName: Full=Protein E25;
GN Name=Itm2a; Synonyms=E25, Itm2;
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=BALB/cJ; TISSUE=Mandible;
RX PubMed=8702637; DOI=10.1074/jbc.271.32.19475;
RA Deleersnijder W., Hong G., Cortvrindt R., Poirier C., Tylzanowski P.,
RA Pittois K., Vanmarck E., Merregaert J.;
RT "Isolation of markers for chondro-osteogenic differentiation using cDNA
RT library subtraction. Molecular cloning and characterization of a gene
RT belonging to a novel multigene family of integral membrane proteins.";
RL J. Biol. Chem. 271:19475-19482(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RX PubMed=9892734; DOI=10.1007/s003359900942;
RA Pittois K., Wauters J., Bossuyt P., Deleersnijder W., Merregaert J.;
RT "Genomic organization and chromosomal localization of the Itm2a gene.";
RL Mamm. Genome 10:54-56(1999).
RN [3]
RP SEQUENCE REVISION TO 21.
RA Van den Plas D., Merregaert J.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, Embryonic eye, and Embryonic head;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in mandibular condyles, in bone and in
CC hair follicles. Strong expression in osteogenic tissues, such as
CC neonatal calvaria, paws, tail and skin.
CC -!- SIMILARITY: Belongs to the ITM2 family. {ECO:0000305}.
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DR EMBL; L38971; AAC37700.1; -; mRNA.
DR EMBL; AF074020; AAD14549.2; -; Genomic_DNA.
DR EMBL; AK014024; BAB29119.1; -; mRNA.
DR EMBL; AK051956; BAC34819.1; -; mRNA.
DR EMBL; AK167351; BAE39450.1; -; mRNA.
DR EMBL; BC031420; AAH31420.1; -; mRNA.
DR CCDS; CCDS30349.1; -.
DR RefSeq; NP_032435.2; NM_008409.2.
DR AlphaFoldDB; Q61500; -.
DR BioGRID; 200843; 1.
DR IntAct; Q61500; 1.
DR STRING; 10090.ENSMUSP00000033591; -.
DR GlyGen; Q61500; 1 site.
DR iPTMnet; Q61500; -.
DR PhosphoSitePlus; Q61500; -.
DR PaxDb; Q61500; -.
DR PeptideAtlas; Q61500; -.
DR PRIDE; Q61500; -.
DR ProteomicsDB; 268906; -.
DR Antibodypedia; 493; 146 antibodies from 24 providers.
DR DNASU; 16431; -.
DR Ensembl; ENSMUST00000033591; ENSMUSP00000033591; ENSMUSG00000031239.
DR GeneID; 16431; -.
DR KEGG; mmu:16431; -.
DR UCSC; uc009ucg.1; mouse.
DR CTD; 9452; -.
DR MGI; MGI:107706; Itm2a.
DR VEuPathDB; HostDB:ENSMUSG00000031239; -.
DR eggNOG; KOG4681; Eukaryota.
DR GeneTree; ENSGT00950000183115; -.
DR HOGENOM; CLU_074596_0_0_1; -.
DR InParanoid; Q61500; -.
DR OMA; RMYHGAM; -.
DR OrthoDB; 1322680at2759; -.
DR PhylomeDB; Q61500; -.
DR TreeFam; TF317770; -.
DR BioGRID-ORCS; 16431; 2 hits in 69 CRISPR screens.
DR ChiTaRS; Itm2a; mouse.
DR PRO; PR:Q61500; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q61500; protein.
DR Bgee; ENSMUSG00000031239; Expressed in humerus cartilage element and 264 other tissues.
DR Genevisible; Q61500; MM.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001540; F:amyloid-beta binding; IBA:GO_Central.
DR GO; GO:0042985; P:negative regulation of amyloid precursor protein biosynthetic process; IBA:GO_Central.
DR GO; GO:0002317; P:plasma cell differentiation; IMP:MGI.
DR InterPro; IPR007084; BRICHOS_dom.
DR InterPro; IPR040145; ITM2.
DR PANTHER; PTHR10962; PTHR10962; 1.
DR Pfam; PF04089; BRICHOS; 1.
DR SMART; SM01039; BRICHOS; 1.
DR PROSITE; PS50869; BRICHOS; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..263
FT /note="Integral membrane protein 2A"
FT /id="PRO_0000154819"
FT TRANSMEM 54..74
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT DOMAIN 133..227
FT /note="BRICHOS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 160..219
FT /evidence="ECO:0000250"
FT CONFLICT 21
FT /note="V -> I (in Ref. 1; AAC37700)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 29691 MW; 3F809DB8DA2BCC37 CRC64;
MVKIAFNTPT AVQKEEARQD VEALVSRTVR AQILTGKELR VVPQEKDGSS GRCMLTLLGL
SFILAGLIVG GACIYKYFMP KSTIYHGEMC FFDSEDPVNS IPGGEPYFLP VTEEADIRED
DNIAIIDVPV PSFSDSDPAA IIHDFEKGMT AYLDLLLGNC YLMPLNTSIV MTPKNLVELF
GKLASGKYLP HTYVVREDLV AVEEIRDVSN LGIFIYQLCN NRKSFRLRRR DLLLGFNKRA
IDKCWKIRHF PNEFIVETKI CQE
