位置:首页 > 蛋白库 > TM2D1_MOUSE
TM2D1_MOUSE
ID   TM2D1_MOUSE             Reviewed;         208 AA.
AC   Q99MB3; A2ADR1; A2ADR4;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=TM2 domain-containing protein 1;
DE   AltName: Full=Amyloid-beta-binding protein;
DE            Short=mBBP;
DE   Flags: Precursor;
GN   Name=Tm2d1; Synonyms=Bbp;
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] (ISOFORM 1).
RC   STRAIN=BALB/cJ;
RX   PubMed=11278849; DOI=10.1074/jbc.m011161200;
RA   Kajkowski E.M., Lo C.F., Ning X., Walker S., Sofia H.J., Wang W., Edris W.,
RA   Chanda P., Wagner E., Vile S., Ryan K., McHendry-Rinde B., Smith S.C.,
RA   Wood A., Rhodes K.J., Kennedy J.D., Bard J., Jacobsen J.S.,
RA   Ozenberger B.A.;
RT   "Beta-amyloid peptide-induced apoptosis regulated by a novel protein
RT   containing a G protein activation module.";
RL   J. Biol. Chem. 276:18748-18756(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
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   -!- FUNCTION: May participate in amyloid-beta-induced apoptosis via its
CC       interaction with beta-APP42. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with APP beta-APP42 (amyloid-beta protein 42).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99MB3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99MB3-2; Sequence=VSP_027494;
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TM2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AK009511; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAM26981.1; Type=Erroneous gene model prediction; 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; AF353993; AAK35067.1; -; mRNA.
DR   EMBL; AK009511; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AL671140; CAM26981.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL671140; CAM26983.1; -; Genomic_DNA.
DR   EMBL; AL671140; CAM26984.1; -; Genomic_DNA.
DR   EMBL; BC089492; AAH89492.1; -; mRNA.
DR   CCDS; CCDS18374.1; -. [Q99MB3-1]
DR   RefSeq; NP_444387.1; NM_053157.2. [Q99MB3-1]
DR   AlphaFoldDB; Q99MB3; -.
DR   STRING; 10090.ENSMUSP00000099855; -.
DR   GlyConnect; 2433; 2 N-Linked glycans (2 sites). [Q99MB3-2]
DR   GlyGen; Q99MB3; 2 sites.
DR   PhosphoSitePlus; Q99MB3; -.
DR   PaxDb; Q99MB3; -.
DR   PeptideAtlas; Q99MB3; -.
DR   PRIDE; Q99MB3; -.
DR   ProteomicsDB; 259559; -. [Q99MB3-1]
DR   ProteomicsDB; 259560; -. [Q99MB3-2]
DR   Antibodypedia; 46902; 66 antibodies from 17 providers.
DR   DNASU; 94043; -.
DR   Ensembl; ENSMUST00000030292; ENSMUSP00000030292; ENSMUSG00000028563. [Q99MB3-2]
DR   Ensembl; ENSMUST00000102793; ENSMUSP00000099855; ENSMUSG00000028563. [Q99MB3-1]
DR   GeneID; 94043; -.
DR   KEGG; mmu:94043; -.
DR   UCSC; uc033idg.1; mouse. [Q99MB3-1]
DR   CTD; 83941; -.
DR   MGI; MGI:2137022; Tm2d1.
DR   VEuPathDB; HostDB:ENSMUSG00000028563; -.
DR   eggNOG; KOG4272; Eukaryota.
DR   GeneTree; ENSGT00940000157668; -.
DR   HOGENOM; CLU_110523_0_0_1; -.
DR   InParanoid; Q99MB3; -.
DR   OMA; ETFRKPH; -.
DR   OrthoDB; 1467308at2759; -.
DR   PhylomeDB; Q99MB3; -.
DR   TreeFam; TF314896; -.
DR   BioGRID-ORCS; 94043; 6 hits in 77 CRISPR screens.
DR   ChiTaRS; Tm2d1; mouse.
DR   PRO; PR:Q99MB3; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q99MB3; protein.
DR   Bgee; ENSMUSG00000028563; Expressed in embryonic brain and 62 other tissues.
DR   ExpressionAtlas; Q99MB3; baseline and differential.
DR   Genevisible; Q99MB3; MM.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR   GO; GO:0001540; F:amyloid-beta binding; IDA:MGI.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IDA:MGI.
DR   GO; GO:0097190; P:apoptotic signaling pathway; IDA:MGI.
DR   InterPro; IPR007829; TM2.
DR   Pfam; PF05154; TM2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Apoptosis; Glycoprotein; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000250"
FT   CHAIN           38..208
FT                   /note="TM2 domain-containing protein 1"
FT                   /id="PRO_0000298979"
FT   TRANSMEM        120..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         81..85
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_027494"
FT   CONFLICT        6
FT                   /note="P -> S (in Ref. 2; AK009511)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        86
FT                   /note="A -> E (in Ref. 2; AK009511)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   208 AA;  22272 MW;  91A7932163F4F04C CRC64;
     MAAAWPAGRA SPAAGPPGLL RTLWLVTVAA GHCGAAASGA VGGEETPKCE DLRVGQYICK
     EPKINDATQE PVNCTNYTAH VQCFPAPKIT CKDLSGNETH FTGSEVGFLK PISCRNVNGY
     SYKVAVALSL FLGWLGADRF YLGYPALGLL KFCTVGFCGI GSLIDFILIS MQIVGPSDGS
     SYIIDYYGTR LTRLSITNET FRKTQLYP
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024