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EMP3_MOUSE
ID   EMP3_MOUSE              Reviewed;         163 AA.
AC   O35912; O88333; Q3UIF8;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Epithelial membrane protein 3;
DE            Short=EMP-3;
DE   AltName: Full=Hematopoietic neural membrane protein 1;
DE            Short=HNMP-1;
DE   AltName: Full=Protein YMP;
GN   Name=Emp3; Synonyms=Ymp;
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].
RX   PubMed=9204931; DOI=10.1523/jneurosci.17-14-05493.1997;
RA   Bolin L.M., McNeil T., Lucian L.A., Devaux B., Franz-Bacon K., Gorman D.M.,
RA   Zurawski S., Murray R., McClanahan T.K.;
RT   "HNMP-1: a novel hematopoietic and neural membrane protein differentially
RT   regulated in neural development and injury.";
RL   J. Neurosci. 17:5493-5502(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9615230; DOI=10.1006/geno.1998.5238;
RA   Ben-Porath I., Kozak C.A., Benvenisty N.;
RT   "Chromosomal mapping of Tmp (Emp1), Xmp (Emp2), and Ymp (Emp3), genes
RT   encoding membrane proteins related to Pmp22.";
RL   Genomics 49:443-447(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; 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   -!- FUNCTION: Probably involved in cell proliferation and cell-cell
CC       interactions.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. {ECO:0000305}.
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DR   EMBL; U87948; AAC53324.1; -; mRNA.
DR   EMBL; AF011750; AAC33407.1; -; mRNA.
DR   EMBL; AK146939; BAE27548.1; -; mRNA.
DR   EMBL; AC149053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC001999; AAH01999.1; -; mRNA.
DR   CCDS; CCDS21270.1; -.
DR   RefSeq; NP_001139818.1; NM_001146346.1.
DR   RefSeq; NP_034259.2; NM_010129.2.
DR   AlphaFoldDB; O35912; -.
DR   SMR; O35912; -.
DR   STRING; 10090.ENSMUSP00000132519; -.
DR   GlyGen; O35912; 2 sites.
DR   iPTMnet; O35912; -.
DR   PhosphoSitePlus; O35912; -.
DR   PaxDb; O35912; -.
DR   PRIDE; O35912; -.
DR   ProteomicsDB; 277862; -.
DR   TopDownProteomics; O35912; -.
DR   Antibodypedia; 31695; 233 antibodies from 26 providers.
DR   DNASU; 13732; -.
DR   Ensembl; ENSMUST00000038876; ENSMUSP00000037289; ENSMUSG00000040212.
DR   Ensembl; ENSMUST00000164119; ENSMUSP00000132519; ENSMUSG00000040212.
DR   Ensembl; ENSMUST00000210297; ENSMUSP00000147800; ENSMUSG00000040212.
DR   GeneID; 13732; -.
DR   KEGG; mmu:13732; -.
DR   UCSC; uc009gxv.2; mouse.
DR   CTD; 2014; -.
DR   MGI; MGI:1098729; Emp3.
DR   VEuPathDB; HostDB:ENSMUSG00000040212; -.
DR   eggNOG; ENOG502RZP6; Eukaryota.
DR   GeneTree; ENSGT00950000182696; -.
DR   HOGENOM; CLU_138632_1_0_1; -.
DR   InParanoid; O35912; -.
DR   OMA; CRFDNFT; -.
DR   OrthoDB; 1420219at2759; -.
DR   PhylomeDB; O35912; -.
DR   TreeFam; TF330414; -.
DR   BioGRID-ORCS; 13732; 1 hit in 72 CRISPR screens.
DR   ChiTaRS; Emp3; mouse.
DR   PRO; PR:O35912; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; O35912; protein.
DR   Bgee; ENSMUSG00000040212; Expressed in humerus cartilage element and 234 other tissues.
DR   ExpressionAtlas; O35912; baseline and differential.
DR   Genevisible; O35912; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0032060; P:bleb assembly; ISO:MGI.
DR   GO; GO:0008219; P:cell death; ISO:MGI.
DR   InterPro; IPR003934; EMP_3.
DR   InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
DR   InterPro; IPR004032; PMP22_EMP_MP20.
DR   PANTHER; PTHR10671:SF8; PTHR10671:SF8; 1.
DR   Pfam; PF00822; PMP22_Claudin; 1.
DR   PRINTS; PR01453; EPMEMFAMILY.
DR   PRINTS; PR01456; EPMEMPROT3.
DR   PROSITE; PS01221; PMP22_1; 1.
DR   PROSITE; PS01222; PMP22_2; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..163
FT                   /note="Epithelial membrane protein 3"
FT                   /id="PRO_0000164661"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        96
FT                   /note="L -> I (in Ref. 2; AAC33407)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        106
FT                   /note="C -> W (in Ref. 2; AAC33407)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        129
FT                   /note="H -> Q (in Ref. 2; AAC33407)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        154..155
FT                   /note="TV -> IMY (in Ref. 2; AAC33407)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        154
FT                   /note="T -> I (in Ref. 1; AAC53324 and 5; AAH01999)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   163 AA;  18253 MW;  91620FD4C6AEB70C CRC64;
     MSLLLLVVSA LHILILVLLF VATLDKSWWT LPDKESLNLW YDCTWNTTTQ TWACSNVSEN
     GWLKAVQALM VLSLILCCLS FILFMFQLYT MRRGGLFYAT GLCQLCTSAA VFSGALIYAI
     HTEEILAKHP SGGSFGYCFA LAWVAFPLAL VSGTVYIHLR KRE
 
 
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