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TMM8B_MOUSE
ID   TMM8B_MOUSE             Reviewed;         472 AA.
AC   B1AWJ5; B9EJV2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Transmembrane protein 8B;
DE   AltName: Full=Protein NGX6;
GN   Name=Tmem8b;
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 [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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and 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 function as a regulator of the EGFR pathway. Probable
CC       tumor suppressor which may function in cell growth, proliferation and
CC       adhesion (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: May interact with EZR. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A6NDV4};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:A6NDV4}. Cytoplasm
CC       {ECO:0000250|UniProtKB:A6NDV4}. Nucleus {ECO:0000250|UniProtKB:A6NDV4}.
CC       Mitochondrion {ECO:0000250|UniProtKB:A6NDV4}. Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:A6NDV4}. Note=Also detected in mitochondrion and
CC       endoplasmic reticulum. {ECO:0000250|UniProtKB:A6NDV4}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TMEM8 family. {ECO:0000305}.
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DR   EMBL; AL732626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC147569; AAI47570.1; -; mRNA.
DR   EMBL; BC147574; AAI47575.1; -; mRNA.
DR   EMBL; BC151067; AAI51068.1; -; mRNA.
DR   EMBL; BC151070; AAI51071.1; -; mRNA.
DR   CCDS; CCDS51168.1; -.
DR   RefSeq; NP_001078977.1; NM_001085508.2.
DR   RefSeq; XP_011248332.1; XM_011250030.2.
DR   AlphaFoldDB; B1AWJ5; -.
DR   STRING; 10090.ENSMUSP00000103497; -.
DR   GlyGen; B1AWJ5; 1 site.
DR   iPTMnet; B1AWJ5; -.
DR   PhosphoSitePlus; B1AWJ5; -.
DR   PaxDb; B1AWJ5; -.
DR   PRIDE; B1AWJ5; -.
DR   ProteomicsDB; 259435; -.
DR   Antibodypedia; 26101; 155 antibodies from 20 providers.
DR   Ensembl; ENSMUST00000107864; ENSMUSP00000103496; ENSMUSG00000078716.
DR   Ensembl; ENSMUST00000107865; ENSMUSP00000103497; ENSMUSG00000078716.
DR   Ensembl; ENSMUST00000167153; ENSMUSP00000129760; ENSMUSG00000078716.
DR   GeneID; 242409; -.
DR   KEGG; mmu:242409; -.
DR   UCSC; uc008sqv.1; mouse.
DR   CTD; 51754; -.
DR   MGI; MGI:2441680; Tmem8b.
DR   VEuPathDB; HostDB:ENSMUSG00000078716; -.
DR   eggNOG; ENOG502QQ7Q; Eukaryota.
DR   GeneTree; ENSGT00940000157861; -.
DR   HOGENOM; CLU_012979_1_0_1; -.
DR   InParanoid; B1AWJ5; -.
DR   OMA; LDCREWN; -.
DR   PhylomeDB; B1AWJ5; -.
DR   TreeFam; TF331003; -.
DR   BioGRID-ORCS; 242409; 0 hits in 72 CRISPR screens.
DR   PRO; PR:B1AWJ5; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; B1AWJ5; protein.
DR   Bgee; ENSMUSG00000078716; Expressed in spermatid and 58 other tissues.
DR   ExpressionAtlas; B1AWJ5; baseline and differential.
DR   Genevisible; B1AWJ5; MM.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR021910; NGX6/PGAP6/MYMK.
DR   PANTHER; PTHR14319; PTHR14319; 1.
DR   Pfam; PF12036; DUF3522; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
PE   2: Evidence at transcript level;
KW   Cell adhesion; Cell membrane; Cytoplasm; Disulfide bond; EGF-like domain;
KW   Endoplasmic reticulum; Glycoprotein; Growth regulation; Membrane;
KW   Mitochondrion; Nucleus; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..472
FT                   /note="Transmembrane protein 8B"
FT                   /id="PRO_0000333040"
FT   TOPO_DOM        1..233
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        255..257
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        258..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        278..292
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        293..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        314..315
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        337..342
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        364..379
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        401..405
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        406..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        427..472
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          182..221
FT                   /note="EGF-like"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        186..196
FT                   /evidence="ECO:0000250"
FT   DISULFID        190..209
FT                   /evidence="ECO:0000250"
FT   DISULFID        211..220
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   472 AA;  52114 MW;  7CA09DD6D1676DDE CRC64;
     MNMPQSLGTQ PLPPEPPSLG TPIEGSGAIA PTEHCWPVRP TLRNELDTFS VHFYIFFGPS
     VALPPERPAV FALRLLPVLD SGGVLSLELQ LNASSLRQEN VTVFGCLTHE VPLSLGDAAV
     TCSKESLAGF LLSVSATSRV ARLRIPFPQT GTWFLTLRSL CGVGPRFVRC RNATAEVRLR
     TFLSPCVDDC GPYGQCKLLR THNYLYAACE CKAGWRGWGC TDSADALTYG FQLLSTLLLC
     LSNLMFLPPV VLAIRSRYVL EAAVYTFTMF FSTFYHACDQ PGIVVFCIMD YDVLQFCDFL
     GSLMSVWVTV IAMARLQPVI KQVLYLLGAM LLSMALQLDR HGLWNLLGPS LFALGILATA
     WTVRSVRRRH CYPPTWRRWL FYLCPGSLIA GSAVLLYAFV ETRDNYFYIH SIWHMLIAGS
     VGFLLPPRAK TDRRVPSGAR ARGCGYQLCI NEQEELGLVG PGGTTVSSIC VS
 
 
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