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CAD15_MOUSE
ID   CAD15_MOUSE             Reviewed;         784 AA.
AC   P33146; B2RXU1; Q9QYZ7;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=Cadherin-15;
DE   AltName: Full=Cadherin-14;
DE   AltName: Full=Muscle cadherin;
DE            Short=M-cadherin;
DE   Flags: Precursor;
GN   Name=Cdh15; Synonyms=Cdh14;
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=C3H/HeJ; TISSUE=Muscle;
RA   Link D.;
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Muscle;
RX   PubMed=1840697; DOI=10.1073/pnas.88.18.8024;
RA   Donalies M., Cramer M., Ringwald M., Starzinski-Powitz A.;
RT   "Expression of M-cadherin, a member of the cadherin multigene family,
RT   correlates with differentiation of skeletal muscle cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:8024-8028(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 539-617.
RX   PubMed=10610704; DOI=10.1006/geno.1999.6022;
RA   Kelsey G., Bodle D., Miller H.J., Beechey C.V., Coombes C., Peters J.,
RA   Williamson C.M.;
RT   "Identification of imprinted loci by methylation-sensitive representational
RT   difference analysis: application to mouse distal chromosome 2.";
RL   Genomics 62:129-138(1999).
RN   [5]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-106 AND ASN-537.
RC   TISSUE=Myoblast;
RX   PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA   Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA   Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT   "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT   identification, glycosite occupancy, and membrane orientation.";
RL   Mol. Cell. Proteomics 8:2555-2569(2009).
CC   -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC       preferentially interact with themselves in a homophilic manner in
CC       connecting cells; cadherins may thus contribute to the sorting of
CC       heterogeneous cell types. M-cadherin is part of the myogenic program
CC       and may provide a trigger for terminal muscle differentiation.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- TISSUE SPECIFICITY: Skeletal muscle.
CC   -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC       cadherin domain and rigidify the connections, imparting a strong
CC       curvature to the full-length ectodomain. {ECO:0000250}.
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DR   EMBL; BC157978; AAI57979.1; -; mRNA.
DR   EMBL; M74541; AAC23585.1; -; mRNA.
DR   EMBL; AJ245402; CAB57281.2; -; Genomic_DNA.
DR   CCDS; CCDS22746.1; -.
DR   PIR; A40986; IJMSCM.
DR   RefSeq; NP_031688.2; NM_007662.2.
DR   AlphaFoldDB; P33146; -.
DR   SMR; P33146; -.
DR   BioGRID; 198634; 2.
DR   STRING; 10090.ENSMUSP00000034443; -.
DR   GlyConnect; 2167; 1 N-Linked glycan (1 site).
DR   GlyGen; P33146; 5 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; P33146; -.
DR   PhosphoSitePlus; P33146; -.
DR   PaxDb; P33146; -.
DR   PeptideAtlas; P33146; -.
DR   PRIDE; P33146; -.
DR   ProteomicsDB; 281741; -.
DR   Antibodypedia; 2417; 312 antibodies from 35 providers.
DR   DNASU; 12555; -.
DR   Ensembl; ENSMUST00000034443; ENSMUSP00000034443; ENSMUSG00000031962.
DR   GeneID; 12555; -.
DR   KEGG; mmu:12555; -.
DR   UCSC; uc009ntv.1; mouse.
DR   CTD; 1013; -.
DR   MGI; MGI:106672; Cdh15.
DR   VEuPathDB; HostDB:ENSMUSG00000031962; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT00940000160118; -.
DR   HOGENOM; CLU_005284_2_0_1; -.
DR   InParanoid; P33146; -.
DR   OMA; TTLYPWR; -.
DR   OrthoDB; 395835at2759; -.
DR   PhylomeDB; P33146; -.
DR   TreeFam; TF316817; -.
DR   Reactome; R-MMU-418990; Adherens junctions interactions.
DR   Reactome; R-MMU-525793; Myogenesis.
DR   BioGRID-ORCS; 12555; 2 hits in 75 CRISPR screens.
DR   PRO; PR:P33146; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; P33146; protein.
DR   Bgee; ENSMUSG00000031962; Expressed in myotome and 88 other tissues.
DR   Genevisible; P33146; MM.
DR   GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR   GO; GO:0005901; C:caveola; IDA:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031594; C:neuromuscular junction; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   Gene3D; 4.10.900.10; -; 1.
DR   InterPro; IPR039808; Cadherin.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR   InterPro; IPR027397; Catenin-bd_sf.
DR   PANTHER; PTHR24027; PTHR24027; 1.
DR   Pfam; PF00028; Cadherin; 5.
DR   Pfam; PF01049; Cadherin_C; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 4.
DR   SUPFAM; SSF49313; SSF49313; 5.
DR   PROSITE; PS00232; CADHERIN_1; 2.
DR   PROSITE; PS50268; CADHERIN_2; 5.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion; Cell membrane; Cleavage on pair of basic residues;
KW   Glycoprotein; Membrane; Metal-binding; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   PROPEP          22..59
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003807"
FT   CHAIN           60..784
FT                   /note="Cadherin-15"
FT                   /id="PRO_0000003808"
FT   TOPO_DOM        60..605
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        606..625
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        626..784
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          60..151
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          152..259
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          260..374
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          375..480
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          481..589
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   REGION          676..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19656770"
FT   CARBOHYD        226
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        530
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        537
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19656770"
FT   CARBOHYD        575
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        26
FT                   /note="K -> E (in Ref. 3; AAC23585)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        159
FT                   /note="R -> H (in Ref. 3; AAC23585)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        622
FT                   /note="L -> F (in Ref. 3; AAC23585)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   784 AA;  85644 MW;  A21D73960A6F0063 CRC64;
     MGSALLLALG LLAQSLGLSW AVPEPKPSTL YPWRRASAPG RVRRAWVIPP ISVSENHKRL
     PYPLVQIKSD KQQLGSVIYS IQGPGVDEEP RNVFSIDKFT GRVYLNATLD REKTDRFRLR
     AFALDLGGST LEDPTDLEIV VVDQNDNRPA FLQDVFRGRI LEGAIPGTFV TRAEATDADD
     PETDNAALRF SILEQGSPEF FSIDEHTGEI RTVQVGLDRE VVAVYNLTLQ VADMSGDGLT
     ATASAIISID DINDNAPEFT KDEFFMEAAE AVSGVDVGRL EVEDKDLPGS PNWVARFTIL
     EGDPDGQFKI YTDPKTNEGV LSVVKPLDYE SREQYELRVS VQNEAPLQAA APRARRGQTR
     VSVWVQDTNE APVFPENPLR TSIAEGAPPG TSVATFSARD PDTEQLQRIS YSKDYDPEDW
     LQVDGATGRI QTQRVLSPAS PFLKDGWYRA IILALDNAIP PSTATGTLSI EILEVNDHAP
     ALALPPSGSL CSEPDQGPGL LLGATDEDLP PHGAPFHFQL NPRVPDLGRN WSVSQINVSH
     ARLRLRHQVS EGLHRLSLLL QDSGEPPQQR EQTLNVTVCR CGSDGTCLPG AAALRGGGVG
     VSLGALVIVL ASTVVLLVLI LLAALRTRFR GHSRGKSLLH GLQEDLRDNI LNYDEQGGGE
     EDQDAYDINQ LRHPVEPRAT SRSLGRPPLR RDAPFSYVPQ PHRVLPTSPS DIANFISDGL
     EAADSDPSVP PYDTALIYDY EGDGSVAGTL SSILSSLGDE DQDYDYLRDW GPRFARLADM
     YGHQ
 
 
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