MUC13_MOUSE
ID MUC13_MOUSE Reviewed; 573 AA.
AC P19467;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Mucin-13;
DE Short=MUC-13;
DE AltName: Full=Cell surface antigen 114/A10;
DE AltName: Full=Lymphocyte antigen 64;
DE Flags: Precursor;
GN Name=Muc13; Synonyms=Ly64;
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=2784793; DOI=10.1016/s0021-9258(18)83377-4;
RA Dougherty G.J., Kay R.J., Humphries R.K.;
RT "Molecular cloning of 114/A10, a cell surface antigen containing highly
RT conserved repeated elements, which is expressed by murine hemopoietic
RT progenitor cells and interleukin-3-dependent cell lines.";
RL J. Biol. Chem. 264:6509-6514(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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: Epithelial and hemopoietic transmembrane mucin that may play
CC a role in cell signaling. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer of beta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Secreted {ECO:0000250}. Note=Also
CC exists as a soluble form. {ECO:0000250}.
CC -!- PTM: Cleaved into two subunits, alpha and beta, probably between the
CC first EGF domain and the SEA domain. Beta subunit contains the
CC cytoplasmic tail and alpha subunit the extracellular tail. The
CC homooligomerization into dimers is dependent on intrachain disulfide
CC bonds (By similarity). {ECO:0000250}.
CC -!- PTM: Highly N-glycosylated. {ECO:0000250}.
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DR EMBL; J04634; AAA37239.1; -; mRNA.
DR EMBL; BC024321; AAH24321.1; -; mRNA.
DR CCDS; CCDS28134.1; -.
DR PIR; A33533; A33533.
DR RefSeq; NP_034869.1; NM_010739.2.
DR RefSeq; XP_011244137.1; XM_011245835.1.
DR AlphaFoldDB; P19467; -.
DR BioGRID; 201238; 1.
DR STRING; 10090.ENSMUSP00000110696; -.
DR GlyGen; P19467; 3 sites.
DR iPTMnet; P19467; -.
DR PhosphoSitePlus; P19467; -.
DR PaxDb; P19467; -.
DR PeptideAtlas; P19467; -.
DR PRIDE; P19467; -.
DR ProteomicsDB; 290070; -.
DR Antibodypedia; 33002; 321 antibodies from 31 providers.
DR Ensembl; ENSMUST00000023520; ENSMUSP00000023520; ENSMUSG00000022824.
DR Ensembl; ENSMUST00000115044; ENSMUSP00000110696; ENSMUSG00000022824.
DR GeneID; 17063; -.
DR KEGG; mmu:17063; -.
DR UCSC; uc007zal.1; mouse.
DR CTD; 56667; -.
DR MGI; MGI:103190; Muc13.
DR VEuPathDB; HostDB:ENSMUSG00000022824; -.
DR eggNOG; ENOG502S3PG; Eukaryota.
DR GeneTree; ENSGT00940000154419; -.
DR HOGENOM; CLU_020534_1_0_1; -.
DR InParanoid; P19467; -.
DR OMA; GYQEDAN; -.
DR OrthoDB; 1023611at2759; -.
DR PhylomeDB; P19467; -.
DR TreeFam; TF335941; -.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR Reactome; R-MMU-9696273; RND1 GTPase cycle.
DR Reactome; R-MMU-977068; Termination of O-glycan biosynthesis.
DR BioGRID-ORCS; 17063; 0 hits in 74 CRISPR screens.
DR PRO; PR:P19467; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P19467; protein.
DR Bgee; ENSMUSG00000022824; Expressed in small intestine Peyer's patch and 93 other tissues.
DR ExpressionAtlas; P19467; baseline and differential.
DR Genevisible; P19467; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; ISO:MGI.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR000082; SEA_dom.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00200; SEA; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50024; SEA; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..573
FT /note="Mucin-13"
FT /id="PRO_0000019285"
FT TOPO_DOM 18..480
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 481..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..573
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 233..273
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 274..391
FT /note="SEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 385..425
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 425..467
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 16..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 237..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 242..257
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 259..272
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 389..402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 394..408
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 410..424
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 429..441
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 433..451
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 453..466
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 573 AA; 58701 MW; 1154C4F04E2D58A9 CRC64;
MKGFLLLSLS LLLVTVGSSS QASSTTSSSG GTSPPTTVQS QSPGSSSQAS TTTSSSGGAS
PPTTVQSQSP GSSSQASTTT SSSGGASPPT TVQSQSPGSS SQASTTTSSS GGASPPTTVQ
SQSPGSSSQA STTTSSSGGA SPPTTVQSQS PGSSSQASTT TSSSGGASPP TTVQSQSPGS
SSQVSTTTSS SGGASPPTTV QSQSPGSSSQ PGPTQPSGGA SSSTVPSGGS TGPSDLCNPN
PCKGTASCVK LHSKHFCLCL EGYYYNSSLS SCVKGTTFPG DISMSVSETA NLEDENSVGY
QELYNSVTDF FETTFNKTDY GQTVIIKVST APSRSARSAM RDATKDVSVS VVNIFGADTK
ETEKSVSSAI ETAIKTSGNV KDYVSINLCD HYGCVGNDSS KCQDILQCTC KPGLDRLNPQ
VPFCVAVTCS QPCNAEEKEQ CLKMDNGVMD CVCMPGYQRA NGNRKCEECP FGYSGMNCKD
QFQLILTIVG TIAGALILIL LIAFIVSARS KNKKKDGEEQ RLIEDDFHNL RLRQTGFSNL
GADNSIFPKV RTGVPSQTPN PYANQRSMPR PDY
