MUC13_HUMAN
ID MUC13_HUMAN Reviewed; 512 AA.
AC Q9H3R2; Q6UWD9; Q9NXT5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 14-MAY-2014, sequence version 3.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Mucin-13;
DE Short=MUC-13;
DE AltName: Full=Down-regulated in colon cancer 1;
DE Flags: Precursor;
GN Name=MUC13; Synonyms=DRCC1, RECC; ORFNames=UNQ6194/PRO20221;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Masayoshi I., Furukawa Y., Akashi H., Han H., Nakajima Y., Sugano S.,
RA Ogawa M., Nakamura Y.;
RT "Isolation and characterization of a novel human gene DRCC1 encoding a
RT mucin-like glycoprotein, homologous to murine cell surface antigen 114/A10,
RT and its reduced expression in colorectal cancers.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTRACELLULAR CLEAVAGE, SUBUNIT, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION.
RX PubMed=11278439; DOI=10.1074/jbc.m008850200;
RA Williams S.J., Wreschner D.H., Tran M., Eyre H.J., Sutherland G.R.,
RA McGuckin M.A.;
RT "Muc13, a novel human cell surface mucin expressed by epithelial and
RT hemopoietic cells.";
RL J. Biol. Chem. 276:18327-18336(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-503.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 196-512.
RC TISSUE=Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
CC -!- FUNCTION: Epithelial and hemopoietic transmembrane mucin that may play
CC a role in cell signaling.
CC -!- SUBUNIT: Homodimer of beta subunits. {ECO:0000269|PubMed:11278439}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11278439};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:11278439}.
CC Apical cell membrane {ECO:0000269|PubMed:11278439}. Secreted
CC {ECO:0000269|PubMed:11278439}. Note=Also exists as a soluble form.
CC -!- TISSUE SPECIFICITY: Highly expressed in epithelial tissues,
CC particularly those of the gastrointestinal and respiratory tracts, such
CC as large intestine and trachea, followed by kidney, small intestine,
CC appendix and stomach. {ECO:0000269|PubMed:11278439}.
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.
CC -!- PTM: Highly N-glycosylated. {ECO:0000269|PubMed:11278439}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA90925.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Mucin database;
CC URL="http://www.medkem.gu.se/mucinbiology/databases/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MUC13ID41454ch3q21.html";
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DR EMBL; AB035807; BAB19651.1; -; mRNA.
DR EMBL; AF286113; AAK56861.1; -; mRNA.
DR EMBL; AY358831; AAQ89190.1; -; mRNA.
DR EMBL; AC026342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK000070; BAA90925.1; ALT_INIT; mRNA.
DR CCDS; CCDS33839.2; -.
DR RefSeq; NP_149038.3; NM_033049.3.
DR AlphaFoldDB; Q9H3R2; -.
DR SMR; Q9H3R2; -.
DR BioGRID; 121177; 38.
DR IntAct; Q9H3R2; 18.
DR STRING; 9606.ENSP00000485028; -.
DR GlyGen; Q9H3R2; 6 sites.
DR iPTMnet; Q9H3R2; -.
DR PhosphoSitePlus; Q9H3R2; -.
DR BioMuta; MUC13; -.
DR DMDM; 296438300; -.
DR jPOST; Q9H3R2; -.
DR MassIVE; Q9H3R2; -.
DR MaxQB; Q9H3R2; -.
DR PaxDb; Q9H3R2; -.
DR PeptideAtlas; Q9H3R2; -.
DR PRIDE; Q9H3R2; -.
DR ProteomicsDB; 80744; -.
DR Antibodypedia; 33002; 321 antibodies from 31 providers.
DR DNASU; 56667; -.
DR Ensembl; ENST00000616727.4; ENSP00000485028.1; ENSG00000173702.7.
DR GeneID; 56667; -.
DR KEGG; hsa:56667; -.
DR MANE-Select; ENST00000616727.4; ENSP00000485028.1; NM_033049.4; NP_149038.3.
DR UCSC; uc032sai.1; human.
DR CTD; 56667; -.
DR DisGeNET; 56667; -.
DR GeneCards; MUC13; -.
DR HGNC; HGNC:7511; MUC13.
DR HPA; ENSG00000173702; Tissue enriched (intestine).
DR MIM; 612181; gene.
DR neXtProt; NX_Q9H3R2; -.
DR OpenTargets; ENSG00000173702; -.
DR PharmGKB; PA31312; -.
DR VEuPathDB; HostDB:ENSG00000173702; -.
DR eggNOG; ENOG502S3PG; Eukaryota.
DR GeneTree; ENSGT00940000154419; -.
DR HOGENOM; CLU_020534_1_0_1; -.
DR InParanoid; Q9H3R2; -.
DR OMA; GYQEDAN; -.
DR OrthoDB; 1023611at2759; -.
DR TreeFam; TF335941; -.
DR PathwayCommons; Q9H3R2; -.
DR Reactome; R-HSA-5083625; Defective GALNT3 causes HFTC.
DR Reactome; R-HSA-5083632; Defective C1GALT1C1 causes TNPS.
DR Reactome; R-HSA-5083636; Defective GALNT12 causes CRCS1.
DR Reactome; R-HSA-5621480; Dectin-2 family.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR Reactome; R-HSA-9696273; RND1 GTPase cycle.
DR Reactome; R-HSA-977068; Termination of O-glycan biosynthesis.
DR SignaLink; Q9H3R2; -.
DR BioGRID-ORCS; 56667; 4 hits in 248 CRISPR screens.
DR ChiTaRS; MUC13; human.
DR GenomeRNAi; 56667; -.
DR Pharos; Q9H3R2; Tbio.
DR PRO; PR:Q9H3R2; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9H3R2; protein.
DR Bgee; ENSG00000173702; Expressed in jejunal mucosa and 134 other tissues.
DR ExpressionAtlas; Q9H3R2; baseline and differential.
DR Genevisible; Q9H3R2; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IMP:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IMP:UniProtKB.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR000082; SEA_dom.
DR Pfam; PF01390; SEA; 1.
DR SMART; SM00181; EGF; 3.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50024; SEA; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..512
FT /note="Mucin-13"
FT /id="PRO_0000019284"
FT TOPO_DOM 19..421
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..512
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 173..211
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 212..336
FT /note="SEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 322..361
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 363..404
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 22..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 177..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 182..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 199..210
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 326..338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 331..344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 346..360
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 367..378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 371..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 391..403
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VARIANT 18
FT /note="A -> V (in dbSNP:rs4679394)"
FT /id="VAR_056589"
FT VARIANT 100
FT /note="I -> T (in dbSNP:rs4679392)"
FT /id="VAR_063124"
FT VARIANT 364
FT /note="S -> G (in dbSNP:rs16836185)"
FT /id="VAR_056590"
FT VARIANT 503
FT /note="R -> S (in dbSNP:rs1127233)"
FT /evidence="ECO:0000269|PubMed:12975309"
FT /id="VAR_056591"
FT CONFLICT 196
FT /note="F -> I (in Ref. 5; BAA90925)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 54604 MW; 17D34E17B1637581 CRC64;
MKAIIHLTLL ALLSVNTATN QGNSADAVTT TETATSGPTV AAADTTETNF PETASTTANT
PSFPTATSPA PPIISTHSSS TIPTPAPPII STHSSSTIPI PTAADSESTT NVNSLATSDI
ITASSPNDGL ITMVPSETQS NNEMSPTTED NQSSGPPTGT ALLETSTLNS TGPSNPCQDD
PCADNSLCVK LHNTSFCLCL EGYYYNSSTC KKGKVFPGKI SVTVSETFDP EEKHSMAYQD
LHSEITSLFK DVFGTSVYGQ TVILTVSTSL SPRSEMRADD KFVNVTIVTI LAETTSDNEK
TVTEKINKAI RSSSSNFLNY DLTLRCDYYG CNQTADDCLN GLACDCKSDL QRPNPQSPFC
VASSLKCPDA CNAQHKQCLI KKSGGAPECA CVPGYQEDAN GNCQKCAFGY SGLDCKDKFQ
LILTIVGTIA GIVILSMIIA LIVTARSNNK TKHIEEENLI DEDFQNLKLR STGFTNLGAE
GSVFPKVRIT ASRDSQMQNP YSRHSSMPRP DY
