MUC15_HUMAN
ID MUC15_HUMAN Reviewed; 334 AA.
AC Q8N387; B3KY00; E9PII6; F8W945; Q6UWS3; Q8IXI8; Q8WW41;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Mucin-15;
DE Short=MUC-15;
DE Flags: Precursor;
GN Name=MUC15; ORFNames=UNQ750/PRO1481;
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] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP VARIANT ILE-202.
RC TISSUE=Lactating mammary gland;
RX PubMed=12047385; DOI=10.1046/j.1432-1033.2002.02949.x;
RA Pallesen L.T., Berglund L., Rasmussen L.K., Petersen T.E., Rasmussen J.T.;
RT "Isolation and characterization of MUC15, a novel cell membrane associated
RT mucin.";
RL Eur. J. Biochem. 269:2755-2763(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thymus;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-202.
RC TISSUE=Placenta;
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 play a role in the cell adhesion to the extracellular
CC matrix.
CC -!- INTERACTION:
CC Q8N387; P07766: CD3E; NbExp=3; IntAct=EBI-17937277, EBI-1211297;
CC Q8N387; P34972: CNR2; NbExp=3; IntAct=EBI-17937277, EBI-2835940;
CC Q8N387; P13473-2: LAMP2; NbExp=3; IntAct=EBI-17937277, EBI-21591415;
CC Q8N387; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-17937277, EBI-2623095;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000305}; Single-
CC pass type I membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=MUC15;
CC IsoId=Q8N387-1; Sequence=Displayed;
CC Name=2; Synonyms=MUC15/S;
CC IsoId=Q8N387-2; Sequence=VSP_010825;
CC -!- TISSUE SPECIFICITY: Expressed in spleen, thymus, prostate, testis,
CC ovary, small intestine, colon, peripheral blood leukocyte, bone marrow,
CC lymph node and lung. {ECO:0000269|PubMed:12047385}.
CC -!- PTM: Highly glycosylated (N- and O-linked carbohydrates).
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH20912.2; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Mucin database;
CC URL="http://www.medkem.gu.se/mucinbiology/databases/";
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DR EMBL; AJ417818; CAD10624.1; -; mRNA.
DR EMBL; AJ507429; CAD45555.1; -; mRNA.
DR EMBL; AY358668; AAQ89031.1; -; mRNA.
DR EMBL; AK128337; BAG54662.1; -; mRNA.
DR EMBL; AC036114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC020912; AAH20912.2; ALT_SEQ; mRNA.
DR EMBL; BC058007; AAH58007.1; -; mRNA.
DR CCDS; CCDS7859.1; -. [Q8N387-1]
DR RefSeq; NP_001128563.1; NM_001135091.1.
DR RefSeq; NP_001128564.1; NM_001135092.1.
DR RefSeq; NP_663625.2; NM_145650.3. [Q8N387-1]
DR AlphaFoldDB; Q8N387; -.
DR BioGRID; 126813; 5.
DR IntAct; Q8N387; 6.
DR STRING; 9606.ENSP00000416753; -.
DR GlyGen; Q8N387; 9 sites.
DR iPTMnet; Q8N387; -.
DR PhosphoSitePlus; Q8N387; -.
DR BioMuta; MUC15; -.
DR DMDM; 84028223; -.
DR MassIVE; Q8N387; -.
DR PaxDb; Q8N387; -.
DR PeptideAtlas; Q8N387; -.
DR PRIDE; Q8N387; -.
DR ProteomicsDB; 20820; -.
DR ProteomicsDB; 30258; -.
DR ProteomicsDB; 71777; -. [Q8N387-1]
DR ProteomicsDB; 71778; -. [Q8N387-2]
DR Antibodypedia; 12684; 143 antibodies from 28 providers.
DR DNASU; 143662; -.
DR Ensembl; ENST00000455601.6; ENSP00000397339.2; ENSG00000169550.14. [Q8N387-1]
DR GeneID; 143662; -.
DR KEGG; hsa:143662; -.
DR UCSC; uc001mqx.4; human. [Q8N387-1]
DR CTD; 143662; -.
DR DisGeNET; 143662; -.
DR GeneCards; MUC15; -.
DR HGNC; HGNC:14956; MUC15.
DR HPA; ENSG00000169550; Tissue enriched (epididymis).
DR MIM; 608566; gene.
DR neXtProt; NX_Q8N387; -.
DR OpenTargets; ENSG00000169550; -.
DR PharmGKB; PA31313; -.
DR VEuPathDB; HostDB:ENSG00000169550; -.
DR eggNOG; ENOG502S7P0; Eukaryota.
DR GeneTree; ENSGT00390000001698; -.
DR HOGENOM; CLU_054055_0_0_1; -.
DR InParanoid; Q8N387; -.
DR OMA; PDEWLTT; -.
DR OrthoDB; 1263362at2759; -.
DR PhylomeDB; Q8N387; -.
DR TreeFam; TF338656; -.
DR PathwayCommons; Q8N387; -.
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-977068; Termination of O-glycan biosynthesis.
DR SignaLink; Q8N387; -.
DR BioGRID-ORCS; 143662; 9 hits in 1064 CRISPR screens.
DR ChiTaRS; MUC15; human.
DR GenomeRNAi; 143662; -.
DR Pharos; Q8N387; Tbio.
DR PRO; PR:Q8N387; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8N387; protein.
DR Bgee; ENSG00000169550; Expressed in corpus epididymis and 101 other tissues.
DR ExpressionAtlas; Q8N387; baseline and differential.
DR Genevisible; Q8N387; HS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 InterPro; IPR031371; Mucin-15.
DR PANTHER; PTHR45427; PTHR45427; 1.
DR Pfam; PF15672; Mucin15; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000250"
FT CHAIN 24..334
FT /note="Mucin-15"
FT /id="PRO_0000019288"
FT TOPO_DOM 24..236
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 64..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 232..281
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12047385"
FT /id="VSP_010825"
FT VARIANT 19
FT /note="S -> W (in dbSNP:rs293979)"
FT /id="VAR_050452"
FT VARIANT 184
FT /note="I -> T (in dbSNP:rs2292290)"
FT /id="VAR_019376"
FT VARIANT 202
FT /note="T -> I (in dbSNP:rs15783)"
FT /evidence="ECO:0000269|PubMed:12047385,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_019377"
FT CONFLICT 143
FT /note="A -> T (in Ref. 1; CAD45555)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 36294 MW; 3CA38EEB40D533F1 CRC64;
MLALAKILLI STLFYSLLSG SHGKENQDIN TTQNIAEVFK TMENKPISLE SEANLNSDKE
NITTSNLKAS HSPPLNLPNN SHGITDFSSN SSAEHSLGSL KPTSTISTSP PLIHSFVSKV
PWNAPIADED LLPISAHPNA TPALSSENFT WSLVNDTVKT PDNSSITVSI LSSEPTSPSV
TPLIVEPSGW LTTNSDSFTG FTPYQEKTTL QPTLKFTNNS KLFPNTSDPQ KENRNTGIVF
GAILGAILGV SLLTLVGYLL CGKRKTDSFS HRRLYDDRNE PVLRLDNAPE PYDVSFGNSS
YYNPTLNDSA MPESEENARD GIPMDDIPPL RTSV
