MUC7_HUMAN
ID MUC7_HUMAN Reviewed; 377 AA.
AC Q8TAX7; Q9UCD7; Q9UCD8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Mucin-7;
DE Short=MUC-7;
DE AltName: Full=Apo-MG2;
DE AltName: Full=Salivary mucin-7;
DE Flags: Precursor;
GN Name=MUC7; Synonyms=MG2;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Submandibular gland;
RX PubMed=7690757; DOI=10.1016/s0021-9258(20)80762-5;
RA Bobek L.A., Tsai H., Biesbrock A.R., Levine M.J.;
RT "Molecular cloning, sequence, and specificity of expression of the gene
RT encoding the low molecular weight human salivary mucin (MUC7).";
RL J. Biol. Chem. 268:20563-20569(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [4]
RP PROTEIN SEQUENCE OF 70-92 AND 143-168, AND TISSUE SPECIFICITY.
RC TISSUE=Saliva;
RX PubMed=1445223; DOI=10.1042/bj2870639;
RA Reddy M.S., Bobek L.A., Haraszthy G.G., Biesbrock A.R., Levine M.J.;
RT "Structural features of the low-molecular-mass human salivary mucin.";
RL Biochem. J. 287:639-643(1992).
RN [5]
RP PROTEIN SEQUENCE OF 93-112 AND 143-168, FUNCTION, AND GLYCOSYLATION.
RC TISSUE=Saliva;
RX PubMed=8104046; DOI=10.1177/10454411930040030901;
RA Reddy M.S., Levine M.J., Paranchych W.;
RT "Low-molecular-mass human salivary mucin, MG2: structure and binding of
RT Pseudomonas aeruginosa.";
RL Crit. Rev. Oral Biol. Med. 4:315-323(1993).
RN [6]
RP FUNCTION, POLYMORPHISM, AND INVOLVEMENT IN SUSCEPTIBILITY TO ASTHMA.
RX PubMed=11378823; DOI=10.1038/sj.ejhg.5200642;
RA Kirkbride H.J., Bolscher J.G., Nazmi K., Vinall L.E., Nash M.W., Moss F.M.,
RA Mitchell D.M., Swallow D.M.;
RT "Genetic polymorphism of MUC7: allele frequencies and association with
RT asthma.";
RL Eur. J. Hum. Genet. 9:347-354(2001).
RN [7]
RP GLYCOSYLATION AT THR-176; SER-182; SER-183; THR-188 AND THR-189.
RX PubMed=12407114; DOI=10.1074/jbc.m203094200;
RA Zhang Y., Iwasaki H., Wang H., Kudo T., Kalka T.B., Hennet T., Kubota T.,
RA Cheng L., Inaba N., Gotoh M., Togayachi A., Guo J.-M., Hisatomi H.,
RA Nakajima K., Nishihara S., Nakamura M., Marth J.D., Narimatsu H.;
RT "Cloning and characterization of a new human UDP-N-acetyl-alpha-D-
RT galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-
RT GalNAc-T13, that is specifically expressed in neurons and synthesizes
RT GalNAc alpha-serine/threonine antigen.";
RL J. Biol. Chem. 278:573-584(2003).
CC -!- FUNCTION: May function in a protective capacity by promoting the
CC clearance of bacteria in the oral cavity and aiding in mastication,
CC speech, and swallowing. Binds P.aeruginosa pili.
CC {ECO:0000269|PubMed:11378823, ECO:0000269|PubMed:8104046}.
CC -!- SUBUNIT: Monomer.
CC -!- INTERACTION:
CC Q8TAX7; P04745: AMY1A; NbExp=2; IntAct=EBI-738582, EBI-738586;
CC Q8TAX7; P15515: HTN1; NbExp=2; IntAct=EBI-738582, EBI-738638;
CC Q8TAX7; P02810: PRH2; NbExp=2; IntAct=EBI-738582, EBI-738601;
CC Q8TAX7; P02808: STATH; NbExp=2; IntAct=EBI-738582, EBI-738687;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7690757}.
CC -!- TISSUE SPECIFICITY: Expressed in salivary gland tissues and only in
CC those that contain mucous acinar cells (e.g. sublingual and
CC submandibular glands) and not in salivary glands containing only serous
CC acinar cells (e.g. parotid gland). {ECO:0000269|PubMed:1445223,
CC ECO:0000269|PubMed:7690757}.
CC -!- PTM: N- and O-glycosylated. Contains fucose, mannose, galactose, N-
CC acetylglucosamine and N-acetylgalactosamine.
CC {ECO:0000269|PubMed:8104046}.
CC -!- POLYMORPHISM: The most common allele, MUC7*6, contains a tandem repeat
CC domain comprising 6 repeats (shown here) each composed of 23 amino
CC acids. These repeats are very similar but not identical. In a large
CC cohort of 375 individuals from a variety of ethnic backgrounds, three
CC different alleles were detected, MUC7*6 being the most common, in all
CC populations studied, followed by MUC7*5 (5 repeats), with frequency
CC varying from 0.05 in Africans to 0.22 in East Asians. The MUC7*5 allele
CC is less prevalent in patients with asthma than in controls, and seems
CC to have a protective role in respiratory function. MUC7*8 (8 repeats),
CC a novel rare allele, was identified in 1 Northern European individual.
CC -!- DISEASE: Asthma (ASTHMA) [MIM:600807]: The most common chronic disease
CC affecting children and young adults. It is a complex genetic disorder
CC with a heterogeneous phenotype, largely attributed to the interactions
CC among many genes and between these genes and the environment. It is
CC characterized by recurrent attacks of paroxysmal dyspnea, with wheezing
CC due to spasmodic contraction of the bronchi.
CC {ECO:0000269|PubMed:11378823}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=Mucin database;
CC URL="http://www.medkem.gu.se/mucinbiology/databases/";
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DR EMBL; AC106884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025688; AAH25688.1; -; mRNA.
DR CCDS; CCDS3541.1; -.
DR PIR; A48018; A48018.
DR RefSeq; NP_001138478.1; NM_001145006.1.
DR RefSeq; NP_001138479.1; NM_001145007.1.
DR RefSeq; NP_689504.2; NM_152291.2.
DR AlphaFoldDB; Q8TAX7; -.
DR BMRB; Q8TAX7; -.
DR BioGRID; 110676; 27.
DR IntAct; Q8TAX7; 20.
DR STRING; 9606.ENSP00000407422; -.
DR GlyConnect; 418; 14 O-Linked glycans.
DR GlyGen; Q8TAX7; 5 sites, 21 O-linked glycans (1 site).
DR BioMuta; MUC7; -.
DR DMDM; 296439230; -.
DR MassIVE; Q8TAX7; -.
DR PaxDb; Q8TAX7; -.
DR PeptideAtlas; Q8TAX7; -.
DR PRIDE; Q8TAX7; -.
DR ProteomicsDB; 73933; -.
DR Antibodypedia; 1459; 158 antibodies from 25 providers.
DR DNASU; 4589; -.
DR Ensembl; ENST00000304887.6; ENSP00000302021.5; ENSG00000171195.11.
DR Ensembl; ENST00000413702.5; ENSP00000407422.1; ENSG00000171195.11.
DR Ensembl; ENST00000456088.5; ENSP00000400585.1; ENSG00000171195.11.
DR GeneID; 4589; -.
DR KEGG; hsa:4589; -.
DR MANE-Select; ENST00000304887.6; ENSP00000302021.5; NM_152291.3; NP_689504.2.
DR UCSC; uc003hfj.3; human.
DR CTD; 4589; -.
DR DisGeNET; 4589; -.
DR GeneCards; MUC7; -.
DR HGNC; HGNC:7518; MUC7.
DR HPA; ENSG00000171195; Tissue enriched (salivary).
DR MalaCards; MUC7; -.
DR MIM; 158375; gene.
DR MIM; 600807; phenotype.
DR neXtProt; NX_Q8TAX7; -.
DR OpenTargets; ENSG00000171195; -.
DR PharmGKB; PA31323; -.
DR VEuPathDB; HostDB:ENSG00000171195; -.
DR eggNOG; ENOG502QU51; Eukaryota.
DR GeneTree; ENSGT00730000111663; -.
DR HOGENOM; CLU_063474_0_0_1; -.
DR InParanoid; Q8TAX7; -.
DR OMA; SIGTNCL; -.
DR OrthoDB; 1448371at2759; -.
DR PhylomeDB; Q8TAX7; -.
DR TreeFam; TF341506; -.
DR PathwayCommons; Q8TAX7; -.
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; Q8TAX7; -.
DR BioGRID-ORCS; 4589; 12 hits in 1042 CRISPR screens.
DR ChiTaRS; MUC7; human.
DR GeneWiki; MUC7; -.
DR GenomeRNAi; 4589; -.
DR Pharos; Q8TAX7; Tbio.
DR PRO; PR:Q8TAX7; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q8TAX7; protein.
DR Bgee; ENSG00000171195; Expressed in trachea and 98 other tissues.
DR ExpressionAtlas; Q8TAX7; baseline and differential.
DR Genevisible; Q8TAX7; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR InterPro; IPR033529; MUC7.
DR PANTHER; PTHR41683; PTHR41683; 1.
PE 1: Evidence at protein level;
KW Asthma; Direct protein sequencing; Glycoprotein; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..377
FT /note="Mucin-7"
FT /id="PRO_0000239228"
FT REPEAT 165..187
FT /note="1"
FT REPEAT 188..210
FT /note="2"
FT REPEAT 211..233
FT /note="3"
FT REPEAT 234..256
FT /note="4"
FT REPEAT 257..279
FT /note="5"
FT REPEAT 280..302
FT /note="6"
FT REGION 70..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..92
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..199
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..245
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..301
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="O-linked (GalNAc) threonine; by GALNT13"
FT /evidence="ECO:0000269|PubMed:12407114"
FT CARBOHYD 182
FT /note="O-linked (GalNAc) serine; by GALNT13"
FT /evidence="ECO:0000269|PubMed:12407114"
FT CARBOHYD 183
FT /note="O-linked (GalNAc) serine; by GALNT13"
FT /evidence="ECO:0000269|PubMed:12407114"
FT CARBOHYD 188
FT /note="O-linked (GalNAc) threonine; by GALNT13"
FT /evidence="ECO:0000269|PubMed:12407114"
FT CARBOHYD 189
FT /note="O-linked (GalNAc) threonine; by GALNT13"
FT /evidence="ECO:0000269|PubMed:12407114"
FT VARIANT 80
FT /note="N -> K (in dbSNP:rs6826961)"
FT /id="VAR_050451"
FT CONFLICT 70
FT /note="C -> S (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="K -> P (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="P -> A (in Ref. 4; AA sequence and 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="T -> I (in Ref. 3; AAH25688)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 39159 MW; 1BF92D1855C13F4A CRC64;
MKTLPLFVCI CALSACFSFS EGRERDHELR HRRHHHQSPK SHFELPHYPG LLAHQKPFIR
KSYKCLHKRC RPKLPPSPNN PPKFPNPHQP PKHPDKNSSV VNPTLVATTQ IPSVTFPSAS
TKITTLPNVT FLPQNATTIS SRENVNTSSS VATLAPVNSP APQDTTAAPP TPSATTPAPP
SSSAPPETTA APPTPSATTQ APPSSSAPPE TTAAPPTPPA TTPAPPSSSA PPETTAAPPT
PSATTPAPLS SSAPPETTAV PPTPSATTLD PSSASAPPET TAAPPTPSAT TPAPPSSPAP
QETTAAPITT PNSSPTTLAP DTSETSAAPT HQTTTSVTTQ TTTTKQPTSA PGQNKISRFL
LYMKNLLNRI IDDMVEQ
