MUC24_HUMAN
ID MUC24_HUMAN Reviewed; 197 AA.
AC Q04900; B4DQ85; E1P5E7; E1P5E8; E1P5E9; O95413; Q5JSU6; Q9BPV0; Q9NR26;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Sialomucin core protein 24;
DE Short=MUC-24;
DE AltName: Full=Endolyn;
DE AltName: Full=Multi-glycosylated core protein 24;
DE Short=MGC-24;
DE Short=MGC-24v;
DE AltName: CD_antigen=CD164;
DE Flags: Precursor;
GN Name=CD164;
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] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP GLYCOSYLATION.
RC TISSUE=Gastric carcinoma;
RX PubMed=1478919; DOI=10.1093/oxfordjournals.jbchem.a123948;
RA Masuzawa Y., Miyauchi T., Hamanoue M., Ando S., Yoshida J., Takao S.,
RA Shimazu H., Adachi M., Muramatsu T.;
RT "A novel core protein as well as polymorphic epithelial mucin carry peanut
RT agglutinin binding sites in human gastric carcinoma cells: sequence
RT analysis and examination of gene expression.";
RL J. Biochem. 112:609-615(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Bone marrow;
RX PubMed=9763543;
RA Zannettino A.C.W., Buehring H.-J., Niutta S., Watt S.M., Benton M.A.,
RA Simmons P.J.;
RT "The sialomucin CD164 (MGC-24v) is an adhesive glycoprotein expressed by
RT human hematopoietic progenitors and bone marrow stromal cells that serves
RT as a potent negative regulator of hematopoiesis.";
RL Blood 92:2613-2628(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=10878358; DOI=10.4049/jimmunol.165.2.840;
RA Doyonnas R., Chan J.Y.-H., Butler L.H., Rappold I., Lee-Prudhoe J.E.,
RA Zannettino A.C.W., Simmons P.J., Buehring H.-J., Levesque J.-P., Watt S.M.;
RT "CD164 monoclonal antibodies that block hemopoietic progenitor cell
RT adhesion and proliferation interact with the first mucin domain of the
RT CD164 receptor.";
RL J. Immunol. 165:840-851(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 3 AND 4), ALTERNATIVE
RP SPLICING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11027692; DOI=10.1074/jbc.m007965200;
RA Chan J.Y.-H., Lee-Prudhoe J.E., Jorgensen B., Ihrke G., Doyonnas R.,
RA Zannettino A.C.W., Buckle V.J., Ward C.J., Simmons P.J., Watt S.M.;
RT "Relationship between novel isoforms, functionally important domains, and
RT subcellular distribution of CD164/endolyn.";
RL J. Biol. Chem. 276:2139-2152(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5).
RC TISSUE=Amygdala, Astrocyte, Neutrophil, and 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC 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).
RN [9]
RP FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=16859559; DOI=10.1186/1471-2407-6-195;
RA Havens A.M., Jung Y., Sun Y.X., Wang J., Shah R.B., Buehring H.J.,
RA Pienta K.J., Taichman R.S.;
RT "The role of sialomucin CD164 (MGC-24v or endolyn) in prostate cancer
RT metastasis.";
RL BMC Cancer 6:195-195(2006).
RN [10]
RP FUNCTION, AND INTERACTION WITH CXCR4.
RX PubMed=17077324; DOI=10.1182/blood-2006-05-023028;
RA Forde S., Tye B.J., Newey S.E., Roubelakis M., Smythe J., McGuckin C.P.,
RA Pettengell R., Watt S.M.;
RT "Endolyn (CD164) modulates the CXCL12-mediated migration of umbilical cord
RT blood CD133+ cells.";
RL Blood 109:1825-1833(2007).
RN [11]
RP SUBCELLULAR LOCATION, AND INVOLVEMENT IN DFNA66.
RX PubMed=26197441; DOI=10.1371/journal.pgen.1005386;
RA Nyegaard M., Rendtorff N.D., Nielsen M.S., Corydon T.J., Demontis D.,
RA Starnawska A., Hedemand A., Buniello A., Niola F., Overgaard M.T.,
RA Leal S.M., Ahmad W., Wikman F.P., Petersen K.B., Crueger D.G., Oostrik J.,
RA Kremer H., Tommerup N., Froedin M., Steel K.P., Tranebjaerg L.,
RA Boerglum A.D.;
RT "A novel locus harbouring a functional CD164 nonsense mutation identified
RT in a large Danish family with nonsyndromic hearing impairment.";
RL PLoS Genet. 11:E1005386-E1005386(2015).
CC -!- FUNCTION: Sialomucin that may play a key role in hematopoiesis by
CC facilitating the adhesion of CD34(+) cells to the stroma and by
CC negatively regulating CD34(+)CD38(lo/-) cell proliferation. Modulates
CC the migration of umbilical cord blood CD133+ cells and this is mediated
CC through the CXCL12/CXCR4 axis. May play an important role in prostate
CC cancer metastasis and the infiltration of bone marrow by cancer cells.
CC Promotes myogenesis by enhancing CXCR4-dependent cell motility.
CC Positively regulates myoblast migration and promotes myoblast fusion
CC into myotubes (By similarity). {ECO:0000250|UniProtKB:Q9R0L9,
CC ECO:0000269|PubMed:16859559, ECO:0000269|PubMed:17077324,
CC ECO:0000269|PubMed:9763543}.
CC -!- SUBUNIT: Homodimer (isoform 4). Interacts with CXCR4.
CC {ECO:0000269|PubMed:17077324, ECO:0000269|PubMed:9763543}.
CC -!- INTERACTION:
CC Q04900; P61073: CXCR4; NbExp=2; IntAct=EBI-2115896, EBI-489411;
CC Q04900; P49639: HOXA1; NbExp=3; IntAct=EBI-2115896, EBI-740785;
CC Q04900; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-2115896, EBI-945833;
CC Q04900; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-2115896, EBI-22310682;
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:11027692};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:11027692}.
CC Endosome membrane {ECO:0000269|PubMed:11027692}; Single-pass type I
CC membrane protein {ECO:0000269|PubMed:11027692}. Cell membrane
CC {ECO:0000269|PubMed:11027692, ECO:0000269|PubMed:26197441}; Single-pass
CC type I membrane protein {ECO:0000269|PubMed:11027692}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=CD164(E1-6);
CC IsoId=Q04900-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q04900-2; Sequence=VSP_037974;
CC Name=3; Synonyms=CD164(Delta 4);
CC IsoId=Q04900-3; Sequence=VSP_037972;
CC Name=4; Synonyms=CD164(Delta 5);
CC IsoId=Q04900-4; Sequence=VSP_037973;
CC Name=5;
CC IsoId=Q04900-5; Sequence=VSP_038018, VSP_038019;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 3 are expressed in
CC hematopoietic and non-hematopoietic tissues. Isoform 1 is expressed by
CC prostate cancer tumors and prostate cancer cell lines. The expression
CC is greater in bone metastases than in primary tumors. Expression in
CC osseous metastasis is greater than that in soft tissue metastasis.
CC Isoform 2 is expressed in the small intestine, colon, lung, thyroid and
CC in colorectal and pancreatic adenocarcinoma. Isoform 4 is expressed by
CC both hematopoietic progenitor cells and bone marrow stromal cells.
CC {ECO:0000269|PubMed:10878358, ECO:0000269|PubMed:11027692,
CC ECO:0000269|PubMed:1478919, ECO:0000269|PubMed:16859559,
CC ECO:0000269|PubMed:9763543}.
CC -!- INDUCTION: Up-regulated by CXCL12 in prostate cancer cell lines.
CC {ECO:0000269|PubMed:16859559}.
CC -!- PTM: Highly N- and O-glycosylated; contains sialic acid.
CC {ECO:0000269|PubMed:1478919}.
CC -!- PTM: The motif Ser-Gly may serve as the site of attachment of a
CC glycosaminoglycan side chain.
CC -!- DISEASE: Deafness, autosomal dominant, 66 (DFNA66) [MIM:616969]: A form
CC of non-syndromic sensorineural hearing loss. Sensorineural deafness
CC results from damage to the neural receptors of the inner ear, the nerve
CC pathways to the brain, or the area of the brain that receives sound
CC information. {ECO:0000269|PubMed:26197441}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CD164 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D14043; BAA03130.1; -; mRNA.
DR EMBL; AF106518; AAC82473.1; -; mRNA.
DR EMBL; AF263279; AAF85965.1; -; mRNA.
DR EMBL; AF299341; AAG53906.1; -; mRNA.
DR EMBL; AF299342; AAG53907.1; -; mRNA.
DR EMBL; AF299343; AAG53908.1; -; mRNA.
DR EMBL; AF299340; AAG53903.1; -; Genomic_DNA.
DR EMBL; AF299340; AAG53904.1; -; Genomic_DNA.
DR EMBL; AF299340; AAG53905.1; -; Genomic_DNA.
DR EMBL; AK298684; BAG60847.1; -; mRNA.
DR EMBL; AK303525; BAG64553.1; -; mRNA.
DR EMBL; AK312357; BAG35275.1; -; mRNA.
DR EMBL; AK315908; BAH14279.1; -; mRNA.
DR EMBL; AL359711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48348.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48352.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48349.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48353.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48354.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48355.1; -; Genomic_DNA.
DR EMBL; BC011522; AAH11522.1; -; mRNA.
DR CCDS; CCDS47462.1; -. [Q04900-5]
DR CCDS; CCDS47463.1; -. [Q04900-2]
DR CCDS; CCDS47464.1; -. [Q04900-3]
DR CCDS; CCDS47465.1; -. [Q04900-4]
DR CCDS; CCDS5073.1; -. [Q04900-1]
DR PIR; JX0235; JX0235.
DR RefSeq; NP_001135873.1; NM_001142401.2. [Q04900-3]
DR RefSeq; NP_001135874.1; NM_001142402.2. [Q04900-4]
DR RefSeq; NP_001135875.1; NM_001142403.2. [Q04900-2]
DR RefSeq; NP_001135876.1; NM_001142404.2. [Q04900-5]
DR RefSeq; NP_001333429.1; NM_001346500.1.
DR RefSeq; NP_006007.2; NM_006016.5. [Q04900-1]
DR AlphaFoldDB; Q04900; -.
DR SMR; Q04900; -.
DR BioGRID; 114297; 8.
DR DIP; DIP-43970N; -.
DR IntAct; Q04900; 13.
DR MINT; Q04900; -.
DR STRING; 9606.ENSP00000309376; -.
DR GlyConnect; 1744; 5 N-Linked glycans (2 sites).
DR GlyGen; Q04900; 13 sites, 5 N-linked glycans (2 sites), 3 O-linked glycans (2 sites).
DR iPTMnet; Q04900; -.
DR PhosphoSitePlus; Q04900; -.
DR SwissPalm; Q04900; -.
DR BioMuta; CD164; -.
DR DMDM; 257051036; -.
DR CPTAC; CPTAC-1481; -.
DR MassIVE; Q04900; -.
DR MaxQB; Q04900; -.
DR PaxDb; Q04900; -.
DR PeptideAtlas; Q04900; -.
DR PRIDE; Q04900; -.
DR ProteomicsDB; 58289; -. [Q04900-1]
DR ProteomicsDB; 58290; -. [Q04900-2]
DR ProteomicsDB; 58291; -. [Q04900-3]
DR ProteomicsDB; 58292; -. [Q04900-4]
DR ProteomicsDB; 58293; -. [Q04900-5]
DR Antibodypedia; 2460; 285 antibodies from 28 providers.
DR DNASU; 8763; -.
DR Ensembl; ENST00000275080.11; ENSP00000275080.7; ENSG00000135535.17. [Q04900-3]
DR Ensembl; ENST00000310786.10; ENSP00000309376.4; ENSG00000135535.17. [Q04900-1]
DR Ensembl; ENST00000324953.9; ENSP00000314177.5; ENSG00000135535.17. [Q04900-4]
DR Ensembl; ENST00000413644.6; ENSP00000402237.2; ENSG00000135535.17. [Q04900-2]
DR Ensembl; ENST00000512821.5; ENSP00000427546.1; ENSG00000135535.17. [Q04900-5]
DR GeneID; 8763; -.
DR KEGG; hsa:8763; -.
DR MANE-Select; ENST00000310786.10; ENSP00000309376.4; NM_006016.6; NP_006007.2.
DR UCSC; uc003ptd.4; human. [Q04900-1]
DR CTD; 8763; -.
DR DisGeNET; 8763; -.
DR GeneCards; CD164; -.
DR HGNC; HGNC:1632; CD164.
DR HPA; ENSG00000135535; Low tissue specificity.
DR MalaCards; CD164; -.
DR MIM; 603356; gene.
DR MIM; 616969; phenotype.
DR neXtProt; NX_Q04900; -.
DR OpenTargets; ENSG00000135535; -.
DR Orphanet; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
DR PharmGKB; PA26191; -.
DR VEuPathDB; HostDB:ENSG00000135535; -.
DR eggNOG; ENOG502S7HA; Eukaryota.
DR GeneTree; ENSGT00530000063929; -.
DR HOGENOM; CLU_101414_0_0_1; -.
DR InParanoid; Q04900; -.
DR OrthoDB; 1643926at2759; -.
DR PhylomeDB; Q04900; -.
DR TreeFam; TF333380; -.
DR PathwayCommons; Q04900; -.
DR SignaLink; Q04900; -.
DR BioGRID-ORCS; 8763; 20 hits in 1077 CRISPR screens.
DR ChiTaRS; CD164; human.
DR GeneWiki; CD164; -.
DR GenomeRNAi; 8763; -.
DR Pharos; Q04900; Tbio.
DR PRO; PR:Q04900; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q04900; protein.
DR Bgee; ENSG00000135535; Expressed in mucosa of sigmoid colon and 213 other tissues.
DR ExpressionAtlas; Q04900; baseline and differential.
DR Genevisible; Q04900; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR GO; GO:0030097; P:hemopoiesis; NAS:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:MGI.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0007162; P:negative regulation of cell adhesion; NAS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR007947; CD164_MGC24.
DR PANTHER; PTHR11337; PTHR11337; 1.
DR Pfam; PF05283; MGC-24; 1.
DR PRINTS; PR01701; CD164ANTIGEN.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Deafness; Endosome;
KW Glycoprotein; Lysosome; Membrane; Myogenesis; Non-syndromic deafness;
KW Proteoglycan; Reference proteome; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..197
FT /note="Sialomucin core protein 24"
FT /id="PRO_0000019292"
FT TOPO_DOM 24..162
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 118..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..197
FT /note="Required for endosomal and lysosomal localization"
FT /evidence="ECO:0000250"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="O-linked (Xyl...) (glycosaminoglycan) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 111..123
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11027692,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_037972"
FT VAR_SEQ 124..142
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11027692,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:9763543"
FT /id="VSP_037973"
FT VAR_SEQ 143..157
FT /note="GTTNNTVTPTSQPVR -> EIRCHTRNYIPDLKK (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038018"
FT VAR_SEQ 158..197
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038019"
FT VAR_SEQ 175..197
FT /note="GVQAVIFFLYKFCKSKERNYHTL -> EIRCHTRNYIPDLKK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:1478919"
FT /id="VSP_037974"
SQ SEQUENCE 197 AA; 20917 MW; 4855E02646F4CB35 CRC64;
MSRLSRSLLW AATCLGVLCV LSADKNTTQH PNVTTLAPIS NVTSAPVTSL PLVTTPAPET
CEGRNSCVSC FNVSVVNTTC FWIECKDESY CSHNSTVSDC QVGNTTDFCS VSTATPVPTA
NSTAKPTVQP SPSTTSKTVT TSGTTNNTVT PTSQPVRKST FDAASFIGGI VLVLGVQAVI
FFLYKFCKSK ERNYHTL
