MUC24_MOUSE
ID MUC24_MOUSE Reviewed; 197 AA.
AC Q9R0L9; Q3UM47; Q9Z317;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
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 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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=10491205; DOI=10.1046/j.1432-1327.1999.00777.x;
RA Kurosawa N., Kanemitsu Y., Matsui T., Shimada K., Ishihama H.,
RA Muramatsu T.;
RT "Genomic analysis of a murine cell-surface sialomucin, MGC-24/CD164.";
RL Eur. J. Biochem. 265:466-472(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], 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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR; TISSUE=Brain;
RA Kurosawa N., Matsui T., Muramatsu T.;
RT "Mouse MGC-24v.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [6]
RP FUNCTION, INTERACTION WITH CXCR4, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP ASN-193 AND TYR-194.
RX PubMed=18227060; DOI=10.1074/jbc.m706730200;
RA Bae G.-U., Gaio U., Yang Y.-J., Lee H.-J., Kang J.-S., Krauss R.S.;
RT "Regulation of myoblast motility and fusion by the CXCR4-associated
RT sialomucin, CD164.";
RL J. Biol. Chem. 283:8301-8309(2008).
RN [7]
RP TISSUE SPECIFICITY.
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. May be
CC involved in cell adhesion (By similarity). Promotes myogenesis by
CC enhancing CXCR4-dependent cell motility. Positively regulates myoblast
CC migration and promotes myoblast fusion into myotubes.
CC {ECO:0000250|UniProtKB:Q04900, ECO:0000269|PubMed:18227060}.
CC -!- SUBUNIT: Interacts with CXCR4. {ECO:0000269|PubMed:18227060}.
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q04900};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q04900}.
CC Endosome membrane {ECO:0000250|UniProtKB:Q04900}; Single-pass type I
CC membrane protein {ECO:0000250|UniProtKB:Q04900}. Cell membrane
CC {ECO:0000250|UniProtKB:Q04900}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q04900}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the submaxillary gland
CC and kidney, at moderate levels in the brain, heart, lung, liver,
CC intestine, testis, muscle and bone marrow, and at low levels in the
CC pancreas, spleen and thymus. In the ear, expressed in the inner and
CC outer hair cells of the organ of Corti, cells of Kolliker's organ,
CC cells in the lateral cochlear wall behind the spiral prominence and
CC cells of the stria vascularis (PubMed:26197441).
CC {ECO:0000269|PubMed:10491205, ECO:0000269|PubMed:11027692,
CC ECO:0000269|PubMed:26197441}.
CC -!- DEVELOPMENTAL STAGE: During embryogenesis, expression in found in all
CC stages examined, with the highest levels of expression at early stages
CC (8.5 dpc) and moderate levels of expression being found at mid- to late
CC stages of embryogenesis. Expressed during early stages of skeletal
CC muscle development. At embryonic stages 9.5 dpc and 10.5 dpc, expressed
CC strongly in the dorsal somite (the structure of origin for skeletal
CC muscle precursors). It is also expressed at later stages of muscle
CC development;. {ECO:0000269|PubMed:10491205,
CC ECO:0000269|PubMed:18227060}.
CC -!- PTM: Highly N- and O-glycosylated; contains sialic acid. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CD164 family. {ECO:0000305}.
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DR EMBL; AB028895; BAA78909.1; -; mRNA.
DR EMBL; AF299345; AAG53910.1; -; mRNA.
DR EMBL; AF299344; AAG53909.1; -; Genomic_DNA.
DR EMBL; AB014464; BAA34547.1; -; mRNA.
DR EMBL; AK145131; BAE26251.1; -; mRNA.
DR EMBL; AK169275; BAE41034.1; -; mRNA.
DR EMBL; BC005414; AAH05414.1; -; mRNA.
DR CCDS; CCDS23806.1; -.
DR RefSeq; NP_058594.1; NM_016898.2.
DR AlphaFoldDB; Q9R0L9; -.
DR SMR; Q9R0L9; -.
DR IntAct; Q9R0L9; 1.
DR STRING; 10090.ENSMUSP00000019962; -.
DR GlyGen; Q9R0L9; 9 sites.
DR PhosphoSitePlus; Q9R0L9; -.
DR PaxDb; Q9R0L9; -.
DR PRIDE; Q9R0L9; -.
DR ProteomicsDB; 291458; -.
DR Antibodypedia; 2460; 285 antibodies from 28 providers.
DR DNASU; 53599; -.
DR Ensembl; ENSMUST00000019962; ENSMUSP00000019962; ENSMUSG00000019818.
DR GeneID; 53599; -.
DR KEGG; mmu:53599; -.
DR UCSC; uc007exv.1; mouse.
DR CTD; 8763; -.
DR MGI; MGI:1859568; Cd164.
DR VEuPathDB; HostDB:ENSMUSG00000019818; -.
DR eggNOG; ENOG502S7HA; Eukaryota.
DR GeneTree; ENSGT00530000063929; -.
DR HOGENOM; CLU_101414_0_0_1; -.
DR InParanoid; Q9R0L9; -.
DR OMA; CYWIECK; -.
DR OrthoDB; 1643926at2759; -.
DR PhylomeDB; Q9R0L9; -.
DR TreeFam; TF333380; -.
DR BioGRID-ORCS; 53599; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Cd164; mouse.
DR PRO; PR:Q9R0L9; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9R0L9; protein.
DR Bgee; ENSMUSG00000019818; Expressed in parotid gland and 283 other tissues.
DR ExpressionAtlas; Q9R0L9; baseline and differential.
DR Genevisible; Q9R0L9; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:MGI.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
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 Cell adhesion; Cell membrane; Endosome; Glycoprotein; Lysosome; Membrane;
KW Myogenesis; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..197
FT /note="Sialomucin core protein 24"
FT /id="PRO_0000383341"
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 116..156
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 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 193
FT /note="N->G: Increased targeting to the endosomal/lysosomal
FT compartment and reduced myotube formation."
FT /evidence="ECO:0000269|PubMed:18227060"
FT MUTAGEN 194
FT /note="Y->A: Inefficient targeting to the
FT endosomal/lysosomal compartment and enhanced myotube
FT formation."
FT /evidence="ECO:0000269|PubMed:18227060"
FT CONFLICT 2
FT /note="S -> L (in Ref. 4; BAE26251)"
FT /evidence="ECO:0000305"
FT CONFLICT 24..25
FT /note="QP -> HA (in Ref. 3; BAA34547)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 197 AA; 21059 MW; 8099FFF978430C91 CRC64;
MSGSSRRLLW AATCLAVLCV SAAQPNITTL APNVTEVPTT TTKVVPTTQM PTVLPETCAS
FNSCVSCVNA TFTNNITCFW LHCQEANKTY CANEPLSNCS QVNRTDLCSV IPPTTPVPTN
STAKPTTRPS SPTPTPSVVT SAGTTNTTLT PTSQPERKST FDAASFIGGI VLVLGVQAVI
FFLYKFCKSK ERNYHTL
