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Sialomucin core protein 24 (MUC-24) (Endolyn) (Multi-glycosylated core protein 24) (MGC-24) (MGC-24v) (CD antigen CD164)

 MUC24_MOUSE             Reviewed;         197 AA.
Q9R0L9; Q3UM47; Q9Z317;
01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
05-JUL-2017, entry version 106.
RecName: Full=Sialomucin core protein 24;
Short=MUC-24;
AltName: Full=Endolyn;
AltName: Full=Multi-glycosylated core protein 24;
Short=MGC-24;
Short=MGC-24v;
AltName: CD_antigen=CD164;
Flags: Precursor;
Name=Cd164;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=10491205; DOI=10.1046/j.1432-1327.1999.00777.x;
Kurosawa N., Kanemitsu Y., Matsui T., Shimada K., Ishihama H.,
Muramatsu T.;
"Genomic analysis of a murine cell-surface sialomucin, MGC-24/CD164.";
Eur. J. Biochem. 265:466-472(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
PubMed=11027692; DOI=10.1074/jbc.M007965200;
Chan J.Y.-H., Lee-Prudhoe J.E., Jorgensen B., Ihrke G., Doyonnas R.,
Zannettino A.C.W., Buckle V.J., Ward C.J., Simmons P.J., Watt S.M.;
"Relationship between novel isoforms, functionally important domains,
and subcellular distribution of CD164/endolyn.";
J. Biol. Chem. 276:2139-2152(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=ICR; TISSUE=Brain;
Kurosawa N., Matsui T., Muramatsu T.;
"Mouse MGC-24v.";
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary gland;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, INTERACTION WITH CXCR4, DEVELOPMENTAL STAGE, AND MUTAGENESIS
OF ASN-193 AND TYR-194.
PubMed=18227060; DOI=10.1074/jbc.M706730200;
Bae G.-U., Gaio U., Yang Y.-J., Lee H.-J., Kang J.-S., Krauss R.S.;
"Regulation of myoblast motility and fusion by the CXCR4-associated
sialomucin, CD164.";
J. Biol. Chem. 283:8301-8309(2008).
[7]
TISSUE SPECIFICITY.
PubMed=26197441; DOI=10.1371/journal.pgen.1005386;
Nyegaard M., Rendtorff N.D., Nielsen M.S., Corydon T.J., Demontis D.,
Starnawska A., Hedemand A., Buniello A., Niola F., Overgaard M.T.,
Leal S.M., Ahmad W., Wikman F.P., Petersen K.B., Crueger D.G.,
Oostrik J., Kremer H., Tommerup N., Froedin M., Steel K.P.,
Tranebjaerg L., Boerglum A.D.;
"A novel locus harbouring a functional CD164 nonsense mutation
identified in a large Danish family with nonsyndromic hearing
impairment.";
PLoS Genet. 11:E1005386-E1005386(2015).
-!- FUNCTION: Sialomucin that may play a key role in hematopoiesis.
May be involved in cell adhesion (By similarity). Promotes
myogenesis by enhancing CXCR4-dependent cell motility. Positively
regulates myoblast migration and promotes myoblast fusion into
myotubes. {ECO:0000250|UniProtKB:Q04900,
ECO:0000269|PubMed:18227060}.
-!- SUBUNIT: Interacts with CXCR4. {ECO:0000269|PubMed:18227060}.
-!- SUBCELLULAR LOCATION: Lysosome membrane
{ECO:0000250|UniProtKB:Q04900}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:Q04900}. Endosome membrane
{ECO:0000250|UniProtKB:Q04900}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:Q04900}. Cell membrane
{ECO:0000250|UniProtKB:Q04900}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:Q04900}.
-!- TISSUE SPECIFICITY: Expressed at high levels in the submaxillary
gland and kidney, at moderate levels in the brain, heart, lung,
liver, intestine, testis, muscle and bone marrow, and at low
levels in the pancreas, spleen and thymus. In the ear, expressed
in the inner and outer hair cells of the organ of Corti, cells of
Kolliker's organ, cells in the lateral cochlear wall behind the
spiral prominence and cells of the stria vascularis
(PubMed:26197441). {ECO:0000269|PubMed:10491205,
ECO:0000269|PubMed:11027692, ECO:0000269|PubMed:26197441}.
-!- DEVELOPMENTAL STAGE: During embryogenesis, expression in found in
all stages examined, with the highest levels of expression at
early stages (E8.5) and moderate levels of expression being found
at mid- to late stages of embryogenesis. Expressed during early
stages of skeletal muscle development. At embryonic stages E9.5
and E10.5, expressed strongly in the dorsal somite (the structure
of origin for skeletal muscle precursors). It is also expressed at
later stages of muscle development;. {ECO:0000269|PubMed:10491205,
ECO:0000269|PubMed:18227060}.
-!- PTM: Highly N- and O-glycosylated; contains sialic acid.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the CD164 family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AB028895; BAA78909.1; -; mRNA.
EMBL; AF299345; AAG53910.1; -; mRNA.
EMBL; AF299344; AAG53909.1; -; Genomic_DNA.
EMBL; AB014464; BAA34547.1; -; mRNA.
EMBL; AK145131; BAE26251.1; -; mRNA.
EMBL; AK169275; BAE41034.1; -; mRNA.
EMBL; BC005414; AAH05414.1; -; mRNA.
CCDS; CCDS23806.1; -.
RefSeq; NP_058594.1; NM_016898.2.
UniGene; Mm.269815; -.
ProteinModelPortal; Q9R0L9; -.
IntAct; Q9R0L9; 1.
MINT; MINT-1744078; -.
PhosphoSitePlus; Q9R0L9; -.
PaxDb; Q9R0L9; -.
PRIDE; Q9R0L9; -.
Ensembl; ENSMUST00000019962; ENSMUSP00000019962; ENSMUSG00000019818.
GeneID; 53599; -.
KEGG; mmu:53599; -.
UCSC; uc007exv.1; mouse.
CTD; 8763; -.
MGI; MGI:1859568; Cd164.
eggNOG; ENOG410J0NP; Eukaryota.
eggNOG; ENOG410XVJX; LUCA.
GeneTree; ENSGT00530000063929; -.
HOGENOM; HOG000070053; -.
InParanoid; Q9R0L9; -.
KO; K06546; -.
OMA; VSCFNAS; -.
OrthoDB; EOG091G141K; -.
PhylomeDB; Q9R0L9; -.
TreeFam; TF333380; -.
PRO; PR:Q9R0L9; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000019818; -.
ExpressionAtlas; Q9R0L9; baseline and differential.
Genevisible; Q9R0L9; MM.
GO; GO:0005768; C:endosome; ISS:UniProtKB.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0005764; C:lysosome; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; ISO:MGI.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:MGI.
GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
InterPro; IPR007947; CD164_MGC24.
PANTHER; PTHR11337; PTHR11337; 1.
Pfam; PF05283; MGC-24; 1.
PRINTS; PR01701; CD164ANTIGEN.
1: Evidence at protein level;
Cell adhesion; Cell membrane; Complete proteome; Endosome;
Glycoprotein; Lysosome; Membrane; Myogenesis; Reference proteome;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 197 Sialomucin core protein 24.
/FTId=PRO_0000383341.
TOPO_DOM 24 162 Extracellular. {ECO:0000255}.
TRANSMEM 163 183 Helical. {ECO:0000255}.
TOPO_DOM 184 197 Cytoplasmic. {ECO:0000255}.
REGION 191 197 Required for endosomal and lysosomal
localization. {ECO:0000250}.
COMPBIAS 28 152 Thr-rich.
CARBOHYD 26 26 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 33 33 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 69 69 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 75 75 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 87 87 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 120 120 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 146 146 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 193 193 N->G: Increased targeting to the
endosomal/lysosomal compartment and
reduced myotube formation.
{ECO:0000269|PubMed:18227060}.
MUTAGEN 194 194 Y->A: Ineffcient targeting to the
endosomal/lysosomal compartment and
enhanced myotube formation.
{ECO:0000269|PubMed:18227060}.
CONFLICT 2 2 S -> L (in Ref. 4; BAE26251).
{ECO:0000305}.
CONFLICT 24 25 QP -> HA (in Ref. 3; BAA34547).
{ECO:0000305}.
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


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