Q9R0L9 (MUC24_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sialomucin core protein 24
Short name=MUC-24

Alternative name(s):
Endolyn
Multi-glycosylated core protein 24
Short name=MGC-24
Short name=MGC-24v
CD_antigen=CD164

Gene names

Name:

Cd164

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	197 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.6
Subunit structure	Interacts with CXCR4. Ref.6
Subcellular location	Lysosome membrane; Single-pass type I membrane protein Potential. Endosome membrane; Single-pass type I membrane protein By similarity. Cell membrane; Single-pass type I membrane protein By similarity.
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. Ref.1 Ref.2
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;. Ref.1 Ref.6
Post-translational modification	Highly N- and O-glycosylated; contains sialic acid By similarity.
Sequence similarities	Belongs to the CD164 family.

Ontologies

Keywords
Biological process	Cell adhesion Myogenesis
Cellular component	Cell membrane Endosome Lysosome Membrane
Domain	Signal Transmembrane Transmembrane helix
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	heterophilic cell-cell adhesion Inferred from sequence orthology Ref.1. Source: MGI muscle organ development Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW lysosomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from sequence orthology Ref.1. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 197	174	Sialomucin core protein 24		PRO_0000383341
Regions
	Topological domain	24 – 162	139	Extracellular Potential
	Transmembrane	163 – 183	21	Helical; Potential
	Topological domain	184 – 197	14	Cytoplasmic Potential
	Region	191 – 197	7	Required for endosomal and lysosomal localization By similarity
	Compositional bias	28 – 152	125	Thr-rich
Amino acid modifications
	Glycosylation	26	1	N-linked (GlcNAc...) Potential
	Glycosylation	33	1	N-linked (GlcNAc...) Potential
	Glycosylation	69	1	N-linked (GlcNAc...) Potential
	Glycosylation	75	1	N-linked (GlcNAc...) Potential
	Glycosylation	87	1	N-linked (GlcNAc...) Potential
	Glycosylation	98	1	N-linked (GlcNAc...) Potential
	Glycosylation	103	1	N-linked (GlcNAc...) Potential
	Glycosylation	120	1	N-linked (GlcNAc...) Potential
	Glycosylation	146	1	N-linked (GlcNAc...) Potential
Experimental info
	Mutagenesis	193	1	N → G: Increased targeting to the endosomal/lysosomal compartment and reduced myotube formation. Ref.6
	Mutagenesis	194	1	Y → A: Ineffcient targeting to the endosomal/lysosomal compartment and enhanced myotube formation. Ref.6
	Sequence conflict	2	1	S → L in BAE26251. Ref.4
	Sequence conflict	24 – 25	2	QP → HA in BAA34547. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9R0L9 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 8099FFF978430C91	FASTA	197	21,059
	10 20 30 40 50 60 MSGSSRRLLW AATCLAVLCV SAAQPNITTL APNVTEVPTT TTKVVPTTQM PTVLPETCAS 70 80 90 100 110 120 FNSCVSCVNA TFTNNITCFW LHCQEANKTY CANEPLSNCS QVNRTDLCSV IPPTTPVPTN 130 140 150 160 170 180 STAKPTTRPS SPTPTPSVVT SAGTTNTTLT PTSQPERKST FDAASFIGGI VLVLGVQAVI 190 FFLYKFCKSK ERNYHTL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic analysis of a murine cell-surface sialomucin, MGC-24/CD164." Kurosawa N., Kanemitsu Y., Matsui T., Shimada K., Ishihama H., Muramatsu T. Eur. J. Biochem. 265:466-472(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[2]	"Relationship between novel isoforms, functionally important domains, and subcellular distribution of CD164/endolyn." 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. J. Biol. Chem. 276:2139-2152(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
[3]	"Mouse MGC-24v." Kurosawa N., Matsui T., Muramatsu T. Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: ICR. Tissue: Brain.
[4]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Mammary gland.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary tumor.
[6]	"Regulation of myoblast motility and fusion by the CXCR4-associated sialomucin, CD164." Bae G.-U., Gaio U., Yang Y.-J., Lee H.-J., Kang J.-S., Krauss R.S. J. Biol. Chem. 283:8301-8309(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CXCR4, DEVELOPMENTAL STAGE, MUTAGENESIS OF ASN-193 AND TYR-194.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB028895 mRNA. Translation: BAA78909.1. AF299345 mRNA. Translation: AAG53910.1. AF299344 Genomic DNA. Translation: AAG53909.1. AB014464 mRNA. Translation: BAA34547.1. AK145131 mRNA. Translation: BAE26251.1. AK169275 mRNA. Translation: BAE41034.1. BC005414 mRNA. Translation: AAH05414.1.
IPI	IPI00127770.
RefSeq	NP_058594.1. NM_016898.2.
UniGene	Mm.269815.
3D structure databases
ProteinModelPortal	Q9R0L9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9R0L9. 1 interaction.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000019962; ENSMUSP00000019962; ENSMUSG00000019818.
GeneID	53599.
KEGG	mmu:53599.
UCSC	uc007exv.1. mouse.
Organism-specific databases
CTD	8763.
MGI	MGI:1859568. Cd164.
Phylogenomic databases
eggNOG	NOG77756.
GeneTree	ENSGT00530000063929.
HOGENOM	HOG000070053.
InParanoid	Q3UM47.
KO	K06546.
OMA	NSCVSCV.
OrthoDB	EOG4C2HBQ.
Gene expression databases
Bgee	Q9R0L9.
Genevestigator	Q9R0L9.
Family and domain databases
InterPro	IPR007947. CD164_MGC24. [Graphical view]
PANTHER	PTHR11337:SF8. PTHR11337:SF8. 1 hit.
Pfam	PF05283. MGC-24. 1 hit. [Graphical view]
PRINTS	PR01701. CD164ANTIGEN.
ProtoNet	Search...
Other
ChiTaRS	CD164. mouse.
NextBio	310273.
SOURCE	Search...

Entry information

Entry name

MUC24_MOUSE

Accession

Primary (citable) accession number: Q9R0L9
Secondary accession number(s): Q3UM47, Q9Z317

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 1, 2009
Last sequence update:	May 1, 2000
Last modified:	April 3, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program