MUCEN_MOUSE
ID MUCEN_MOUSE Reviewed; 261 AA.
AC Q9R0H2; Q78KL2; Q9DCN9; Q9ULC1; Q9Z2I1;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Endomucin;
DE AltName: Full=Endomucin-1/2;
DE AltName: Full=Mucin-14;
DE Short=MUC-14;
DE Flags: Precursor;
GN Name=Emcn; Synonyms=Muc14;
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] (ISOFORM 2), AND O-SIALOGLYCOSYLATION.
RC TISSUE=Brain;
RX PubMed=9864158;
RA Morgan S.M., Samulowitz U., Darley L., Simmons D.L., Vestweber D.;
RT "Biochemical characterization and molecular cloning of a novel endothelial-
RT specific sialomucin.";
RL Blood 93:165-175(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GLYCOSYLATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=11418125; DOI=10.1016/s0014-5793(01)02520-0;
RA Kinoshita M., Nakamura T., Ihara M., Haraguchi T., Hiraoka Y., Tashiro K.,
RA Noda M.;
RT "Identification of human endomucin-1 and -2 as membrane-bound O-
RT sialoglycoproteins with anti-adhesive activity.";
RL FEBS Lett. 499:121-126(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
RX PubMed=11554756; DOI=10.1006/bbrc.2001.5587;
RA Ueno M., Igarashi K., Kimura N., Okita K., Takizawa M., Nobuhisa I.,
RA Kojima T., Kitamura T., Samulowitz U., Vestweber D., Shimomura T., Suda T.,
RA Nakashima K., Taga T.;
RT "Endomucin is expressed in embryonic dorsal aorta and is able to inhibit
RT cell adhesion.";
RL Biochem. Biophys. Res. Commun. 287:501-506(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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] (ISOFORM 1).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Endothelial sialomucin, also called endomucin or mucin-like
CC sialoglycoprotein, which interferes with the assembly of focal adhesion
CC complexes and inhibits interaction between cells and the extracellular
CC matrix. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=1a;
CC IsoId=Q9R0H2-1; Sequence=Displayed;
CC Name=2; Synonyms=1b;
CC IsoId=Q9R0H2-2; Sequence=VSP_010829;
CC Name=3; Synonyms=1c;
CC IsoId=Q9R0H2-3; Sequence=VSP_010827;
CC Name=4; Synonyms=1d;
CC IsoId=Q9R0H2-4; Sequence=VSP_010828;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart and kidney, followed by
CC brain, spleen, thymus, liver and lung. Exclusively expressed in
CC endothelial cells. {ECO:0000269|PubMed:11418125}.
CC -!- PTM: Highly O-glycosylated. Sialic acid-rich glycoprotein.
CC {ECO:0000269|PubMed:11418125}.
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; AF060883; AAD05208.1; -; mRNA.
DR EMBL; AB034693; BAA86226.1; -; mRNA.
DR EMBL; AB034694; BAA86227.1; -; mRNA.
DR EMBL; AK002616; BAB22232.1; -; mRNA.
DR EMBL; BC003706; AAH03706.1; -; mRNA.
DR CCDS; CCDS17861.1; -. [Q9R0H2-2]
DR CCDS; CCDS51075.1; -. [Q9R0H2-1]
DR RefSeq; NP_001156994.1; NM_001163522.1. [Q9R0H2-1]
DR RefSeq; NP_058581.2; NM_016885.2. [Q9R0H2-2]
DR RefSeq; XP_006501905.1; XM_006501842.2. [Q9R0H2-3]
DR AlphaFoldDB; Q9R0H2; -.
DR SMR; Q9R0H2; -.
DR STRING; 10090.ENSMUSP00000112603; -.
DR GlyGen; Q9R0H2; 5 sites.
DR iPTMnet; Q9R0H2; -.
DR PhosphoSitePlus; Q9R0H2; -.
DR jPOST; Q9R0H2; -.
DR MaxQB; Q9R0H2; -.
DR PaxDb; Q9R0H2; -.
DR PRIDE; Q9R0H2; -.
DR ProteomicsDB; 290072; -. [Q9R0H2-1]
DR ProteomicsDB; 290073; -. [Q9R0H2-2]
DR ProteomicsDB; 290074; -. [Q9R0H2-3]
DR ProteomicsDB; 290075; -. [Q9R0H2-4]
DR Antibodypedia; 989; 218 antibodies from 32 providers.
DR DNASU; 59308; -.
DR Ensembl; ENSMUST00000119475; ENSMUSP00000114102; ENSMUSG00000054690. [Q9R0H2-2]
DR Ensembl; ENSMUST00000122064; ENSMUSP00000112603; ENSMUSG00000054690. [Q9R0H2-1]
DR GeneID; 59308; -.
DR KEGG; mmu:59308; -.
DR UCSC; uc008rmk.2; mouse. [Q9R0H2-2]
DR UCSC; uc008rml.2; mouse. [Q9R0H2-1]
DR CTD; 51705; -.
DR MGI; MGI:1891716; Emcn.
DR VEuPathDB; HostDB:ENSMUSG00000054690; -.
DR eggNOG; ENOG502S6VA; Eukaryota.
DR GeneTree; ENSGT00390000012139; -.
DR InParanoid; Q9R0H2; -.
DR OMA; XPQSDKE; -.
DR OrthoDB; 1471475at2759; -.
DR PhylomeDB; Q9R0H2; -.
DR TreeFam; TF337783; -.
DR BioGRID-ORCS; 59308; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q9R0H2; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9R0H2; protein.
DR Bgee; ENSMUSG00000054690; Expressed in left lung lobe and 223 other tissues.
DR ExpressionAtlas; Q9R0H2; baseline and differential.
DR Genevisible; Q9R0H2; MM.
DR GO; GO:0016021; C:integral component of membrane; ISA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:HGNC.
DR GO; GO:0030246; F:carbohydrate binding; ISS:HGNC.
DR GO; GO:0001525; P:angiogenesis; ISS:HGNC.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:HGNC.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IMP:MGI.
DR GO; GO:0030155; P:regulation of cell adhesion; ISS:HGNC.
DR InterPro; IPR010740; Endomucin.
DR PANTHER; PTHR15869; PTHR15869; 1.
DR Pfam; PF07010; Endomucin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..261
FT /note="Endomucin"
FT /id="PRO_0000019291"
FT TOPO_DOM 21..190
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 21..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 221..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 91..141
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11554756"
FT /id="VSP_010828"
FT VAR_SEQ 91..129
FT /note="VGTTTEGPLRNESSTMKITVPNTPTSNANSTLPGSQNKT -> A (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:11554756"
FT /id="VSP_010827"
FT VAR_SEQ 129..142
FT /note="TENQSSIRTTEISV -> I (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11554756,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9864158"
FT /id="VSP_010829"
FT CONFLICT 18
FT /note="C -> G (in Ref. 4; BAB22232)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="S -> P (in Ref. 1; AAD05208)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="Q -> R (in Ref. 4; BAB22232)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 261 AA; 27756 MW; EF797205E9BEF3F4 CRC64;
MRLLQATVLF FLLSNSLCHS EDGKDVQNDS IPTPAETSTT KASVTIPGIV SVTNPNKPAD
GTPPEGTTKS DVSQTSLVTT INSLTTPKHE VGTTTEGPLR NESSTMKITV PNTPTSNANS
TLPGSQNKTE NQSSIRTTEI SVTTQLLDAL PKITATSSAS LTTAHTMSLL QDTEDRKIAT
TPSTTPSYSS IILPVVIALV VITLLVFTLV GLYRICWKRD PGTPENGNDQ PQSDKESVKL
LTVKTISHES GEHSAQGKTK N
