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Protein

Endomucin

Gene

Emcn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Endothelial sialomucin, also called endomucin or mucin-like sialoglycoprotein, which interferes with the assembly of focal adhesion complexes and inhibits interaction between cells and the extracellular matrix.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Endomucin
Alternative name(s):
Endomucin-1/2
Mucin-14
Short name:
MUC-14
Gene namesi
Name:Emcn
Synonyms:Muc14
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1891716. Emcn.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 190170ExtracellularSequence analysisAdd
BLAST
Transmembranei191 – 21121HelicalSequence analysisAdd
BLAST
Topological domaini212 – 26150CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 261241EndomucinPRO_0000019291Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi28 – 281N-linked (GlcNAc...)Sequence analysis
Glycosylationi101 – 1011N-linked (GlcNAc...)Sequence analysis
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence analysis
Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence analysis
Glycosylationi131 – 1311N-linked (GlcNAc...)Sequence analysis
Modified residuei237 – 2371PhosphoserineCombined sources

Post-translational modificationi

Highly O-glycosylated. Sialic acid-rich glycoprotein.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9R0H2.
PaxDbiQ9R0H2.
PRIDEiQ9R0H2.

PTM databases

iPTMnetiQ9R0H2.
PhosphoSiteiQ9R0H2.

Expressioni

Tissue specificityi

Highly expressed in heart and kidney, followed by brain, spleen, thymus, liver and lung. Exclusively expressed in endothelial cells.1 Publication

Gene expression databases

BgeeiQ9R0H2.
CleanExiMM_EMCN.
ExpressionAtlasiQ9R0H2. baseline and differential.
GenevisibleiQ9R0H2. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000112603.

Structurei

3D structure databases

ProteinModelPortaliQ9R0H2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi33 – 185153Thr-richAdd
BLAST

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410J0MP. Eukaryota.
ENOG4111AC7. LUCA.
GeneTreeiENSGT00390000012139.
HOGENOMiHOG000013126.
HOVERGENiHBG052537.
InParanoidiQ9R0H2.
KOiK16664.
OMAiTTDVRKN.
OrthoDBiEOG7CNZH6.
PhylomeDBiQ9R0H2.
TreeFamiTF337783.

Family and domain databases

InterProiIPR010740. Endomucin.
[Graphical view]
PANTHERiPTHR15869. PTHR15869. 1 hit.
PfamiPF07010. Endomucin. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9R0H2-1) [UniParc]FASTAAdd to basket

Also known as: 1a

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRLLQATVLF FLLSNSLCHS EDGKDVQNDS IPTPAETSTT KASVTIPGIV
60 70 80 90 100
SVTNPNKPAD GTPPEGTTKS DVSQTSLVTT INSLTTPKHE VGTTTEGPLR
110 120 130 140 150
NESSTMKITV PNTPTSNANS TLPGSQNKTE NQSSIRTTEI SVTTQLLDAL
160 170 180 190 200
PKITATSSAS LTTAHTMSLL QDTEDRKIAT TPSTTPSYSS IILPVVIALV
210 220 230 240 250
VITLLVFTLV GLYRICWKRD PGTPENGNDQ PQSDKESVKL LTVKTISHES
260
GEHSAQGKTK N
Length:261
Mass (Da):27,756
Last modified:May 1, 2000 - v1
Checksum:iEF797205E9BEF3F4
GO
Isoform 2 (identifier: Q9R0H2-2) [UniParc]FASTAAdd to basket

Also known as: 1b

The sequence of this isoform differs from the canonical sequence as follows:
     129-142: TENQSSIRTTEISV → I

Show »
Length:248
Mass (Da):26,323
Checksum:i9337753FF47A79BF
GO
Isoform 3 (identifier: Q9R0H2-3) [UniParc]FASTAAdd to basket

Also known as: 1c

The sequence of this isoform differs from the canonical sequence as follows:
     91-129: VGTTTEGPLRNESSTMKITVPNTPTSNANSTLPGSQNKT → A

Note: No experimental confirmation available.
Show »
Length:223
Mass (Da):23,813
Checksum:i614F7B5882F5CA30
GO
Isoform 4 (identifier: Q9R0H2-4) [UniParc]FASTAAdd to basket

Also known as: 1d

The sequence of this isoform differs from the canonical sequence as follows:
     91-141: Missing.

Note: No experimental confirmation available.
Show »
Length:210
Mass (Da):22,395
Checksum:i13168D7928F62E3A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181C → G in BAB22232 (PubMed:16141072).Curated
Sequence conflicti157 – 1571S → P in AAD05208 (PubMed:9864158).Curated
Sequence conflicti256 – 2561Q → R in BAB22232 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei91 – 14151Missing in isoform 4. 1 PublicationVSP_010828Add
BLAST
Alternative sequencei91 – 12939VGTTT…SQNKT → A in isoform 3. 1 PublicationVSP_010827Add
BLAST
Alternative sequencei129 – 14214TENQS…TEISV → I in isoform 2. 3 PublicationsVSP_010829Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF060883 mRNA. Translation: AAD05208.1.
AB034693 mRNA. Translation: BAA86226.1.
AB034694 mRNA. Translation: BAA86227.1.
AK002616 mRNA. Translation: BAB22232.1.
BC003706 mRNA. Translation: AAH03706.1.
CCDSiCCDS17861.1. [Q9R0H2-2]
CCDS51075.1. [Q9R0H2-1]
RefSeqiNP_001156994.1. NM_001163522.1. [Q9R0H2-1]
NP_058581.2. NM_016885.2. [Q9R0H2-2]
XP_006501905.1. XM_006501842.2. [Q9R0H2-3]
UniGeneiMm.27343.

Genome annotation databases

EnsembliENSMUST00000119475; ENSMUSP00000114102; ENSMUSG00000054690. [Q9R0H2-2]
ENSMUST00000122064; ENSMUSP00000112603; ENSMUSG00000054690. [Q9R0H2-1]
GeneIDi59308.
KEGGimmu:59308.
UCSCiuc008rmk.2. mouse. [Q9R0H2-2]
uc008rml.2. mouse. [Q9R0H2-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF060883 mRNA. Translation: AAD05208.1.
AB034693 mRNA. Translation: BAA86226.1.
AB034694 mRNA. Translation: BAA86227.1.
AK002616 mRNA. Translation: BAB22232.1.
BC003706 mRNA. Translation: AAH03706.1.
CCDSiCCDS17861.1. [Q9R0H2-2]
CCDS51075.1. [Q9R0H2-1]
RefSeqiNP_001156994.1. NM_001163522.1. [Q9R0H2-1]
NP_058581.2. NM_016885.2. [Q9R0H2-2]
XP_006501905.1. XM_006501842.2. [Q9R0H2-3]
UniGeneiMm.27343.

3D structure databases

ProteinModelPortaliQ9R0H2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000112603.

PTM databases

iPTMnetiQ9R0H2.
PhosphoSiteiQ9R0H2.

Proteomic databases

MaxQBiQ9R0H2.
PaxDbiQ9R0H2.
PRIDEiQ9R0H2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000119475; ENSMUSP00000114102; ENSMUSG00000054690. [Q9R0H2-2]
ENSMUST00000122064; ENSMUSP00000112603; ENSMUSG00000054690. [Q9R0H2-1]
GeneIDi59308.
KEGGimmu:59308.
UCSCiuc008rmk.2. mouse. [Q9R0H2-2]
uc008rml.2. mouse. [Q9R0H2-1]

Organism-specific databases

CTDi51705.
MGIiMGI:1891716. Emcn.

Phylogenomic databases

eggNOGiENOG410J0MP. Eukaryota.
ENOG4111AC7. LUCA.
GeneTreeiENSGT00390000012139.
HOGENOMiHOG000013126.
HOVERGENiHBG052537.
InParanoidiQ9R0H2.
KOiK16664.
OMAiTTDVRKN.
OrthoDBiEOG7CNZH6.
PhylomeDBiQ9R0H2.
TreeFamiTF337783.

Miscellaneous databases

NextBioi314800.
PROiQ9R0H2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R0H2.
CleanExiMM_EMCN.
ExpressionAtlasiQ9R0H2. baseline and differential.
GenevisibleiQ9R0H2. MM.

Family and domain databases

InterProiIPR010740. Endomucin.
[Graphical view]
PANTHERiPTHR15869. PTHR15869. 1 hit.
PfamiPF07010. Endomucin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Biochemical characterization and molecular cloning of a novel endothelial-specific sialomucin."
    Morgan S.M., Samulowitz U., Darley L., Simmons D.L., Vestweber D.
    Blood 93:165-175(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), O-SIALOGLYCOSYLATION.
    Tissue: Brain.
  2. "Identification of human endomucin-1 and -2 as membrane-bound O-sialoglycoproteins with anti-adhesive activity."
    Kinoshita M., Nakamura T., Ihara M., Haraguchi T., Hiraoka Y., Tashiro K., Noda M.
    FEBS Lett. 499:121-126(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GLYCOSYLATION, TISSUE SPECIFICITY.
    Strain: C57BL/6J.
    Tissue: Brain.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
  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] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Kidney.
  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] (ISOFORM 1).
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart and Kidney.

Entry informationi

Entry nameiMUCEN_MOUSE
AccessioniPrimary (citable) accession number: Q9R0H2
Secondary accession number(s): Q78KL2
, Q9DCN9, Q9ULC1, Q9Z2I1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: May 1, 2000
Last modified: January 20, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.