ID   MUCEN_PONAB             Reviewed;         260 AA.
AC   Q5RFI9;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Endomucin;
DE   Flags: Precursor;
GN   Name=EMCN;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 membrane
CC       protein {ECO:0000305}.
CC   -!- PTM: Highly O-glycosylated. Sialic acid-rich glycoprotein (By
CC       similarity). {ECO:0000250}.
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DR   EMBL; CR857167; CAH89468.1; -; mRNA.
DR   RefSeq; NP_001128972.1; NM_001135500.1.
DR   AlphaFoldDB; Q5RFI9; -.
DR   STRING; 9601.ENSPPYP00000016704; -.
DR   Ensembl; ENSPPYT00000017383; ENSPPYP00000016704; ENSPPYG00000014959.
DR   GeneID; 100190812; -.
DR   KEGG; pon:100190812; -.
DR   CTD; 51705; -.
DR   eggNOG; ENOG502S6VA; Eukaryota.
DR   GeneTree; ENSGT00390000012139; -.
DR   HOGENOM; CLU_092835_0_0_1; -.
DR   InParanoid; Q5RFI9; -.
DR   OMA; XPQSDKE; -.
DR   OrthoDB; 1471475at2759; -.
DR   TreeFam; TF337783; -.
DR   Proteomes; UP000001595; Chromosome 4.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR010740; Endomucin.
DR   PANTHER; PTHR15869; PTHR15869; 1.
DR   Pfam; PF07010; Endomucin; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..260
FT                   /note="Endomucin"
FT                   /id="PRO_0000249726"
FT   TOPO_DOM        19..189
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        211..260
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          119..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         236
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R0H2"
FT   CARBOHYD        19
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        97
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        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   260 AA;  27415 MW;  B70C2E99A0402363 CRC64;
     MELLQVTILF LLPSICSSNS TGVLEAANNS LVVTTIKTSI TTPNTESLQK NVITPTTGTT
     PKGKITNELL KMSLMSAVTL TSKDEGLKVT TTDVRKNESI VSNVTVTIVT LPNAVSTLQS
     SKPKTETQSS IKTTEIPGSI LQPDASPSET GTLSSIPVTI PENTSQSQVI GTEGGKNAST
     SATSRSYSSI ILPVVIALIV ITLSVFVLVG LYRMCWKADP GTPENGNDQP QSDKESVKLL
     TVKTISHESG EHSAQGKTKN