CD109_HUMAN
ID CD109_HUMAN Reviewed; 1445 AA.
AC Q6YHK3; A5YKK4; B2R948; B3KW25; Q0P6K7; Q5SYA8; Q5XUM7; Q5XUM9; Q6MZI7;
AC Q8N3A7; Q8N915; Q8TDJ2; Q8TDJ3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=CD109 antigen;
DE AltName: Full=150 kDa TGF-beta-1-binding protein;
DE AltName: Full=C3 and PZP-like alpha-2-macroglobulin domain-containing protein 7;
DE AltName: Full=Platelet-specific Gov antigen;
DE AltName: Full=p180;
DE AltName: Full=r150;
DE AltName: CD_antigen=CD109;
DE Flags: Precursor;
GN Name=CD109; Synonyms=CPAMD7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 86-98; 127-137;
RP 170-183; 185-196; 355-374; 413-425; 444-451; 465-471; 478-491; 494-510;
RP 573-589; 649-655; 666-672; 677-683; 698-709 AND 791-806, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, AND VARIANT MET-1241.
RX PubMed=11861284; DOI=10.1182/blood.v99.5.1683;
RA Lin M., Sutherland D.R., Horsfall W., Totty N., Yeo E., Nayar R., Wu X.-F.,
RA Schuh A.C.;
RT "Cell surface antigen CD109 is a novel member of the alpha(2)
RT macroglobulin/C3, C4, C5 family of thioester-containing proteins.";
RL Blood 99:1683-1691(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 22-50 (ISOFORM
RP 1), TISSUE SPECIFICITY, AND VARIANTS SER-703; SER-797 AND ILE-845.
RX PubMed=14980714; DOI=10.1016/j.gene.2003.11.025;
RA Solomon K.R., Sharma P., Chan M., Morrison P.T., Finberg R.W.;
RT "CD109 represents a novel branch of the alpha2-macroglobulin/complement
RT gene family.";
RL Gene 327:171-183(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), PROTEIN SEQUENCE OF 173-191,
RP FUNCTION, INTERACTION WITH TGFB1 AND TGFBR1, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, PROTEOLYTIC CLEAVAGE, AND VARIANTS SER-703; SER-797 AND
RP ILE-845.
RC TISSUE=Placenta;
RX PubMed=16754747; DOI=10.1096/fj.05-5229fje;
RA Finnson K.W., Tam B.Y.Y., Liu K., Marcoux A., Lepage P., Roy S.,
RA Bizet A.A., Philip A.;
RT "Identification of CD109 as part of the TGF-beta receptor system in human
RT keratinocytes.";
RL FASEB J. 20:1525-1527(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS
RP SER-703; SER-797 AND ILE-845.
RC TISSUE=Chondrocyte, Trachea, and Vascular endothelial cell;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP SER-703; SER-797; ILE-845 AND MET-1241.
RC TISSUE=Colon endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 370-444 AND 922-959.
RA Prosper J.Y.A., Wu X.-F., Sutherland D.R., Irwin D.M., Schuh A.C.;
RT "CD109 defines an ancient branch of the alpha2M/C3, C4, C5 family.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 703-741, POLYMORPHISM, AND VARIANT
RP GOV(B) SER-703.
RX PubMed=11861285; DOI=10.1182/blood.v99.5.1692;
RA Schuh A.C., Watkins N.A., Nguyen Q., Harmer N.J., Lin M., Prosper J.Y.A.,
RA Campbell K., Sutherland D.R., Metcalfe P., Horsfall W., Ouwehand W.H.;
RT "A tyrosine703serine polymorphism of CD109 defines the Gov platelet
RT alloantigens.";
RL Blood 99:1692-1698(2002).
RN [9]
RP PROTEOLYTIC CLEAVAGE, AND GLYCOSYLATION.
RX PubMed=1984805;
RA Sutherland D.R., Yeo E., Ryan A., Mills G.B., Bailey D., Baker M.A.;
RT "Identification of a cell-surface antigen associated with activated T
RT lymphoblasts and activated platelets.";
RL Blood 77:84-93(1991).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-68; ASN-118; ASN-247 AND
RP ASN-419.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-247.
RC TISSUE=Platelet;
RX PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200;
RA Lewandrowski U., Moebius J., Walter U., Sickmann A.;
RT "Elucidation of N-glycosylation sites on human platelet proteins: a
RT glycoproteomic approach.";
RL Mol. Cell. Proteomics 5:226-233(2006).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-419.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [13]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-68 AND ASN-118.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP VARIANTS [LARGE SCALE ANALYSIS] GLU-1007 AND LYS-1065.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [16]
RP VARIANT GLY-791.
RX PubMed=25787250; DOI=10.1073/pnas.1503696112;
RA Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W.,
RA Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D., Stalberg P.,
RA Akerstroem G., Westin G., Hellman P., Carling T., Bjoerklund P.,
RA Lifton R.P.;
RT "Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in
RT insulin-producing adenomas.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015).
CC -!- FUNCTION: Modulates negatively TGFB1 signaling in keratinocytes.
CC {ECO:0000269|PubMed:16754747}.
CC -!- SUBUNIT: Heterodimer; disulfide-linked. Interacts with TGFB1 and
CC TGFBR1. Forms a heteromeric complex with TGFBR1, TGFBR2 and TGFBR3 in a
CC ligand-independent manner. {ECO:0000269|PubMed:16754747}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11861284,
CC ECO:0000269|PubMed:16754747}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:11861284, ECO:0000269|PubMed:16754747}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=CD109 180-kDa;
CC IsoId=Q6YHK3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6YHK3-2; Sequence=VSP_021312;
CC Name=3;
CC IsoId=Q6YHK3-3; Sequence=VSP_021313, VSP_021314;
CC Name=4; Synonyms=CD109S;
CC IsoId=Q6YHK3-4; Sequence=VSP_021315;
CC -!- TISSUE SPECIFICITY: Widely expressed with high level in uterus, aorta,
CC heart, lung, trachea, placenta and in fetal heart, kidney, liver,
CC spleen and lung. Expressed by CD34(+) acute myeloid leukemia cell
CC lines, T-cell lines, activated T-lymphoblasts, endothelial cells and
CC activated platelets. Isoform 4 is expressed in placenta. Isoform 1 is
CC expressed in keratinocytes and placenta. {ECO:0000269|PubMed:11861284,
CC ECO:0000269|PubMed:14980714, ECO:0000269|PubMed:16754747}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:16263699,
CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218,
CC ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:1984805}.
CC -!- PTM: 2 forms of 150 (p150) and 120 kDa (p120) exist due to proteolytic
CC degradation from a 180 kDa form.
CC -!- POLYMORPHISM: The Gov(b) variant in position 703 defines the Gov
CC alloantigenic determinants. {ECO:0000269|PubMed:11861285}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG53987.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAE46045.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAE46045.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="https://atlasgeneticsoncology.org/gene/42925/cd109-(cd109-molecule)";
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DR EMBL; AF410459; AAL84159.1; -; mRNA.
DR EMBL; AY149920; AAN78483.1; -; mRNA.
DR EMBL; AY788891; AAX14639.1; -; mRNA.
DR EMBL; AK095888; BAC04642.1; -; mRNA.
DR EMBL; AK123960; BAG53987.1; ALT_INIT; mRNA.
DR EMBL; AK313636; BAG36395.1; -; mRNA.
DR EMBL; AL834478; CAD39137.1; -; mRNA.
DR EMBL; BX641095; CAE46045.1; ALT_SEQ; mRNA.
DR EMBL; EF553520; ABQ66266.1; -; mRNA.
DR EMBL; AL590428; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY736555; AAU94642.1; -; Genomic_DNA.
DR EMBL; AY736557; AAU94644.1; -; Genomic_DNA.
DR EMBL; AF410460; AAL84160.1; -; Genomic_DNA.
DR CCDS; CCDS4982.1; -. [Q6YHK3-1]
DR CCDS; CCDS55038.1; -. [Q6YHK3-4]
DR CCDS; CCDS55039.1; -. [Q6YHK3-2]
DR RefSeq; NP_001153059.1; NM_001159587.2. [Q6YHK3-4]
DR RefSeq; NP_001153060.1; NM_001159588.2. [Q6YHK3-2]
DR RefSeq; NP_598000.2; NM_133493.4. [Q6YHK3-1]
DR RefSeq; XP_005248716.1; XM_005248659.3.
DR AlphaFoldDB; Q6YHK3; -.
DR SMR; Q6YHK3; -.
DR BioGRID; 126424; 92.
DR IntAct; Q6YHK3; 39.
DR STRING; 9606.ENSP00000287097; -.
DR MEROPS; I39.006; -.
DR CarbonylDB; Q6YHK3; -.
DR GlyConnect; 795; 30 N-Linked glycans (12 sites).
DR GlyGen; Q6YHK3; 16 sites, 32 N-linked glycans (12 sites).
DR iPTMnet; Q6YHK3; -.
DR PhosphoSitePlus; Q6YHK3; -.
DR SwissPalm; Q6YHK3; -.
DR BioMuta; CD109; -.
DR DMDM; 117949389; -.
DR EPD; Q6YHK3; -.
DR jPOST; Q6YHK3; -.
DR MassIVE; Q6YHK3; -.
DR MaxQB; Q6YHK3; -.
DR PaxDb; Q6YHK3; -.
DR PeptideAtlas; Q6YHK3; -.
DR PRIDE; Q6YHK3; -.
DR ProteomicsDB; 67842; -. [Q6YHK3-1]
DR ProteomicsDB; 67843; -. [Q6YHK3-2]
DR ProteomicsDB; 67844; -. [Q6YHK3-3]
DR ProteomicsDB; 67845; -. [Q6YHK3-4]
DR Antibodypedia; 2141; 399 antibodies from 32 providers.
DR DNASU; 135228; -.
DR Ensembl; ENST00000287097.6; ENSP00000287097.4; ENSG00000156535.15. [Q6YHK3-1]
DR Ensembl; ENST00000422508.6; ENSP00000404475.2; ENSG00000156535.15. [Q6YHK3-2]
DR Ensembl; ENST00000437994.6; ENSP00000388062.2; ENSG00000156535.15. [Q6YHK3-4]
DR GeneID; 135228; -.
DR KEGG; hsa:135228; -.
DR MANE-Select; ENST00000287097.6; ENSP00000287097.4; NM_133493.5; NP_598000.2.
DR UCSC; uc003php.4; human. [Q6YHK3-1]
DR CTD; 135228; -.
DR DisGeNET; 135228; -.
DR GeneCards; CD109; -.
DR HGNC; HGNC:21685; CD109.
DR HPA; ENSG00000156535; Tissue enriched (parathyroid).
DR MalaCards; CD109; -.
DR MIM; 608859; gene.
DR neXtProt; NX_Q6YHK3; -.
DR OpenTargets; ENSG00000156535; -.
DR Orphanet; 853; Fetal and neonatal alloimmune thrombocytopenia.
DR PharmGKB; PA134949237; -.
DR VEuPathDB; HostDB:ENSG00000156535; -.
DR eggNOG; KOG1366; Eukaryota.
DR GeneTree; ENSGT00940000155926; -.
DR HOGENOM; CLU_001634_5_2_1; -.
DR InParanoid; Q6YHK3; -.
DR OMA; EVHIYFE; -.
DR OrthoDB; 354230at2759; -.
DR PhylomeDB; Q6YHK3; -.
DR TreeFam; TF313285; -.
DR PathwayCommons; Q6YHK3; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR SignaLink; Q6YHK3; -.
DR BioGRID-ORCS; 135228; 12 hits in 1074 CRISPR screens.
DR ChiTaRS; CD109; human.
DR GeneWiki; CD109; -.
DR GenomeRNAi; 135228; -.
DR Pharos; Q6YHK3; Tbio.
DR PRO; PR:Q6YHK3; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q6YHK3; protein.
DR Bgee; ENSG00000156535; Expressed in tibia and 184 other tissues.
DR Genevisible; Q6YHK3; HS.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; HDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0031092; C:platelet alpha granule membrane; TAS:Reactome.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0050431; F:transforming growth factor beta binding; IPI:UniProtKB.
DR GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR GO; GO:0043616; P:keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0061045; P:negative regulation of wound healing; IDA:UniProtKB.
DR GO; GO:0072675; P:osteoclast fusion; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0045616; P:regulation of keratinocyte differentiation; IEA:Ensembl.
DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR CDD; cd02897; A2M_2; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.690; -; 1.
DR InterPro; IPR009048; A-macroglobulin_rcpt-bd.
DR InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
DR InterPro; IPR011625; A2M_N_BRD.
DR InterPro; IPR041813; A2M_TED.
DR InterPro; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR019742; MacrogloblnA2_CS.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07703; A2M_BRD; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF01835; MG2; 1.
DR Pfam; PF17791; MG3; 1.
DR Pfam; PF07678; TED_complement; 1.
DR SMART; SM01360; A2M; 1.
DR SMART; SM01359; A2M_N_2; 1.
DR SMART; SM01361; A2M_recep; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF49410; SSF49410; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Bait region; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Protease inhibitor; Reference proteome;
KW Serine protease inhibitor; Signal; Thioester bond.
FT SIGNAL 1..21
FT CHAIN 22..1420
FT /note="CD109 antigen"
FT /id="PRO_0000255945"
FT PROPEP 1421..1445
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000255946"
FT REGION 593..702
FT /note="Bait region (approximate)"
FT /evidence="ECO:0000250"
FT LIPID 1420
FT /note="GPI-anchor amidated alanine"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19349973"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16263699,
FT ECO:0000269|PubMed:16335952"
FT CARBOHYD 279
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 513
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 645
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1086
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CROSSLNK 921..924
FT /note="Isoglutamyl cysteine thioester (Cys-Gln)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 93..169
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_021312"
FT VAR_SEQ 658..665
FT /note="AEYAERFM -> LFGTQEAL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021313"
FT VAR_SEQ 666..1445
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021314"
FT VAR_SEQ 1218..1234
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16754747"
FT /id="VSP_021315"
FT VARIANT 45
FT /note="G -> V (in dbSNP:rs9446983)"
FT /id="VAR_028875"
FT VARIANT 377
FT /note="G -> D (in dbSNP:rs7741152)"
FT /id="VAR_048105"
FT VARIANT 641
FT /note="L -> F (in dbSNP:rs7742662)"
FT /id="VAR_048106"
FT VARIANT 703
FT /note="Y -> S (in allele Gov(b); dbSNP:rs10455097)"
FT /evidence="ECO:0000269|PubMed:11861285,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:14980714,
FT ECO:0000269|PubMed:16754747, ECO:0000269|PubMed:17974005"
FT /id="VAR_028876"
FT VARIANT 791
FT /note="D -> G"
FT /evidence="ECO:0000269|PubMed:25787250"
FT /id="VAR_074179"
FT VARIANT 797
FT /note="N -> S (in dbSNP:rs2351528)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:14980714, ECO:0000269|PubMed:16754747,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_028877"
FT VARIANT 845
FT /note="V -> I (in dbSNP:rs5023688)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:14980714, ECO:0000269|PubMed:16754747,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_028878"
FT VARIANT 1007
FT /note="Q -> E (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1454572681)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036236"
FT VARIANT 1009
FT /note="V -> M (in dbSNP:rs35630075)"
FT /id="VAR_048107"
FT VARIANT 1065
FT /note="N -> K (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036237"
FT VARIANT 1241
FT /note="T -> M (in dbSNP:rs2917862)"
FT /evidence="ECO:0000269|PubMed:11861284,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_028879"
FT VARIANT 1296
FT /note="H -> R (in dbSNP:rs13207595)"
FT /id="VAR_048108"
FT CONFLICT 627
FT /note="M -> I (in Ref. 2; AAN78483)"
FT /evidence="ECO:0000305"
FT CONFLICT 789
FT /note="K -> E (in Ref. 4; BAG36395)"
FT /evidence="ECO:0000305"
FT CONFLICT 803
FT /note="G -> S (in Ref. 2; AAN78483)"
FT /evidence="ECO:0000305"
FT CONFLICT 1046
FT /note="V -> A (in Ref. 5; ABQ66266)"
FT /evidence="ECO:0000305"
FT CONFLICT 1418
FT /note="D -> N (in Ref. 4; BAG53987)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1445 AA; 161689 MW; 0C5B1C3B8CCAF195 CRC64;
MQGPPLLTAA HLLCVCTAAL AVAPGPRFLV TAPGIIRPGG NVTIGVELLE HCPSQVTVKA
ELLKTASNLT VSVLEAEGVF EKGSFKTLTL PSLPLNSADE IYELRVTGRT QDEILFSNST
RLSFETKRIS VFIQTDKALY KPKQEVKFRI VTLFSDFKPY KTSLNILIKD PKSNLIQQWL
SQQSDLGVIS KTFQLSSHPI LGDWSIQVQV NDQTYYQSFQ VSEYVLPKFE VTLQTPLYCS
MNSKHLNGTI TAKYTYGKPV KGDVTLTFLP LSFWGKKKNI TKTFKINGSA NFSFNDEEMK
NVMDSSNGLS EYLDLSSPGP VEILTTVTES VTGISRNVST NVFFKQHDYI IEFFDYTTVL
KPSLNFTATV KVTRADGNQL TLEERRNNVV ITVTQRNYTE YWSGSNSGNQ KMEAVQKINY
TVPQSGTFKI EFPILEDSSE LQLKAYFLGS KSSMAVHSLF KSPSKTYIQL KTRDENIKVG
SPFELVVSGN KRLKELSYMV VSRGQLVAVG KQNSTMFSLT PENSWTPKAC VIVYYIEDDG
EIISDVLKIP VQLVFKNKIK LYWSKVKAEP SEKVSLRISV TQPDSIVGIV AVDKSVNLMN
ASNDITMENV VHELELYNTG YYLGMFMNSF AVFQECGLWV LTDANLTKDY IDGVYDNAEY
AERFMEENEG HIVDIHDFSL GSSPHVRKHF PETWIWLDTN MGYRIYQEFE VTVPDSITSW
VATGFVISED LGLGLTTTPV ELQAFQPFFI FLNLPYSVIR GEEFALEITI FNYLKDATEV
KVIIEKSDKF DILMTSNEIN ATGHQQTLLV PSEDGATVLF PIRPTHLGEI PITVTALSPT
ASDAVTQMIL VKAEGIEKSY SQSILLDLTD NRLQSTLKTL SFSFPPNTVT GSERVQITAI
GDVLGPSING LASLIRMPYG CGEQNMINFA PNIYILDYLT KKKQLTDNLK EKALSFMRQG
YQRELLYQRE DGSFSAFGNY DPSGSTWLSA FVLRCFLEAD PYIDIDQNVL HRTYTWLKGH
QKSNGEFWDP GRVIHSELQG GNKSPVTLTA YIVTSLLGYR KYQPNIDVQE SIHFLESEFS
RGISDNYTLA LITYALSSVG SPKAKEALNM LTWRAEQEGG MQFWVSSESK LSDSWQPRSL
DIEVAAYALL SHFLQFQTSE GIPIMRWLSR QRNSLGGFAS TQDTTVALKA LSEFAALMNT
ERTNIQVTVT GPSSPSPVKF LIDTHNRLLL QTAELAVVQP TAVNISANGF GFAICQLNVV
YNVKASGSSR RRRSIQNQEA FDLDVAVKEN KDDLNHVDLN VCTSFSGPGR SGMALMEVNL
LSGFMVPSEA ISLSETVKKV EYDHGKLNLY LDSVNETQFC VNIPAVRNFK VSNTQDASVS
IVDYYEPRRQ AVRSYNSEVK LSSCDLCSDV QGCRPCEDGA SGSHHHSSVI FIFCFKLLYF
MELWL
