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 27-MAR-2024, entry version 155. 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)"; 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; 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; 97. DR IntAct; Q6YHK3; 41. DR MINT; Q6YHK3; -. DR STRING; 9606.ENSP00000287097; -. DR MEROPS; I39.006; -. DR CarbonylDB; Q6YHK3; -. DR GlyConnect; 795; 30 N-Linked glycans (12 sites). DR GlyCosmos; Q6YHK3; 14 sites, 32 glycans. DR GlyGen; Q6YHK3; 18 sites, 32 N-linked glycans (12 sites), 1 O-linked glycan (2 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; 9606-ENSP00000287097; -. DR PeptideAtlas; Q6YHK3; -. DR ProteomicsDB; 67842; -. [Q6YHK3-1] DR ProteomicsDB; 67843; -. [Q6YHK3-2] DR ProteomicsDB; 67844; -. [Q6YHK3-3] DR ProteomicsDB; 67845; -. [Q6YHK3-4] DR Pumba; Q6YHK3; -. DR Antibodypedia; 2141; 452 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 AGR; HGNC:21685; -. 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; 2970602at2759; -. 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 1154 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 186 other cell types or tissues. 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:0098552; C:side of membrane; IEA:UniProtKB-KW. 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: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; 1.50.10.20; -; 1. DR Gene3D; 2.20.130.20; -; 1. DR Gene3D; 2.60.120.1540; -; 1. DR Gene3D; 2.60.40.1930; -; 2. DR Gene3D; 2.60.40.1940; -; 1. DR Gene3D; 2.60.40.2950; -; 1. DR Gene3D; 6.20.50.160; -; 1. DR Gene3D; 2.60.40.690; Alpha-macroglobulin, receptor-binding domain; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 2. 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; IPR047565; Alpha-macroglob_thiol-ester_cl. 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 PANTHER; PTHR11412:SF162; CD109 ANTIGEN; 1. DR PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1. 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 SMART; SM01419; Thiol-ester_cl; 1. DR SUPFAM; SSF49410; Alpha-macroglobulin receptor domain; 1. DR SUPFAM; SSF81296; E set domains; 1. DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1. DR PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1. DR Genevisible; Q6YHK3; HS. 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 //