ID A0A2I3SDS4_PANTR Unreviewed; 1446 AA.
AC A0A2I3SDS4;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=CD109 molecule {ECO:0000313|Ensembl:ENSPTRP00000075183.1};
GN Name=CD109 {ECO:0000313|Ensembl:ENSPTRP00000075183.1,
GN ECO:0000313|VGNC:VGNC:2656};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000075183.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000075183.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000075183.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. {ECO:0000256|ARBA:ARBA00010952}.
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DR EMBL; AACZ04024866; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPTRT00000088248.1; ENSPTRP00000075183.1; ENSPTRG00000018349.5.
DR VGNC; VGNC:2656; CD109.
DR GeneTree; ENSGT00940000155926; -.
DR InParanoid; A0A2I3SDS4; -.
DR Proteomes; UP000002277; Chromosome 6.
DR Bgee; ENSPTRG00000018349; Expressed in fibroblast and 19 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0050431; F:transforming growth factor beta binding; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0061045; P:negative regulation of wound healing; IEA:Ensembl.
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; 1.20.50.70; -; 1.
DR Gene3D; 1.50.10.20; -; 1.
DR Gene3D; 2.20.130.20; -; 2.
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; 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.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1446
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014159037"
FT DOMAIN 469..600
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 694..785
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1312..1396
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
SQ SEQUENCE 1446 AA; 161611 MW; AA68493133132786 CRC64;
MQGPPLLTAA HLLCVCTAAL AVAPGPRFLV TAPGIIRPGG NVTIGVELLE HCPSQVTVKA
ELLKTASNLT VSVLEAEGVF EKGKINSIKS YPSLPLNSAD EIYELRVTGR TQDEILFSNS
TRLSFETKRI SVFIQTDKAL YKPKQEVKFR IVTLFSDFKP YKTSLNILIK DPKSNLIQQW
LSQQSDLGVI SKTFQLSSHP ILGDWSIQVQ VNDQTYYQSF QVSEYVLPKF EVTLQTPLYC
SMNSKHLNGT ITAKYTYGKP VKGDVTLTFL PLSFWGKKKN ITKTFKINGS ANFSFNDEEM
KNVMDSSNGL SEYLDLSSPG PVEILTTVTE SVTGISRNAS TNVFFKQHDY IIEFFDYTTV
LKPSLNFTAT VKVTRADGNQ LTLEERRNNV VITVTQRNYT EYWSGSNSGN QKMEAVQKIN
YTVPQSGTFK IELPILEDSS ELQLKAYFLG SKSSMAVHSL FKSPSKTYIQ LKTRDENIKV
GSPFELVVSG NKRLKELSYM VVSRGQLVAV GKQNSTMFSL TPENSWTPKA CVIVYYIEDD
GEIISDVLKI PVQLVFKNKI KLYWSKVKAE PSEKVSLRIS VTQPDSIVGI VAVDKSVNLM
NASNDITMEN VVHELELYNT GYYLGMFMNS FAVFQECGLW VLTDANLTKD YIDGVYDNAE
YAERFMEENE GHIVDIHDFS LGSSPHVRKH FPETWIWLDT NMGSRIYQEF EVTVPDSITS
WVATGFVVSE DLGLGLTTTP AELQAFQPFF IFLNLPYSVI RGEEFALEIT IFNYLKDATE
VKVIIEKSDK FDILMTSSEI NATGHQQTLL VPSEDGATVL FPIRPTHLGE IPITVTALSP
TASDAITQMI LVKAEGIEKS YSQSILLDLT DNRLQSTQKT LSFSFPPNTV TGSERVQITA
IGDVLGPSIN GLASLIRMPY GCGEQNMINF APNIYILDYL TKKKQLTDNL KEKALSFMRQ
GYQRELLYQR EDGSFSAFGN YDPSGSTWLS AFVLRCFLEA DPYIDIDQNV LHRTYTWLKG
HQKSNGEFWD PGRVIHSELQ GGNKSPVTLT AYIVTSLLGY RKYQPNIDVQ ESIHFLESEF
SRGISDNYTL ALITYALSSV GSPKAKEALN MLTWRAEQEG GMQFWVSSES KLSDSWQPRS
LDIEVAAYAL LSHFLQFQTS EGIPIMRWLS RQRNSLGGFA SSQDTTVALK ALSEFAALMN
TERTNIQVTV MGPSSPSPAK FLIDTHNRLL LQTAELAVVQ PTAVNISANG FGFAICQLNV
VYNVKASGSS RRRRSIQNQE AFDLDVAVKE NKDDLNHVDL NVCTSFSGPG RSGMALMEVN
LLSGFMVPSD AISLSETVKK VEYDHGKLNL YLDSVNETQF CVNIPAVRNF KVSNTQDASV
SIVDYYEPRR EAVRSYNSEV KLSSCDLCSD VQGCRPCEDG ASGSHHHSSV IFIFCFKLLY
FLELWL
//
