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Database: UniProt
Entry: A0A0D9RNK9_CHLSB
LinkDB: A0A0D9RNK9_CHLSB
Original site: A0A0D9RNK9_CHLSB 
ID   A0A0D9RNK9_CHLSB        Unreviewed;      1201 AA.
AC   A0A0D9RNK9;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=CD109 molecule {ECO:0000313|Ensembl:ENSCSAP00000010198.1};
GN   Name=CD109 {ECO:0000313|Ensembl:ENSCSAP00000010198.1};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000010198.1, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000010198.1, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000010198.1}
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; AQIB01133011; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01133012; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01133013; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01133014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01133015; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01133016; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A0D9RNK9; -.
DR   STRING; 60711.ENSCSAP00000010198; -.
DR   Ensembl; ENSCSAT00000012152.1; ENSCSAP00000010198.1; ENSCSAG00000014064.1.
DR   eggNOG; KOG1366; Eukaryota.
DR   GeneTree; ENSGT00940000155926; -.
DR   OMA; EVHIYFE; -.
DR   Proteomes; UP000029965; Chromosome 17.
DR   Bgee; ENSCSAG00000014064; Expressed in fibroblast and 5 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; 1.50.10.20; -; 1.
DR   Gene3D; 2.20.130.20; -; 1.
DR   Gene3D; 2.60.120.1540; -; 1.
DR   Gene3D; 2.60.40.1930; -; 1.
DR   Gene3D; 2.60.40.1940; -; 1.
DR   Gene3D; 2.60.40.690; Alpha-macroglobulin, receptor-binding domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 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; 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; 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; 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   Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW   Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900}.
FT   DOMAIN          224..355
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          449..540
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   DOMAIN          1067..1151
FT                   /note="Alpha-macroglobulin receptor-binding"
FT                   /evidence="ECO:0000259|SMART:SM01361"
SQ   SEQUENCE   1201 AA;  134309 MW;  E400BBA3248C81D0 CRC64;
     MNSKHLNGTI VAKYTYGKPV KGDVTLTFLP LSFWGKKKNI TKTFKINGSV NFSFNDEEMK
     NIMDSSNGLD VASPGPVEIL ATVTESLTGI ARNASTNVFF KQHDYIIEFF DYTTVLKPSL
     NFTATVKVTR ADGNQLTLEE RRNNVVIAVT QGNCTECWSG SNSGNQKMET VQKINYTVPQ
     NGTFKIGFPI LEDSSELQLK AYFLGSKSSI AVHSMFKSPS KTYIQLKTRD ENIKVGSPFE
     LVVSGNKRLK ELSYMVVSRG QLVAVGKQNS TIFSLTPENS WTPKACVIVY YIEDDGEIIN
     DVLKIPVQLV FKNKIKLYWS KVKAEPSEKV SLRMSVTQPD SIAGIVAVDK TVNLMYASND
     LTMENVVHEL ELYNTGYYLG MFMNSFAVFQ ECGLWVLTDA NLTKDYIDGV YDNAEYAEKF
     MEENEGHVVD IQDFSLGSSP HVRKHFPETW IWLDTNMGSR IYQEFEVTVP DSITSWVATG
     FVISEDLGLG LTKTPVELQA FQPFFIFLNL PYSVIRGEEF ALEITIFNYL KDTTEVKVII
     EKSDKFDILM TSSEINATGH QQTILVPSED GATVLFPIRP THLGEIPITV TALSPTASDA
     ITQMILVKAE GIEKSYSQSI LLDLTDNRLQ STLKTLSFSF PPNTVTGSER VQITAIGDVL
     GPSINGLASL IRMPYGCGEQ NMIHFAPNIY ILDYLTKKKQ LTDNLKEKAL SFMRQGYQRE
     LLYQREDGSF SAFGNYDASG STWLSAFVLR CFLEADPYID IDQNVLHRTY TWLKERQKSN
     GEFWEPGKVI HSELQGGNKS PVTLTAYIVT SLLGYRKYQP NIDVQESIHF LESEFSRGIS
     DNYTLALIAY ALSSVGSPKA KEALNMLTSR AEQEGGMQFW VSSESKLSDS WQPRSLDIEV
     AAYALLSHFL QFQASEGIPI MRWLSRQRNS LGGFASTQDT IVALKALSEF AALMITERTN
     IQVTVMGPSA PSPIKFLIDT HNRLLLQTAE LAVVQPTAVN ISANGFGFAI CQLNVVYNVK
     DSGSSRRRRS IQNQEAFDLD VAVKENKDDL NHVDLNVCTR FLGPARSGMA LMEVNLLSGF
     MVPSDTIPLS ETVKKVEYDH GKLNLYLDSV NETQFCVDIP AVRNFKVSNT QDASVSIVDY
     YEPRRQAVRS YNSEAKLSSC DLCSDVQGCR PCEDGAVGSH HHPSVIFIFC FMLLYFLELW
     P
//
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