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Database: UniProt
Entry: A0A3Q2LH88_HORSE
LinkDB: A0A3Q2LH88_HORSE
Original site: A0A3Q2LH88_HORSE 
ID   A0A3Q2LH88_HORSE        Unreviewed;      1415 AA.
AC   A0A3Q2LH88;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 3.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=CD109 molecule {ECO:0000313|Ensembl:ENSECAP00000040290.3};
GN   Name=CD109 {ECO:0000313|VGNC:VGNC:16244};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000040290.3, ECO:0000313|Proteomes:UP000002281};
RN   [1] {ECO:0000313|Ensembl:ENSECAP00000040290.3, ECO:0000313|Proteomes:UP000002281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000040290.3,
RC   ECO:0000313|Proteomes:UP000002281};
RX   PubMed=19892987; DOI=10.1126/science.1178158;
RG   Broad Institute Genome Sequencing Platform;
RG   Broad Institute Whole Genome Assembly Team;
RA   Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA   Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA   Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA   Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA   Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA   Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA   Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA   Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA   Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA   Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT   "Genome sequence, comparative analysis, and population genetics of the
RT   domestic horse.";
RL   Science 326:865-867(2009).
RN   [2] {ECO:0000313|Ensembl:ENSECAP00000040290.3}
RP   IDENTIFICATION.
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000040290.3};
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   Ensembl; ENSECAT00000057034.3; ENSECAP00000040290.3; ENSECAG00000023066.4.
DR   VGNC; VGNC:16244; CD109.
DR   GeneTree; ENSGT00940000155926; -.
DR   Proteomes; UP000002281; Chromosome 10.
DR   Bgee; ENSECAG00000023066; Expressed in articular cartilage of joint and 23 other cell types or tissues.
DR   ExpressionAtlas; A0A3Q2LH88; baseline.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
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; 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; 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:UP000002281};
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..1415
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5040352373"
FT   DOMAIN          468..599
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          693..784
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   DOMAIN          1311..1395
FT                   /note="Alpha-macroglobulin receptor-binding"
FT                   /evidence="ECO:0000259|SMART:SM01361"
SQ   SEQUENCE   1415 AA;  157963 MW;  80325E4B1E0DF590 CRC64;
     MRGPRPLSAA QLVCVWTAAL AAGPGPRFLV TAPGIIRPGG NVTIGVELLE HSPPQVTVKA
     ELVKKAANLT VSVLEAEGLF EKGSFKTLIL PSLPLNSADE IYELHVAGRA QDEILFSNST
     RLSFETKRMT VFIQTDKSLY KPKQDVKFRI VTLFSDFKPC RTAVNILIKD PKSNLIQQWL
     SEQSDLGVIS KTFRLSSHPI LGDWSIQVQV NDQMYYQSFQ VSEYVLPKFE VALQTPLYCS
     LNSKSLNGTV IAKYTYGKPV KGDVTLTFLP LSFWGMKKNI TKKFKINGYA NFSFNDEEMK
     KVMEFSDGLS EHVYLSSPGP VEILATVTES LTGISRNASS NVFFKQHDHI IEFFDYATVL
     KPSLNFTATV KVTRSDGNQL TPEERRTNVV ITVTQRNYTV YWSRWNSRDQ EVEAVQIINY
     TVPQNGIFKI EFPILDDSSE LQLKASFLNS VSSMAVHGMF MSPSKTYIQL KTRDENIKVG
     SPFELVVSGN KQLKELSYMV VSRGQLVAVG KQNSTAFSLT PENSWAPKAC IIVYYIEDDG
     EIINDVLKIP VHLVFKNKIN LFWSKANAEP SEKVSLRVSV TQPDSVVGIV AVDKSVNLMN
     ASNDITMENV VHELELYNTG YYLGMFMNSF AVFQECGLWV LTDAHLVKDS IDGVYDSVES
     AERFVEESEA YMVDLRDFAL GGRPHVRRHF PETWLWLDAN MGSRMDEEFE VTVPDSITSW
     VATAFVISED LGLGLTTTPV ELQAFQPFFI FLNLPYSVIR GEEFALEVTI FNYLKDVTEV
     KVIIEKSDKF DILMASNEIN ATGHQQTILV PSEDGATVLF PIKPIRLGEI PITVTAVSLA
     ASDAVTQKIL VKAEGIEKSY SQSILLDLTD NKLQTTLKTL SFSFPPDTVS GSARVQVTAI
     GDILGSSING LASLIRMPYG CGEQNMINFA PNIYVLDYLT KKKQLTENLK EKALSFMRQG
     YQRELLYQRE DGSFSAFGKD DPSGSTWLSA FVLRCFLEAD PYIDIDQNVL HRTYTWLKGR
     QKSSGEFWEP GRVIHSELQG GSTSPVTLTA YIVTSLLGYK KYQPNIDVQE SINFLESEFN
     RGISDNYTLA LITHALSSVR SPKAKEALDM LTWRAEREGD TQFWVSSVSR LSESWQPSSL
     DIEVAAYALL SHFLQGQLSA GVPVMRWLSR QRNRLGGFVS TQDTIVALKA LSEFAALMNT
     ERTNIQVTVM GPTSPSPIKF LIDTQNRFLL QTAELAAVQP TTVNISAKGL GFAVCQLNII
     YNVKDSGSSR SQKSIQNQEA FDLDVAVKDN KDDLNHLNLN VCTRFLGPAR SGMALMEVNL
     LSGFMVPSDA IPLSETLKKV EHEHGKLNLY LDSVNETLFC VDIPAVRNFK VSNTQDALVS
     IVDYYEPRRQ AVRSYNSEVK LSSCDLCGDD HSCRP
//
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