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Database: UniProt
Entry: A0A0V1CP07_TRIBR
LinkDB: A0A0V1CP07_TRIBR
Original site: A0A0V1CP07_TRIBR 
ID   A0A0V1CP07_TRIBR        Unreviewed;      1501 AA.
AC   A0A0V1CP07;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Antigen-like protein {ECO:0000313|EMBL:KRY50732.1};
GN   Name=CD109 {ECO:0000313|EMBL:KRY50732.1};
GN   ORFNames=T03_47 {ECO:0000313|EMBL:KRY50732.1};
OS   Trichinella britovi (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY50732.1, ECO:0000313|Proteomes:UP000054653};
RN   [1] {ECO:0000313|EMBL:KRY50732.1, ECO:0000313|Proteomes:UP000054653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS120 {ECO:0000313|EMBL:KRY50732.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRY50732.1}.
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DR   EMBL; JYDI01000142; KRY50732.1; -; Genomic_DNA.
DR   Proteomes; UP000054653; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
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; 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:SF179; LD23292P; 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; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1.
DR   PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
PE   4: Predicted;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Thioester bond {ECO:0000256|ARBA:ARBA00022966}.
FT   DOMAIN          492..627
FT                   /note="Alpha-2-macroglobulin bait region"
FT                   /evidence="ECO:0000259|SMART:SM01359"
FT   DOMAIN          752..843
FT                   /note="Alpha-2-macroglobulin"
FT                   /evidence="ECO:0000259|SMART:SM01360"
FT   DOMAIN          1352..1441
FT                   /note="Alpha-macroglobulin receptor-binding"
FT                   /evidence="ECO:0000259|SMART:SM01361"
SQ   SEQUENCE   1501 AA;  167747 MW;  09103D7B9ECD63AD CRC64;
     MNTTSPSACL LLKIFQLPLL FLSLLLLLFL CDGAIQQNYT GSYVILAPRL VRPNLPYVIS
     VNLLESRQPV VIRARILDSQ NQSIAHTWGQ DLQSGKLTEV RIEKIPSHLP PETVYTLFVQ
     GETVSGRVLF QKSAKLEFVH KSLSIFIQTD KGIYKPGSDV HIRVVVVEPN MKPYKGAANI
     TIMDPSGNMI VQHLDVPIVA GICGMNDSLM LRLTSAPALG QWQITVDVDG ETQFQKFTVE
     KYVLPKFEVK VTPPSVSTIS DDITVFVSAK YTNGRGVEGN VTIKAEYPWP YYGSEELQDV
     VKKTTLDHVG EAAFQFANEE LRQKKLINEY GYNQIKFTAI VTERLTGETR NGSSTVTVHQ
     HPIKVELIRS SDFFKAGINY TFRVAVKTQD DKPFISDSHS DIFLSVDFII RQLHHHNENT
     TADFANFTIF DPKREKYNQV VKLESDGTQV VTISTPFNAS SMRIEAHYGG EESNVYTFDY
     IDASHSPSNN FLQIISKQDE ISDQKFLTFD VIASTVVKEV YAFVIARATI VWSGQVVFEN
     FKATLQIQSS KEMIPKARLL AYALIPDTKE ILVDALDFKF SNGFSDQINL SITPDTVEPN
     ENVTFSINAP PSSYVGLLVV DQTVLLMQSP NDITLEAVEN EILSYELFSY GYHGLTQVAI
     DRRKKRTICY RCGVFGAGSK DAYSIFQNSG IIVITDAFLY QQLNSPFLFR VAAPALASLS
     ADVDNDLMVG SVMTKSGSTS LNVRLRSHFP ETWIWADLFA NEHGLAVYNA VAPDTITSWI
     ASAFSLSDQY GLNALSDAKK VTVFRPFFIR LQLPYSVKRG EAIALQVLIF NYLDKDEKVN
     VILDYHKDSG FEFIVKKSVS SSMIKKSVEV KPENSKTVTV GTLKLSVKAF AQSAADAIQV
     PLLVEAEGYP VSYTRSFAID MKERNTFKQS FQLDHPEDMI DDSMKIEVSV IGDIMAPVIK
     NLDSLIHMPD GCGEQNMIHF VPNIAVMQYL ISTNRLESNL KQTLLRYMEA GYQRELTYRR
     NDDSYSAFGN ADQQGSTWLT AFVVRSFSEA KSFIFIDEEK LKLSAAFLAN QQKENGMFEE
     NGQVLHSGLQ GGSGQGGVPL TAYVYIALLK TGTNNLEALN YLEQSLDYIS NNTYAVSITA
     YALHLANSSK KDAAFYLLEK LSNSKDGRKF WAAESSSESN NGKNMSWYEK PRPADVESTA
     YALLVHVLRG EASNAFPIVR WLTMQQDAFG GFSSSQDTVV GLQALAAFAE ATYSANVEMD
     VTVKNGNEEA AFAINSKNSL VLQTYEIRNF VERQIDIFAT GRGLAFAQIK WRYNVKSLDN
     NRPFFCETDV SQQAYTALTV SFCCKYMFEG TSNMAIMELT APSGFVIDVQ QLNGLTDTNQ
     LQMVETKKQD TQANIYFDSI GISPICFNVS SKLAYQVADQ KPAIVRLYDY YEPQNRIEFE
     YKVKKEVSIE DACGDSCYAE ISSAALTEQP ASKGTMPNCC SIIQTLPVLI YLFYYSVLRF
     H
//
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