ID A0A0B2UV01_TOXCA Unreviewed; 1120 AA.
AC A0A0B2UV01;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Antigen-like protein {ECO:0000313|EMBL:KHN73218.1};
GN Name=CD109 {ECO:0000313|EMBL:KHN73218.1};
GN ORFNames=Tcan_12026 {ECO:0000313|EMBL:KHN73218.1};
OS Toxocara canis (Canine roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Toxocaridae; Toxocara.
OX NCBI_TaxID=6265 {ECO:0000313|EMBL:KHN73218.1, ECO:0000313|Proteomes:UP000031036};
RN [1] {ECO:0000313|EMBL:KHN73218.1, ECO:0000313|Proteomes:UP000031036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PN_DK_2014 {ECO:0000313|EMBL:KHN73218.1};
RA Zhu X.-Q., Korhonen P.K., Cai H., Young N.D., Nejsum P.,
RA von Samson-Himmelstjerna G., Boag P.R., Tan P., Li Q., Min J., Yang Y.,
RA Wang X., Fang X., Hall R.S., Hofmann A., Sternberg P.W., Jex A.R.,
RA Gasser R.B.;
RT "Genetic blueprint of the zoonotic pathogen Toxocara canis.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. {ECO:0000256|ARBA:ARBA00010952}.
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:KHN73218.1}.
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DR EMBL; JPKZ01003130; KHN73218.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B2UV01; -.
DR STRING; 6265.A0A0B2UV01; -.
DR OMA; ETHEHYL; -.
DR Proteomes; UP000031036; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.60.40.690; 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; 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; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR PANTHER; PTHR11412:SF175; TEP (THIOLESTER CONTAINING PROTEIN); 1.
DR Pfam; PF00207; A2M; 1.
DR Pfam; PF07677; A2M_recep; 1.
DR Pfam; PF07678; TED_complement; 1.
DR SMART; SM01360; A2M; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000031036};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Thioester bond {ECO:0000256|ARBA:ARBA00022966};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1093..1116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 288..393
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 959..1048
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
SQ SEQUENCE 1120 AA; 124452 MW; C2362FF618513607 CRC64;
MDLADGVAFQ EALAVPPILP PAVPEVVEAV NDPASAEGAI IETRVRSSFP ELWIWYLAEV
LKSGSELTCF KLSVYMMEMT FVRPMAAFDG TASPVALTTA SVHQPSSDTV PTFKKRTMFP
ETWIWNDLLL FNSVEAKCIL RSGYYHIARV ERPDRMRLDG LPGYMRQTVH VAHTPRVMPL
RMSTTPVAPK IRCKFPESWI WGNLRTKDVI ESDIYNLLGV DMNQGIFVLE ANIVLIVFVA
YVDSRAVLVF DRFFNKEPLG DAVFADATRL FELNYFTVMR TRTYFPHTWL FTCLRTELVD
PVHEHNEIHQ RGTGEAIYEA TAPDTITSWV ASAFAINDET GLGVAPVTSK LTIFRPFFIR
LNLPYSVKRG EKFALQVLVF NYMDTEQDVT VILKHDDGAG FDFLQKDGTS KKPLSKESKS
KNYNMRFVSV PGGGVSKAVY FPIVPTHIGD VKLSVIAQSA KAGDAVEQPL KVEPEGYRVD
RNVPLVIDLS DKATFSRKVD LQYPLDAVDG SKKARVDIIG DIMGPVLANI DSLVKMPYGC
GEQNMVNFVP NIVVLKYLKA TKRAGGQIEA KALKYMESGY QRELTYRRDD NSFSAFGQND
KHGSTWLTAF VVRSFKQAQA FIFVDDQILQ KSIAFLNAQQ QQENGGFAER GEVHHKDMQG
GAAEGGVPLT AYVLIAFLEN GVKNDKAQHY LEQHLEEIKD DPYALAVVTY ALHLTGSTKK
SEALKMLESH KVEDSDGSVH WTAKAGGDKT KDTQRYFYQP RPVDVEMTSY ALLTYMLNDD
VEKGLPIVRW LTAQRNALGG FSSTQDTVMA LQALGVYAEK AFSPTFNISV TVTNGANNQQ
FEDTVMALQA LGVYAEKAFS PTFNISVTVT NGANNQQFEV TPENAIVLQS YELSNLEEPV
LVEAKGRGVI FAQAQYSYYR VATKDDTPFY CTKDVREVHG GNRLQLDLCC NYTKPGQRSN
MAVAEVNALT GYRFDGDEIG RLTEIADLQR AELDKEDTKM NLYFNPLGST PVCLSLFSDM
VYQVADQKPA QMVLFDYYDP EQQVKSSYSA KQTRSLQDAC PDCWPSVETS DEGSGVTATR
ADASSAAPNA TRAGVPLLGL LLLAVLTFVS PLFTFAGSAR
//
