ID A0A091HEM5_BUCRH Unreviewed; 1456 AA.
AC A0A091HEM5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Ovostatin {ECO:0000313|EMBL:KFO93272.1};
DE Flags: Fragment;
GN ORFNames=N320_07265 {ECO:0000313|EMBL:KFO93272.1};
OS Buceros rhinoceros silvestris.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Bucerotiformes; Bucerotidae; Buceros.
OX NCBI_TaxID=175836 {ECO:0000313|EMBL:KFO93272.1, ECO:0000313|Proteomes:UP000054064};
RN [1] {ECO:0000313|EMBL:KFO93272.1, ECO:0000313|Proteomes:UP000054064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N320 {ECO:0000313|EMBL:KFO93272.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. {ECO:0000256|ARBA:ARBA00010952}.
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DR EMBL; KL532526; KFO93272.1; -; Genomic_DNA.
DR Proteomes; UP000054064; Unassembled WGS sequence.
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; -; 2.
DR Gene3D; 2.60.120.1540; -; 1.
DR Gene3D; 2.60.40.1930; -; 2.
DR Gene3D; 2.60.40.1940; -; 1.
DR Gene3D; 2.60.40.690; 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; IPR040839; MG4.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR PANTHER; PTHR11412:SF150; ZGC:171445 PROTEIN-RELATED; 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; PF17789; MG4; 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:UP000054064};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1456
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001874308"
FT DOMAIN 453..600
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 736..826
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1364..1452
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
FT NON_TER 1456
FT /evidence="ECO:0000313|EMBL:KFO93272.1"
SQ SEQUENCE 1456 AA; 164352 MW; F60D213C0E9EB07F CRC64;
MWSRILLSIL SLNWIATVSS EPQYVLLVPT VVRSDSPQTA CVQFHNVSEP LSVNIILEYG
SIPKTIFEES VTKNDFFKCY EFKVPPATSD PLAFISFSAK GTTVNITERR SVAIQNVDNF
IFIQTDKPIY KPAQKVLFRV VALDSQFRPV QETVIRLFPT LQDPEQNKIF QWLDVASKHG
IVQLSFPLIS EPILGSYHIT VEKKSGEKEH QFFTVEEYVL PKFEVTISVP KRISFFDEEI
RVNVCASYTY GQPVQGNARI NVCQRHFYSP RCAKNRKESC ESVTGLLGKD GCLNTVVSVK
TLQLYRSYDR MYTSLNVESI VTENGTGIQM KGYDYVSVNQ ENERAIFKNM DTYYKRGIPY
YGEITVTDMD GKPVADRTVL LELNEEYLAN YTTDKNGTAA FSIDTSNFFD PSLKLSVRQA
TDDCEDFFIW SKDNKPQALF FVRRFYSRTN SFVKIEQVKE KLSCGQQQTI NIHYVLNREG
YGNTSHTDFY YVVMKKGKII LSGQKQVTIS GASRGTFTIT LTVTEKLAPS ARLLVYTLHP
HGEIVADSSW IRSEVCFKNK LQLEFSEKEG LPGSKVSLHL EAAANSYCAL RAVDESVLLL
RPERELSAES VYYQQHVSDL YGYYYNGLNL QDDKPEGCTP VKTTFFDGLY YEPVNVSRDG
DVYRIFRDMG LKVFTNNVLR KPVLCNEDKS DMEDYPGYFE HSVAHGNSYS SGKRSCIHYL
RSHGGVNTVR KFFPETWIWE LVHTDSRGEV NVFYTIPDTI TEWKASAFCV QDDAGFGISS
PVSLRAFLPF FVDLTLPYSV IRGEKFNLIA NVFNYLNRCI QISAVLAKSS DYEAEILSPE
GNTARLCAGE RKTYIWAVSP LKLGEVKFTI TAEAKLNTEG SGNSTSPEEE TIRRDTLIQT
LLVEPEGIKK ELTQSSLVCT KGKMISEPVS LSLPRNLVQG SARAYFSVVG DILGTALRNM
ENLLHMPYGC GEQNMALFTP NIYALDYLNK TGQLTEEIRI KGTGYLSTGY QKQLSYKHRD
GSYSSFGTRD REGSVWLSAF VYKSFAQAKR YIYIDDNVQS QTLIWLASKQ KSDGCFENAG
SHFNNALKDG EEGEYSLTAY VVAALLEAGH SVAHPIVQSG MNCLETAFSN GIHSLYNQAL
FAYAYGLADK EERSQFFLEK LDKTATRDGG SVHWQRGNKP PADHVPVFYS RAPSAEIEMT
SYALLALLNK AKLTPEDLSY CSRIVHWLVK QQNPYGGFSS SQDTVVALQA LAQYGYLTFS
KKPLNTVKVN FMESPSKTFQ VNDKNRFLLQ QASLPTIPGN YSVEVNGTGC VYLQTILRYN
IHLPKKVAGF YLSVQPANVS CTGNFPPKFD LVLSTSYTGN REVSNMAIID VKMLSGFVPV
RSSLEKLRYE NSVVDHVDIK NNHILFYLQK VSQKEINFSF SVEQSLPVSD IKPVPVHIYD
YYETDEYALA EYKTPC
//
