ID A0A091U776_PHALP Unreviewed; 1461 AA.
AC A0A091U776;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Ovostatin {ECO:0000313|EMBL:KFQ69903.1};
DE Flags: Fragment;
GN ORFNames=N335_05378 {ECO:0000313|EMBL:KFQ69903.1};
OS Phaethon lepturus (White-tailed tropicbird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Eurypygimorphae; Phaethontiformes;
OC Phaethontidae; Phaethon.
OX NCBI_TaxID=97097 {ECO:0000313|EMBL:KFQ69903.1, ECO:0000313|Proteomes:UP000053638};
RN [1] {ECO:0000313|EMBL:KFQ69903.1, ECO:0000313|Proteomes:UP000053638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N335 {ECO:0000313|EMBL:KFQ69903.1};
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; KK440035; KFQ69903.1; -; Genomic_DNA.
DR MEROPS; I39.002; -.
DR PhylomeDB; A0A091U776; -.
DR Proteomes; UP000053638; 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:SF170; OVOSTATIN; 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:UP000053638};
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..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..1461
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001882528"
FT DOMAIN 464..611
FT /note="Alpha-2-macroglobulin bait region"
FT /evidence="ECO:0000259|SMART:SM01359"
FT DOMAIN 746..836
FT /note="Alpha-2-macroglobulin"
FT /evidence="ECO:0000259|SMART:SM01360"
FT DOMAIN 1368..1456
FT /note="Alpha-macroglobulin receptor-binding"
FT /evidence="ECO:0000259|SMART:SM01361"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ69903.1"
FT NON_TER 1461
FT /evidence="ECO:0000313|EMBL:KFQ69903.1"
SQ SEQUENCE 1461 AA; 164026 MW; 43F4B5BB40D71C59 CRC64;
NCFLGIELIS FFCLPRKMWL KFLLAILLLN VTAAKEPELQ YVLMVPAVLQ TNSPGQVCLQ
FLNLNETISV RIILEYGAVN TTIFEKTMTA SNGLQCFNFT VPPISSAPLA FMSFSAKGTT
VSLEERRSVM IWNTESIVFV QTDKPIYKPG QSVMFRVVAL DFNFKPVQEM YPLIAIQDPR
GNRIFQWQNV TSEMNIIQIE FPLTEEPILG SYKIIIAKKS GDKTNHSFLV KEYVLPKFDV
TITAPESLTV LDSEFTVKVC GVYTYGQPVE AKVQLSVCRD FDLYGKCKKS PVCQSFTKDL
ETEGCLSQVF SSNIFELNRI GYMRNLDVKA IVTEKGTGLQ LTATQSISIT RVMSSIQFQN
MDRHYRRGIP YFGQIKLVDK DNSPISNEVI QLFVNNKNTD NFTTDDNGIA EFSIDTSKMF
DPEISLKATY KSSDQCHSEG WIEPSYPDAS LSIQRFYSWT SSFVRIEPLW KDLSCGQKMI
ITVHYVLNTE GYKSINMMNF YYVGMAKGKI VLTGEIKVNI QADQNGTFTI PLVVNEQMAP
ALRLLVYTLH PAKELVADSV QFPVEMCFKN KVQLQFSEMQ MPSASNVSLV IEAAANSFCA
VRAVDQGVLL VQSETELSAE MIYSLHPLQD FQGYIFNGLN LEDDPQDPCV SSDNIFHKGL
YYTPVMSGLG PDVYQFLRDM GMKFFTNSKV RQPVVCTSET VRRPPYFLNA GFMASTQHVK
SSAEVAREER GKRLILETIR EFFPETWIWD IVLINSTGKA NISYTIPDTI TEWKASAFCV
EDLVGFGISV PATMTAFQPF FVDLTLPYSV IRGEDFLLRA NVFNYLDHCI KINVLLSESL
DYQAKLISAE DDVCVCAKQR QTYVWNIFPK EMGNVVFSIT AETKDDGACG DKAPRNNSID
YRDTQMRTLL VEPEGIRRER TQNSLICTKD DVVTQDVVLD LPTNLVEGSV RASFSVVGDI
MGTAMQNVHQ LLQMPFGCGE QNMVLFAPNI YVLNYLNKTG QLSEEVKSKA IGYLVSGYQK
QLSYKHPDGS YSIFGTRDKE GNTWLTAFVY KSFAKSSHFI YVDDNVQAQT LMWLASKQKP
DGCFRSVGTL FNNALKGGAD AELLLSAYIT IAMLEAGHSG LYPVLRNAFY CLETASEKNI
SDVYTQALMA YAFCLAGKAE KCDSFLRELK KIDGSQHWDQ AEKSPSEKSP SFLDHAPSAE
VEMTSYVLLA LLYKPNQNQE DLTKASGIVQ WIIRQQNPYG GFSSTQDTVI ALQALAAYGE
ATYNSVTQNV VKITSKKPFE KVFIVNNANR LLLQETPLPE VPGKYSQSVN GSGCVLMQTV
LRYNIHLPEG AFGFSLTVNT SNASCPLDRP GKFDIVLISS YTGKRSSSNM VIIDVKMLSG
FVPVKSSLDK LIDGHTVMQV ENKKNHVLLY LENISQNKRK EITFSVEQDF VVTHPKPAPV
QIYDYYETEE YAVAQYISPC K
//
