OVOS_CHICK
ID OVOS_CHICK Reviewed; 1473 AA.
AC P20740;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Ovostatin;
DE AltName: Full=Ovomacroglobulin;
DE Flags: Precursor;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oviduct;
RX PubMed=7535598; DOI=10.3109/10425179409039712;
RA Nielsen K.L., Sottrup-Jensen L., Nagase H., Thoegersen H.C., Etzerodt M.;
RT "Amino acid sequence of hen ovomacroglobulin (ovostatin) deduced from
RT cloned cDNA.";
RL DNA Seq. 5:111-119(1994).
RN [2]
RP PROTEIN SEQUENCE OF 37-49.
RC TISSUE=Egg white;
RX PubMed=6408074; DOI=10.1016/s0021-9258(18)32203-8;
RA Nagase H., Harris E.D. Jr., Woessner J.F., Brew K.;
RT "Ovostatin: a novel proteinase inhibitor from chicken egg white. I.
RT Purification, physicochemical properties, and tissue distribution of
RT ovostatin.";
RL J. Biol. Chem. 258:7481-7489(1983).
RN [3]
RP PROTEIN SEQUENCE OF 710-743.
RX PubMed=2470748; DOI=10.1016/s0021-9258(18)81861-0;
RA Enghild J.J., Salvesen G., Brew K., Nagase H.;
RT "Interaction of human rheumatoid synovial collagenase (matrix
RT metalloproteinase 1) and stromelysin (matrix metalloproteinase 3) with
RT human alpha 2-macroglobulin and chicken ovostatin. Binding kinetics and
RT identification of matrix metalloproteinase cleavage sites.";
RL J. Biol. Chem. 264:8779-8785(1989).
RN [4]
RP PROTEIN SEQUENCE OF 976-1028.
RC TISSUE=Egg white;
RX PubMed=7680577; DOI=10.1016/0167-4838(93)90153-i;
RA Nielsen K.L., Sottrup-Jensen L.;
RT "Evidence from sequence analysis that hen egg-white ovomacroglobulin
RT (ovostatin) is devoid of an internal beta-Cys-gamma-Glu thiol ester.";
RL Biochim. Biophys. Acta 1162:230-232(1993).
CC -!- FUNCTION: Is able to inhibit all four classes of proteinases by a
CC unique 'trapping' mechanism. This protein has a peptide stretch, called
CC the 'bait region' which contains specific cleavage sites for different
CC proteinases. When a proteinase cleaves the bait region, a
CC conformational change is induced in the protein which traps the
CC proteinase. The entrapped enzyme remains active against low molecular
CC weight substrates (activity against high molecular weight substrates is
CC greatly reduced).
CC -!- SUBUNIT: Homotetramer, which consists of two pairs of disulfide-linked
CC chains.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Lacks the thioester bond found in other members of this family.
CC -!- PTM: Glycosylated; contains 56 glucosamine units per subunit.
CC -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC macroglobulin) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA55385.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X78801; CAA55384.1; -; mRNA.
DR EMBL; X78801; CAA55385.1; ALT_INIT; mRNA.
DR PIR; I50671; A20872.
DR AlphaFoldDB; P20740; -.
DR SMR; P20740; -.
DR STRING; 9031.ENSGALP00000036402; -.
DR MEROPS; I39.002; -.
DR PaxDb; P20740; -.
DR VEuPathDB; HostDB:geneid_396151; -.
DR eggNOG; KOG1366; Eukaryota.
DR PhylomeDB; P20740; -.
DR PRO; PR:P20740; -.
DR Proteomes; UP000000539; Unplaced.
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; 2.60.40.10; -; 2.
DR Gene3D; 2.60.40.690; -; 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; IPR011626; Alpha-macroglobulin_TED.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR001599; Macroglobln_a2.
DR InterPro; IPR002890; MG2.
DR InterPro; IPR041555; MG3.
DR InterPro; IPR040839; MG4.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
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 SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF49410; SSF49410; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Bait region; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Protease inhibitor; Reference proteome; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..36
FT /evidence="ECO:0000269|PubMed:6408074"
FT CHAIN 37..1473
FT /note="Ovostatin"
FT /id="PRO_0000000062"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 342
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 527
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 757
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 46
FT /note="M -> V (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 718..722
FT /note="THHVK -> IHTVA (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 743
FT /note="E -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1473 AA; 166355 MW; A33C6847A14179BF CRC64;
MHCFLGREIL SFFCLTVRKM WLKFILAILL LHAAAGKEPE PQYVLMVPAV LQSDSPSQVC
LQFFNLNQTI SVRVVLEYDT INTTIFEKNT TTSNGLQCLN FMIPPVTSVS LAFISFTAKG
TTFDLKERRS VMIWNMESFV FVQTDKPIYK PGQSVMFRVV ALDFNFKPVQ EMYPLIAVQD
PQNNRIFQWQ NVTSEINIVQ IEFPLTEEPI LGNYKIIVTK KSGERTSHSF LVEEYVLPKF
DVTVTAPGSL TVMDSELTVK ICAVYTYGQP VEGKVQLSVC RDFDSYGRCK KSPVCQSFTK
DLDTDGCLSH ILSSKVFELN RIGYKRNLDV KAIVTEKEQV CNLTATQSIS ITQVMSSLQF
ENVDHHYRRG IPYFGQIKLV DKDNSPISNK VIQLFVNNKN THNFTTDING IAPFSIDTSK
IFDPELSLKA LYKTSDQCHS EGWIEPSYPD ASLSVQRLYS WTSSFVRIEP LWKDMSCGQK
RMITVYYILN TEGYEHINIV NFYYVGMAKG KIVLTGEIKV NIQADQNGTF MIPLVVNEKM
APALRLLVYM LHPAKELVAD SVRFSIEKCF KNKVQLQFSE KQMLTTSNVS LVIEAAANSF
CAVRAVDKSM LLLKSETELS AETIYNLHPI QDLQGYIFNG LNLEDDPQDP CVSSDDIFHK
GLYYRPLTSG LGPDVYQFLR DMGMKFFTNS KIRQPTVCTR ETVRPPSYFL NAGFTASTHH
VKLSAEVARE ERGKRHILET IREFFPETWI WDIILINSTG KASVSYTIPD TITEWKASAF
CVEELAGFGM SVPATLTAFQ PFFVDLTLPY SIIHGEDFLV RANVFNYLNH CIKINVLLLE
SLDYQAKLIS PEDDGCVCAK IRKSYVWNIF PKGTGDVLFS ITAETNDDEA CEEEALRNIR
IDYRDTQIRA LLVEPEGIRR EETQNFLICM KDDVISQDVA IDLPTNVVEG SPRPSFSVVG
DIMGTAIQNV HQLLQMPFGN GEQNMVLFAP NIYVLDYLDK TRQLSEDVKS KTIGYLVSGY
QKQLSYKHPD GSYSTFGIRD KEGNTWLTAF VYKSFAEASR FIYIDDNVQA QTLIWLATKQ
KTDGCFQSTG ILVNNAMKGG VENELSLSAY ITIALLEAGH SMSHTVIRNA FYCLETASEK
NITDIYTQAL VAYAFCLAGK AEICESFLRE LQKSAKEVDG SKYWEQNQRS APEKSHLLDH
VQSTDVEITS YVLLALLYKP NRSQEDLTKA SAIVQWIIRQ QNSYGGFASM QDTVVALQAL
AAYGAATYNS VTQNVIKINS KNTFEKVFTV NNENRLLLQQ TPLPQVPGKY SLTVNGTGCV
LIQTALRYNI HLPEGAFGFS LSVQTSNASC PRDQPGKFDI VLISSYTGKR SSSNMVIIDV
KMLSGFVPVK SSLDQLIDDH TVMQVEYKKN HVLLYLGNIL QKRRKEVTFS VEQDFVVTHP
KPAPVQIYDY YETEEYAVAE YMSLCRGVVE EMG
