ID   OVOS1_HUMAN             Reviewed;        1185 AA.
AC   Q6IE37;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   08-NOV-2023, entry version 101.
DE   RecName: Full=Ovostatin homolog 1;
DE   Flags: Precursor;
GN   Name=OVOS1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=15060002; DOI=10.1101/gr.1946304;
RA   Puente X.S., Lopez-Otin C.;
RT   "A genomic analysis of rat proteases and protease inhibitors.";
RL   Genome Res. 14:609-622(2004).
CC   -!- FUNCTION: Is able to inhibit all four classes of proteinases by a
CC       unique 'trapping' mechanism. {ECO:0000250}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I39 (alpha-2-
CC       macroglobulin) family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AC006432; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC092821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BN000356; CAE51408.1; -; mRNA.
DR   AlphaFoldDB; Q6IE37; -.
DR   SMR; Q6IE37; -.
DR   GlyCosmos; Q6IE37; 5 sites, No reported glycans.
DR   GlyGen; Q6IE37; 5 sites.
DR   iPTMnet; Q6IE37; -.
DR   PhosphoSitePlus; Q6IE37; -.
DR   SwissPalm; Q6IE37; -.
DR   BioMuta; OVOS1; -.
DR   DMDM; 182637456; -.
DR   MassIVE; Q6IE37; -.
DR   PeptideAtlas; Q6IE37; -.
DR   ProteomicsDB; 66403; -.
DR   neXtProt; NX_Q6IE37; -.
DR   InParanoid; Q6IE37; -.
DR   PhylomeDB; Q6IE37; -.
DR   Pharos; Q6IE37; Tdark.
DR   PRO; PR:Q6IE37; -.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; Q6IE37; Protein.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.50.10.20; -; 2.
DR   Gene3D; 2.20.130.20; -; 1.
DR   Gene3D; 2.60.120.1540; -; 2.
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; 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; IPR041555; MG3.
DR   InterPro; IPR040839; MG4.
DR   InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR   PANTHER; PTHR11412; MACROGLOBULIN / COMPLEMENT; 1.
DR   PANTHER; PTHR11412:SF174; OVOSTATIN HOMOLOG 1-RELATED; 1.
DR   Pfam; PF00207; A2M; 1.
DR   Pfam; PF07703; A2M_BRD; 1.
DR   Pfam; PF07677; A2M_recep; 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.
PE   2: Evidence at transcript level;
KW   Bait region; Glycoprotein; Protease inhibitor; Reference proteome;
KW   Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..1185
FT                   /note="Ovostatin homolog 1"
FT                   /id="PRO_0000318965"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        155
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        347
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        452
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        725
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1185 AA;  134499 MW;  569DE9EA344240FD CRC64;
     MHVHVCVCLC VCIYTSSCVC ACVHMCMRDA LLAEGRGGGL AAADDFLYLE CCKCFSQESQ
     IAMVCQERSQ NETYEVKMNN DTEACRATLN LEERRSVAIR SRENVVFVQT DKPTYKPGQK
     DVNGIAQFFL DTYTFTYPNI TLKDPQNNRI FQRQNVTSFR NITQLSFQLI SEPMFGDYWI
     VVKRNSRETV THQFAVKRYV LPKFEVTVNA PQTVTISDDE FQVDVCAYNF GQPVQGETQI
     RVCREYFSSS NCEKNENEIC EQFIAQVQTN LDIFTLLCSS FLTVMQISEK TSVFITQLLG
     TVNFENMDTF YRRGISYFGQ LKFSDPNNVP MVNKLLQLEL NDEFIGNYTT DENGEAQFSI
     DTSDIFDPEF NLKVRHQRTE ECYLPSWLTP QYLDAHFLVS RFYSRTNSFL KIVPEPKQLE
     CNQQKVVTVH YSLNSEAYED DSNVKFFYLN GNFSFPISIS ADLAPAAVLF VYTLHPSGEI
     VADSVRFQVD KCFKHKVNIK FSNEQGLPGS NASLCLQAAP VLFCALRAVD RNVLLLKSEQ
     QLSAESVSSL YNMVPSIEPY GYFYHGLNLD DGKEDPCIPQ RDMFYNGLYY TPVSNYGDGD
     IYNIVRVRSL RILENIIQTV RTNFPETWMW DLVSVSSSGS ANLSFLIPDT ITQWEASGFC
     VNGDVGFGIS STTTLEVSQP FFIEIASPFS VVQNEQFDLI VNVFSYRNTC VEVSYIWECL
     PGKVNITVVA ESKQSSACPN EGMEQQKLNW KDTVVQSFLV EFLFLGDILG LALQNLVVLQ
     MPYGSGEQNA ALLASDTYVL DYLKSTEQLT EEVQSKAFFL SILGYQRQLS FKNSDGSYSV
     FWQQSQKGSI WLSALTFKTL ERMKKYVFID ENVQKQTLIW LSSQQKTSGC FKNDGQLFNH
     ALRNALFCLE AALDSGVTNG YNHAILAYAF ALAGKEKQVE SLLQTLDQSA PKLSKRYYWE
     RERKPKTEEF PSFIPWAPSA QTEKSCYVLL AVISRKIPDL TYASKIVQWL AQRMNSHGGF
     SSNQVINVGL ILIAARGEEG LFSKDQNTVT FSSEGSSEIF QVNGHNRLLV QRSEVTQAPG
     EYTVDVEGHG CTFIQIFRYT GIRNKSSMVV IDVKMLSGFT PTMSSIEEVN NRSLIFQHKD
     SYIEYKRADS FPFSVEQSNL VFNIQPAPAM VYDYYEKGRQ ATAMP
//