OVOS1_HUMAN
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 25-MAY-2022, entry version 96.
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}.
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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 GlyGen; Q6IE37; 5 sites.
DR iPTMnet; Q6IE37; -.
DR PhosphoSitePlus; Q6IE37; -.
DR BioMuta; OVOS1; -.
DR DMDM; 182637456; -.
DR MassIVE; Q6IE37; -.
DR PeptideAtlas; Q6IE37; -.
DR PRIDE; 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; 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; 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 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 SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF49410; SSF49410; 1.
DR SUPFAM; SSF81296; SSF81296; 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
