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OVOS2_HUMAN
ID   OVOS2_HUMAN             Reviewed;        1432 AA.
AC   Q6IE36;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Ovostatin homolog 2;
DE   Flags: Precursor;
GN   Name=OVOS2;
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   -!- SEQUENCE CAUTION:
CC       Sequence=CAE51409.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC008010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC008013; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC024940; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BN000357; CAE51409.1; ALT_SEQ; mRNA.
DR   AlphaFoldDB; Q6IE36; -.
DR   SMR; Q6IE36; -.
DR   GlyGen; Q6IE36; 5 sites.
DR   iPTMnet; Q6IE36; -.
DR   PhosphoSitePlus; Q6IE36; -.
DR   BioMuta; OVOS2; -.
DR   DMDM; 182637457; -.
DR   MassIVE; Q6IE36; -.
DR   PeptideAtlas; Q6IE36; -.
DR   PRIDE; Q6IE36; -.
DR   ProteomicsDB; 66402; -.
DR   GeneCards; OVOS2; -.
DR   neXtProt; NX_Q6IE36; -.
DR   InParanoid; Q6IE36; -.
DR   PhylomeDB; Q6IE36; -.
DR   ChiTaRS; OVOS2; human.
DR   Pharos; Q6IE36; Tdark.
DR   PRO; PR:Q6IE36; -.
DR   Proteomes; UP000005640; Unplaced.
DR   RNAct; Q6IE36; protein.
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; 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..?
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..1432
FT                   /note="Ovostatin homolog 2"
FT                   /id="PRO_0000318966"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        858
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         211
FT                   /note="T -> M (in dbSNP:rs7971718)"
FT                   /id="VAR_055459"
FT   VARIANT         587
FT                   /note="L -> V (in dbSNP:rs12309295)"
FT                   /id="VAR_055460"
FT   VARIANT         789
FT                   /note="S -> L (in dbSNP:rs11051266)"
FT                   /id="VAR_055461"
FT   VARIANT         1328
FT                   /note="V -> A (in dbSNP:rs17418189)"
FT                   /id="VAR_055462"
SQ   SEQUENCE   1432 AA;  161251 MW;  8A32EC146C3EFB80 CRC64;
     MTGSHLSHDS WQYVLLIPSV LQEGSLDKAC AQLFNLTESV VLTVSLNYGE VQTKIFEENV
     TGENFFKCIS FEVPQARSDP LAFITFSAKG ATLNLEERRS VAIRSRENVV FVQTDKPTYK
     PGQKDVNGIA QFFLDTYTFT YPNITLKDPQ NNRIFQWQNV TSFRNITQLS FQLISEPMFG
     DYWIVVKRNS RKTVTHQFAV KRYVLPKFEV TVNAPQTVTI SDDEFQVDVC AKYTFGQPVQ
     GKTQIRVCRE YFSSSNCEKN DNEICEQFIA QLENGCVSQI VNTKVFQLYR SGLFMTFHVA
     VIVTEFGTGN YCMQISEKTS VFITQLLGTV NFENMDTFYR RGISYFGTLK FSDPNNVPMV
     NKLLQLELND EFIGNYTTDE NGEAQFSIDT SDIFDPEFNL KATYVRPKSC YLPSWLTPQY
     LDAHFLVSRF YSRTNSFLKI VPEPKQLECN HQKVVTVHYS LNSEAYEDDS NVKFFYLVSL
     SHDSGNFQHR ISSSPIYTAW NGNFSFPLSI SADLAPAAVL FVYTLHPSGE IVADSVRFQV
     DKCFKHKVNI KFSNEQGLPG SNASLYLQAA PVLFCALGAV DGNVLLLKSE QQLSAESVYN
     MVPSIEPYGY FYHGLNLDDG KEDPCIPQRD MFYNGLYYTP VSNYGDGDIY NIVRNMGLKV
     FTNLHYRKPE VCVMERRLPL PKPLYLETEN YGPMHSVPSR IACRGENADY VEQAIIQTVR
     TNFPETWMWD LVSVDSSGSA NLSFLIPDTI TQWEASGFCV NGDVGFGISS TTTLEVSQPF
     FIEIASPFSV VQNEQFDLIV NAFSYLNTCV EISVQVEESQ NYEANINTWK INGSEVIQAG
     GRKTNIWTII PKKLGKVNIT VVAESKQSSA CPNEGMEQQK LNWKDTVVKS FLVEPEGIEK
     ERTQSFLICT EGAKASKQGV LDLPNDVVEG SARGFFTVVG DILGLAMQNL VVLQMPYGGG
     EQNAALLASD TYVLDYLKST EQLTEEVQSK AFFLLSNGYQ RQLSFKNSDG SYSVFWQQNQ
     KGSIWLSALT FKTLERMKKF VFIDENVQKQ TLIWLSSQQK TSGCFKNDGQ LFNHAWEGGD
     EEDISLTAYV VGMFFEAGLN STFPALRNAL FCLEAALDSG VTNGYNHAIL AYAFALAGKE
     KQVESLLQTL DQSATKLNNV IYWERERKPK TEEFPSFIPW APSAQTEKSC YVLLAVISRK
     IPDLTYASKI VQWLAQQMNS HGGFSSNQVI NVGLILIAIC GEEGLFSKNQ NTVTFSSEGS
     SEIQFNGHNR LLVQRSEVTQ APGQYTVDVE GRGCTFIQAT LKYNVLLPKK ASGFSLSLEI
     VKNYSLTVFD LTVNLKYTGI RNKSSMVVID VKMLSGFTPT MSSIEELENK GQVMKTEVKN
     DHVLFYLENV FGRADSFTFS VEQSNLVFNI QPAPGMVYDY YEKDGEAFLL TN
 
 
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