ID   OVOS_MOUSE              Reviewed;        1456 AA.
AC   Q3UU35; E9QMV5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Ovostatin homolog;
DE   Flags: Precursor;
GN   Name=Ovos;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
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; AK138836; BAE23794.1; -; mRNA.
DR   EMBL; AC123060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS39651.1; -.
DR   RefSeq; NP_001001179.2; NM_001001179.3.
DR   AlphaFoldDB; Q3UU35; -.
DR   SMR; Q3UU35; -.
DR   STRING; 10090.ENSMUSP00000059426; -.
DR   GlyGen; Q3UU35; 3 sites.
DR   iPTMnet; Q3UU35; -.
DR   PhosphoSitePlus; Q3UU35; -.
DR   EPD; Q3UU35; -.
DR   MaxQB; Q3UU35; -.
DR   PaxDb; Q3UU35; -.
DR   PRIDE; Q3UU35; -.
DR   ProteomicsDB; 294413; -.
DR   DNASU; 232400; -.
DR   Ensembl; ENSMUST00000060574; ENSMUSP00000059426; ENSMUSG00000047228.
DR   GeneID; 232400; -.
DR   KEGG; mmu:232400; -.
DR   UCSC; uc009eeh.2; mouse.
DR   CTD; 144568; -.
DR   MGI; MGI:3039594; BC048546.
DR   VEuPathDB; HostDB:ENSMUSG00000047228; -.
DR   eggNOG; KOG1366; Eukaryota.
DR   GeneTree; ENSGT00940000158779; -.
DR   HOGENOM; CLU_001634_0_1_1; -.
DR   InParanoid; Q3UU35; -.
DR   OMA; EKKTYVW; -.
DR   OrthoDB; 354230at2759; -.
DR   PhylomeDB; Q3UU35; -.
DR   TreeFam; TF313285; -.
DR   BioGRID-ORCS; 232400; 0 hits in 71 CRISPR screens.
DR   PRO; PR:Q3UU35; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q3UU35; protein.
DR   Bgee; ENSMUSG00000047228; Expressed in submandibular gland and 72 other tissues.
DR   Genevisible; Q3UU35; MM.
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; IPR019742; MacrogloblnA2_CS.
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.
DR   PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
PE   2: Evidence at transcript level;
KW   Bait region; Glycoprotein; Protease inhibitor; Reference proteome;
KW   Secreted; Serine protease inhibitor; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..1456
FT                   /note="Ovostatin homolog"
FT                   /id="PRO_0000318967"
FT   CARBOHYD        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        172
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        868
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        1127
FT                   /note="E -> G (in Ref. 1; BAE23794)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1292
FT                   /note="S -> C (in Ref. 1; BAE23794)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1456 AA;  162340 MW;  3A0535BDBEA59979 CRC64;
     MVPTILLSAL LLHFTDVVAA EPRYILWVSS VVQRFSSEKA CLHLLNLNES VSLSVTLEYD
     GSSTTIFDQP VDEGNFYACA DFKVSQMSSE QLAFVALLVQ GNTLKISERR SVAIAAEENA
     TFVQTDTPVH KPGDTVHFRV VTLNIWLKPV DDLYPLITVQ DPQSNVIFQW INVTTFRNIT
     QLSFQLTPEP ILGDYTIVIK TQSGTTVMDH FTVNRDVLPK FEVELTAPET ITIADSQFQM
     VTCAKYTYGQ PVQGKAQIKV CRELFSPAHC ESNENEICEQ FTVQLKDGCA SHIINTKVFQ
     LDRSGLFMTL NVNEVVTESG TGVQMSKTHS VFITSVLGTV SFENMDPFYR RGITYFGTLK
     FSGPNNTPLV DKLLQLELDG KPVGNYTTDE NGEARFSINT SEIFGAQISL KAVYVRPRSC
     HRSSWLSPEY LDAYFSASRF YSQTSSFTKI ILEPKQLPCD QEKMFSVLYS LNPEAYKEAS
     DVTFFYLVMV RGGISRSGQK QVRVQAWNGN FSFPISINAD LAPSADLFVY TLHPSGEIVA
     DNVRLQIEKC FKNKVSINFS RDKDLPGSNT SVHLQAAPDS FCALRAVDKS ALLLNHGQEM
     TPESVYFTLP YIHQYGYFYN GLNLDDQQAE PCIPQKDLFY NGLYYTPTGN IWDGDLSNLL
     SNMGLKIFTN LHYRKPEVCS SQENQPLLRT FDHPNERIMM YGGGAPPSSA FHDSVDSISH
     AKVAIKETVR TNFPRTWIWN LVSVDSSGTA NVSFLVPDTI TQWEASAFCV NGNAGFGISP
     KVSLQISQPF FVEVTSPFSV VRSEQSDMVV TVFNYLTTCV EISVQLEASE NYEASINTQR
     NTDSEVLQAG EQKTYVWTII PKTLGKVNVT VVATSKQSRA CPNDASKEQD VHWKDTVVKT
     MLVEAEGIEK EATQSFLICP KGTKASKQTL LELPSNVVEG SVRSFVTIVG DILGVAMQNL
     ESLLQMPYGC GEQNIAQLAS DVYILDYLKA TDQLTEELKS KAQRLLSNGY QNHLSFKNYD
     GSYDVFCQSN QEGSTWLSAL SFKTVEKMKE YIFIEETVPK QTLIWLVKKQ KSNGCFRRDE
     KHVDTAQEGR EGDQEDIALT AYVVGVFLEV GLNASFPALR NGLYCLEEAF SNGVTNGYTQ
     AILAYVFALA GKEQQAKSLL SILDKSATKT NNMIYWERDE KPETDNSPSF IPSALSGETE
     KTCYVLLAVL SQDTQDLDYA SKIVQWLAQR MNSHGGFSAM QDTTVCLLAL TQYMKLTGSN
     PQNTITLSSE ESEEVFYVNR NKRLLVQHSK VSKGHQQYTV DVEGDGCSFI QATLRYNVPL
     PKEASGFSLS VKTGKSNSSD EFQTKFELTV TLTYTGARES SVTVLVDVKM LSGFTPVVSS
     TEELKFNSQV TKTDIKNGHV LFYLENVPKE ATSLTFSIEQ TNHVANIQPA PVTVYSYEKG
     EYAFDSYNIN SISDSQ