GenomeNet

Database: UniProt
Entry: OVCH1_HUMAN
LinkDB: OVCH1_HUMAN
Original site: OVCH1_HUMAN 
ID   OVCH1_HUMAN             Reviewed;        1134 AA.
AC   Q7RTY7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 2.
DT   08-MAY-2019, entry version 118.
DE   RecName: Full=Ovochymase-1;
DE            EC=3.4.21.-;
DE   Flags: Precursor;
GN   Name=OVCH1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   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.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   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.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=12838346; DOI=10.1038/nrg1111;
RA   Puente X.S., Sanchez L.M., Overall C.M., Lopez-Otin C.;
RT   "Human and mouse proteases: a comparative genomic approach.";
RL   Nat. Rev. Genet. 4:544-558(2003).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; AC012151; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BN000128; CAD67579.1; -; mRNA.
DR   SMR; Q7RTY7; -.
DR   IntAct; Q7RTY7; 3.
DR   STRING; 9606.ENSP00000326708; -.
DR   MEROPS; S01.322; -.
DR   GlyConnect; 2011; -.
DR   iPTMnet; Q7RTY7; -.
DR   PhosphoSitePlus; Q7RTY7; -.
DR   BioMuta; OVCH1; -.
DR   DMDM; 118573093; -.
DR   PaxDb; Q7RTY7; -.
DR   PeptideAtlas; Q7RTY7; -.
DR   PRIDE; Q7RTY7; -.
DR   ProteomicsDB; 68936; -.
DR   DNASU; 341350; -.
DR   Ensembl; ENST00000318184; ENSP00000326708; ENSG00000187950.
DR   UCSC; uc001rix.2; human.
DR   GeneCards; OVCH1; -.
DR   HGNC; HGNC:23080; OVCH1.
DR   HPA; HPA040253; -.
DR   neXtProt; NX_Q7RTY7; -.
DR   PharmGKB; PA134910581; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   HOGENOM; HOG000172098; -.
DR   InParanoid; Q7RTY7; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; Q7RTY7; -.
DR   TreeFam; TF318987; -.
DR   GenomeRNAi; 341350; -.
DR   PRO; PR:Q7RTY7; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000187950; Expressed in 77 organ(s), highest expression level in right lung.
DR   ExpressionAtlas; Q7RTY7; baseline and differential.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd00041; CUB; 3.
DR   CDD; cd00190; Tryp_SPc; 2.
DR   Gene3D; 2.60.120.290; -; 3.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF00089; Trypsin; 2.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00020; Tryp_SPc; 2.
DR   SUPFAM; SSF49854; SSF49854; 4.
DR   SUPFAM; SSF50494; SSF50494; 2.
DR   PROSITE; PS01180; CUB; 3.
DR   PROSITE; PS50240; TRYPSIN_DOM; 2.
DR   PROSITE; PS00134; TRYPSIN_HIS; 2.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Complete proteome; Disulfide bond; Glycoprotein; Hydrolase;
KW   Metal-binding; Polymorphism; Protease; Reference proteome; Repeat;
KW   Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL        1     22       {ECO:0000255}.
FT   PROPEP       23     46       Activation peptide. {ECO:0000250}.
FT                                /FTId=PRO_0000261179.
FT   CHAIN        47   1134       Ovochymase-1.
FT                                /FTId=PRO_0000261180.
FT   DOMAIN       38    296       Peptidase S1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   DOMAIN      284    410       CUB 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      419    531       CUB 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   DOMAIN      575    812       Peptidase S1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   DOMAIN      846    957       CUB 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00059}.
FT   ACT_SITE     87     87       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    139    139       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    237    237       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    615    615       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    664    664       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    763    763       Charge relay system. {ECO:0000250}.
FT   METAL       116    116       Calcium. {ECO:0000250}.
FT   CARBOHYD     52     52       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     99     99       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    324    324       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    431    431       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    507    507       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1106   1106       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     72     88       {ECO:0000250}.
FT   DISULFID    173    243       {ECO:0000250}.
FT   DISULFID    204    222       {ECO:0000250}.
FT   DISULFID    233    262       {ECO:0000250}.
FT   DISULFID    341    373       {ECO:0000250}.
FT   DISULFID    419    446       {ECO:0000250}.
FT   DISULFID    473    494       {ECO:0000250}.
FT   DISULFID    600    616       {ECO:0000250}.
FT   DISULFID    698    769       {ECO:0000250}.
FT   DISULFID    729    747       {ECO:0000250}.
FT   DISULFID    759    788       {ECO:0000250}.
FT   DISULFID    846    873       {ECO:0000250}.
FT   VARIANT     133    133       R -> C (in dbSNP:rs10843438).
FT                                /FTId=VAR_029089.
FT   VARIANT     228    228       W -> G (in dbSNP:rs967181).
FT                                /FTId=VAR_029090.
FT   VARIANT     330    330       K -> E (in dbSNP:rs3847680).
FT                                /FTId=VAR_029091.
FT   VARIANT     444    444       I -> T (in dbSNP:rs7975356).
FT                                /FTId=VAR_029092.
FT   VARIANT     557    557       L -> V (in dbSNP:rs35183403).
FT                                /FTId=VAR_057159.
FT   VARIANT     672    672       S -> F (in dbSNP:rs11050243).
FT                                /FTId=VAR_029093.
FT   VARIANT     754    754       G -> R (in dbSNP:rs12305672).
FT                                /FTId=VAR_029094.
FT   VARIANT     881    881       P -> A (in dbSNP:rs1347570).
FT                                /FTId=VAR_029095.
FT   VARIANT     934    934       P -> S (in dbSNP:rs7967676).
FT                                /FTId=VAR_029096.
SQ   SEQUENCE   1134 AA;  125066 MW;  87F935BCCB773B16 CRC64;
     MGLLASAGLL LLLVIGHPRS LGLKCGIRMV NMKSKEPAVG SRFFSRISSW RNSTVTGHPW
     QVSLKSDEHH FCGGSLIQED RVVTAAHCLD SLSEKQLKNI TVTSGEYSLF QKDKQEQNIP
     VSKIITHPEY NSREYMSPDI ALLYLKHKVK FGNAVQPICL PDSDDKVEPG ILCLSSGWGK
     ISKTSEYSNV LQEMELPIMD DRACNTVLKS MNLPPLGRTM LCAGFPDWGM DACQGDSGGP
     LVCRRGGGIW ILAGITSWVA GCAGGSVPVR NNHVKASLGI FSKVSELMDF ITQNLFTGLD
     RGQPLSKVGS RYITKALSSV QEVNGSQRGK GILDMEKQVG CDHDYVSLRS SSGVLFNQRS
     LMEDDGKQNK RVCGKILPSP LLAETSEAMV PFVSDTEDSG SGFELTVTAV QKSEAGSGCG
     SLAILVEEGT NHSAKYPDLY PSNIRCHWFI CAPEKHIIKL TFEDFAVKFS PNCIYDAVVI
     YGDSEEKHKL AKLCGMLTIT SIFSSSNMTV IYFKSDGKNR LQGFKARFTI LPSESLNKFE
     PKLPPQNNPV STVKAILHDV CGIPPFSPQW LSRRIAGGEE ACPHCWPWQV GLRFLGDYQC
     GGAIINPVWI LTAAHCVQLK NNPLSWTIIA GDHDRNLKES TEQVRRAKHI IVHEDFNTLS
     YDSDIALIQL SSPLEYNSVV RPVCLPHSAE PLFSSEICAV TGWGSISADG GLASRLQQIQ
     VHVLEREVCE HTYYSAHPGG ITEKMICAGF AASGEKDFCQ GDSGGPLVCR HENGPFVLYG
     IVSWGAGCVQ PWKPGVFARV MIFLDWIQSK INGPASLQTN NKCKTLKQQL PPPTPSPDSA
     SWPGCCSEAE LEKPRGFFPT PRYLLDYRGR LECSWVLRVS PSSMAKFTIE YLSLLGSPVC
     QDSVLIIYEE RHSKRKTAGG LHGRRLYSMT FMSPGPLVRV TFHALVRGAF GISYIDLKVL
     GPKDSKITRL SQSSNREHLV PCEDVLLTKP EGIMQIPRNS HRTTMGCQWR LVAPLNHIIQ
     LNIINFPMKP TTFVCHGHLR VYEGFGPGKK LIASFAGTLA MILTKDILKR EKLNFINTYI
     MHIWENSVYD NVRSVGKRKQ KKFASNLSYS MEAEKSRIQV PADLVPAKGS LSGS
//
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