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 03-AUG-2022, entry version 132.
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; 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=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. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; AC012151; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BN000128; CAD67579.1; -; mRNA.
DR AlphaFoldDB; Q7RTY7; -.
DR SMR; Q7RTY7; -.
DR BioGRID; 131129; 3.
DR IntAct; Q7RTY7; 3.
DR STRING; 9606.ENSP00000326708; -.
DR MEROPS; S01.078; -.
DR MEROPS; S01.322; -.
DR GlyConnect; 2011; 1 O-Linked glycan (1 site).
DR GlyGen; Q7RTY7; 7 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q7RTY7; -.
DR PhosphoSitePlus; Q7RTY7; -.
DR BioMuta; OVCH1; -.
DR DMDM; 118573093; -.
DR MassIVE; Q7RTY7; -.
DR PaxDb; Q7RTY7; -.
DR PeptideAtlas; Q7RTY7; -.
DR PRIDE; Q7RTY7; -.
DR Antibodypedia; 48487; 60 antibodies from 12 providers.
DR DNASU; 341350; -.
DR Ensembl; ENST00000318184.9; ENSP00000326708.5; ENSG00000187950.8.
DR UCSC; uc001rix.2; human.
DR GeneCards; OVCH1; -.
DR HGNC; HGNC:23080; OVCH1.
DR HPA; ENSG00000187950; Tissue enhanced (lung, testis).
DR neXtProt; NX_Q7RTY7; -.
DR PharmGKB; PA134910581; -.
DR VEuPathDB; HostDB:ENSG00000187950; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_004497_0_0_1; -.
DR InParanoid; Q7RTY7; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q7RTY7; -.
DR TreeFam; TF318987; -.
DR PathwayCommons; Q7RTY7; -.
DR SignaLink; Q7RTY7; -.
DR BioGRID-ORCS; 341350; 5 hits in 311 CRISPR screens.
DR GenomeRNAi; 341350; -.
DR Pharos; Q7RTY7; Tdark.
DR PRO; PR:Q7RTY7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q7RTY7; protein.
DR Bgee; ENSG00000187950; Expressed in right lung and 89 other tissues.
DR ExpressionAtlas; Q7RTY7; baseline and differential.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 3.
DR CDD; cd00190; Tryp_SPc; 2.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.60.120.290; -; 3.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
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; Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Repeat; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..46
FT /note="Activation peptide"
FT /evidence="ECO:0000250"
FT /id="PRO_0000261179"
FT CHAIN 47..1134
FT /note="Ovochymase-1"
FT /id="PRO_0000261180"
FT DOMAIN 38..296
FT /note="Peptidase S1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DOMAIN 284..410
FT /note="CUB 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 419..531
FT /note="CUB 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 575..812
FT /note="Peptidase S1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT DOMAIN 846..957
FT /note="CUB 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT ACT_SITE 87
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 139
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 237
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 615
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 664
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 763
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 507
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 72..88
FT /evidence="ECO:0000250"
FT DISULFID 173..243
FT /evidence="ECO:0000250"
FT DISULFID 204..222
FT /evidence="ECO:0000250"
FT DISULFID 233..262
FT /evidence="ECO:0000250"
FT DISULFID 341..373
FT /evidence="ECO:0000250"
FT DISULFID 419..446
FT /evidence="ECO:0000250"
FT DISULFID 473..494
FT /evidence="ECO:0000250"
FT DISULFID 600..616
FT /evidence="ECO:0000250"
FT DISULFID 698..769
FT /evidence="ECO:0000250"
FT DISULFID 729..747
FT /evidence="ECO:0000250"
FT DISULFID 759..788
FT /evidence="ECO:0000250"
FT DISULFID 846..873
FT /evidence="ECO:0000250"
FT VARIANT 133
FT /note="R -> C (in dbSNP:rs10843438)"
FT /id="VAR_029089"
FT VARIANT 228
FT /note="W -> G (in dbSNP:rs967181)"
FT /id="VAR_029090"
FT VARIANT 330
FT /note="K -> E (in dbSNP:rs3847680)"
FT /id="VAR_029091"
FT VARIANT 444
FT /note="I -> T (in dbSNP:rs7975356)"
FT /id="VAR_029092"
FT VARIANT 557
FT /note="L -> V (in dbSNP:rs35183403)"
FT /id="VAR_057159"
FT VARIANT 672
FT /note="S -> F (in dbSNP:rs11050243)"
FT /id="VAR_029093"
FT VARIANT 754
FT /note="G -> R (in dbSNP:rs12305672)"
FT /id="VAR_029094"
FT VARIANT 881
FT /note="P -> A (in dbSNP:rs1347570)"
FT /id="VAR_029095"
FT VARIANT 934
FT /note="P -> S (in dbSNP:rs7967676)"
FT /id="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
