ID H2NGW6_PONAB Unreviewed; 1071 AA.
AC H2NGW6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Ovochymase 1 {ECO:0000313|Ensembl:ENSPPYP00000005012.2};
GN Name=OVCH1 {ECO:0000313|Ensembl:ENSPPYP00000005012.2};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000005012.2, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000005012.2, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPPYP00000005012.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00059}.
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DR AlphaFoldDB; H2NGW6; -.
DR Ensembl; ENSPPYT00000005210.2; ENSPPYP00000005012.2; ENSPPYG00000004391.2.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000163017; -.
DR HOGENOM; CLU_004497_0_0_1; -.
DR InParanoid; H2NGW6; -.
DR OMA; EHTYYSA; -.
DR TreeFam; TF318987; -.
DR Proteomes; UP000001595; Chromosome 12.
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; 2.60.120.290; Spermadhesin, CUB domain; 3.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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 PANTHER; PTHR24252:SF8; ACROSIN; 1.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
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; Spermadhesin, CUB domain; 3.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 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 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00059}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1071
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5035172241"
FT DOMAIN 38..296
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 333..410
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 419..531
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 575..812
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 846..957
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DISULFID 419..446
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 846..873
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
SQ SEQUENCE 1071 AA; 117927 MW; 671BA55029A818D0 CRC64;
MGVLASAGLL LLLVIGHPRS LGLKCGIRMV NTKNKEPAVG SRFFSRISSW RNSTVTGHPW
QVSLKSEEHH FCGGSLIQED RVVTAAHCLD NLSEKQLKNI TVTSGKYSFF QKDKQEQNIP
VSKIITHPEY NSREYMSPDI ALLYLKHKVK FGNAVQPICL PDSDDKVEPG ILCLSSGWGK
ISKTSEYSNV LQEIELPIMD DRACNTVLKS MNLPPLGRTM LCAGFPDEGM DACQGDSGGP
LVCRRGGGIW ILAGITSWVA GCAGGSAPVR NNHMKASLGI FSKVSELMDF ITQNLFTGLD
RGQPLSKVGP SCITKALSSV QEVNGSQRGE GTLDMEKQVG CDHDYVSLPS SSGVLINQRS
LMEDDGKQNK RVCEKILPSP LLAETSEAMV PFVSDTEDSG SGFELTFTAV QNSEAGSGCG
SLAILVEEGT NHSAKYPDLH PSNVKCHWFI CAPEKHIIKL SFEDFAVKFS PNCIYDAVVI
YGDSEEEHKL AKLCGMLTIT SIFSSSNMMV IHFKSDGKNR LQGFKARFTI LPSESLNKFE
PKLPPQNNPV STVKAILHDV CGIPPFSPQW LSRRIAGGEE ACPHCWPWQV GLRFLGDYQC
GGAIINPVWI LTAAHCVQSK NNPLSWTIIA GDHDRNLKES TEQVRRAKHI IVHEDFNTLS
YDSDIALIQL SSPLEYNSVV RPVCLPHSTE PLFSSEICAV TGWGSISADG GLASRLQQIQ
VHVLEREVCE HTYYSAHPGG ITEKMICAGF AASGERDFCQ GDSGGPLVCR HENGPFVLYG
IVSWGAGCVQ PWKPGVFARV MIFLDWIQSK INGPASLQTN NKCKTLKQQL PPPTPSPDSA
SWPGCCSEAE LEKPRGFFPT SRYLLDYRGR LECSWVLRVS PSSMAKFTIE YLSLLGSPVC
QDSVLIIYEE RHSKRKMAGG LHGRRLYSMT FMSPGPLVRV TFHALVQGAF GISYIVLKVL
GPKDSKITRL SQSSNREHLV PCEDVLLTKP EGIMQIPRNS HRTTMGCQWR LVALLNHVIQ
LNIINFPMKP TTLVCHGHLD REDYPYQESK HVSKNPVADL NLWPELSHGH A
//
