ID G3S939_GORGO Unreviewed; 342 AA.
AC G3S939;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000024604.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000024604.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000024604.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000024604.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; CABD030005278; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G3S939; -.
DR STRING; 9593.ENSGGOP00000024604; -.
DR MEROPS; A01.P02; -.
DR Ensembl; ENSGGOT00000030489.2; ENSGGOP00000024604.2; ENSGGOG00000021928.2.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000162710; -.
DR HOGENOM; CLU_013253_3_0_1; -.
DR InParanoid; G3S939; -.
DR OMA; QNHHRFN; -.
DR TreeFam; TF314990; -.
DR Proteomes; UP000001519; Chromosome 1.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR Gene3D; 2.60.40.1960; -; 1.
DR Gene3D; 6.10.140.60; -; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 3.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR012848; Aspartic_peptidase_N.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF13; CHYMOSIN; 1.
DR Pfam; PF07966; A1_Propeptide; 1.
DR Pfam; PF00026; Asp; 2.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..342
FT /note="Peptidase A1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014131375"
FT DOMAIN 74..339
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 92
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 235
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 105..110
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 226..230
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 269..302
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 342 AA; 37595 MW; F8D37AFD3EB5D451 CRC64;
MRGLVVFLAV FALSEVNAIT RVPLHKGKSL RRALKERRLL EDFLRNHHYA VSRKHSSSGV
VASESLTNYL DCQYFGKIYI GSPPQKFTLV FDTGSLDLWV PSVYCNSDAC LLHPQNMGKS
LSIQYGTGSM RGLLGYDTVT VSNIVDPHQT VGLSTEEPGD IFTYSEFDGI LGLAYPSLAS
EYTLRLGFRN DQGSMLTLRA IDLSYYTEYW QFTVDSVIID GMVVVCDGGC QAILDTGTSL
LVGPGSNILN IQQAIGATAG QYNEFDIDCG RLSSMPTVVF EIHGKKYPLP PSAYTSQDQG
FCTSGFQGDY SSQQWILGGV FTREYYSVFD RANNCVGLAK AV
//
