ID G1SHB1_RABIT Unreviewed; 387 AA.
AC G1SHB1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE RecName: Full=pepsin A {ECO:0000256|ARBA:ARBA00011924};
DE EC=3.4.23.1 {ECO:0000256|ARBA:ARBA00011924};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000002008.2, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000002008.2, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke {ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000002008.2}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000002008.2};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- FUNCTION: Shows particularly broad specificity; although bonds
CC involving phenylalanine and leucine are preferred, many others are also
CC cleaved to some extent. {ECO:0000256|ARBA:ARBA00002318}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR AlphaFoldDB; G1SHB1; -.
DR SMR; G1SHB1; -.
DR MEROPS; A01.001; -.
DR PaxDb; 9986-ENSOCUP00000002008; -.
DR Ensembl; ENSOCUT00000002329.2; ENSOCUP00000002008.2; ENSOCUG00000031644.1.
DR eggNOG; KOG1339; Eukaryota.
DR GeneTree; ENSGT00940000155036; -.
DR HOGENOM; CLU_013253_3_0_1; -.
DR InParanoid; G1SHB1; -.
DR OMA; SEICFGC; -.
DR TreeFam; TF314990; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000031644; Expressed in testis.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0007586; P:digestion; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05478; pepsin_A; 1.
DR Gene3D; 6.10.140.60; -; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR012848; Aspartic_peptidase_N.
DR InterPro; IPR034162; Pepsin_A.
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:SF22; PEPSIN A-3-RELATED; 1.
DR Pfam; PF07966; A1_Propeptide; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Digestion {ECO:0000256|ARBA:ARBA00022757};
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:UP000001811};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..387
FT /note="pepsin A"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012406917"
FT DOMAIN 75..384
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 93
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 276
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 106..111
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 267..271
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 310..343
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 387 AA; 42026 MW; 6BE8D07F99B52153 CRC64;
MKWLLLLSLL ALSECIIHKV PLVRKKSLRK NLIEKGLLKD YLKTHTPNLA TKYLPKAAFD
SVPTETLENY LDTEYFGTIG IGTPAQDFTV IFDTGSSNLW VPSVYCSSAA CSVHNQFNPE
DSSTFQATSE SLSITYGTGS MTGFLGYDTV KVGNIEDTNQ IFGLSESEPG SFLYYAPFDG
ILGLAYPSIS SSDATPVFDN MWNEGLVSED LFSVYLNSDD ESGSVVMFGG IDSSYYTGSL
NWVPVSYEGY WQITLDSITM DGETIACADS CQAIVDTGTS LLAGPTSAIS NIQSYIGASE
NSDGEMIVSC SSMYSLPNIV FTINGVQYPV PASAYILEED DACISGFEGM NLDTYTGELW
ILGDVFIRQY FTVFDRANNQ LGLAAAA
//