ID A0A151NXS3_ALLMI Unreviewed; 382 AA.
AC A0A151NXS3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=pepsin A {ECO:0000256|ARBA:ARBA00011924};
DE EC=3.4.23.1 {ECO:0000256|ARBA:ARBA00011924};
GN ORFNames=Y1Q_0006412 {ECO:0000313|EMBL:KYO41667.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO41667.1};
RN [1] {ECO:0000313|EMBL:KYO41667.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO41667.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO41667.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKHW03001628; KYO41667.1; -; Genomic_DNA.
DR RefSeq; XP_019340824.1; XM_019485279.1.
DR AlphaFoldDB; A0A151NXS3; -.
DR STRING; 8496.A0A151NXS3; -.
DR GeneID; 102562633; -.
DR KEGG; amj:102562633; -.
DR eggNOG; KOG1339; Eukaryota.
DR OrthoDB; 1120702at2759; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 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 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:UP000050525};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..382
FT /note="pepsin A"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007586476"
FT DOMAIN 71..379
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 89
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 271
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 102..107
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 262..266
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 382 AA; 42273 MW; 3E3F9914793CDC3D CRC64;
MKWLLLLLSL VGLAHCLVTK VPLKKRKSMR QNLKEQGLLE DFLKKHPRNL ASKYFPKFGT
EPITNHMDLQ YMGTISIGTP PQEFTVLFDT GSSNLWVPSV HCSSLACTHH NRFSPQDSST
YQTTHQSIAI QYGIGLMTGF LAYDTVEVGD IQITHQIFGL STNESFFTLY FLSFDGILGL
AFPSISLAGA TPVFDNMMNK HLVSQDLFSV YLTSKESGSF VMFGGIDSSC YSGSLKWIPL
SAETYWQITM DRIMINGEAV ACTTGCQAII DTGTSLLTGP PNDVFLILKH IGISQNSYGE
YTVNCHDINN LPDVVFIIHG IEFPLPASAY ISQSTGYCTC NFEGISVPTD SGQLWILGDV
FLRHYYTVFD RANCQVGLAP VV
//