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Database: UniProt
Entry: A0A151NXS3_ALLMI
LinkDB: A0A151NXS3_ALLMI
Original site: A0A151NXS3_ALLMI 
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}.
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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
//
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