ID A0A151P9U3_ALLMI Unreviewed; 522 AA.
AC A0A151P9U3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Cytosol aminopeptidase {ECO:0000256|ARBA:ARBA00014190};
DE EC=3.4.11.1 {ECO:0000256|ARBA:ARBA00012565};
DE EC=3.4.11.5 {ECO:0000256|ARBA:ARBA00012568};
DE EC=3.4.13.23 {ECO:0000256|ARBA:ARBA00023625};
DE AltName: Full=Cysteinylglycine-S-conjugate dipeptidase {ECO:0000256|ARBA:ARBA00030997};
DE AltName: Full=Leucine aminopeptidase 3 {ECO:0000256|ARBA:ARBA00031564};
DE AltName: Full=Leucyl aminopeptidase {ECO:0000256|ARBA:ARBA00033172};
DE AltName: Full=Proline aminopeptidase {ECO:0000256|ARBA:ARBA00030930};
DE AltName: Full=Prolyl aminopeptidase {ECO:0000256|ARBA:ARBA00029605};
GN Name=LAP3 {ECO:0000313|EMBL:KYO45802.1};
GN ORFNames=Y1Q_0021446 {ECO:0000313|EMBL:KYO45802.1};
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:KYO45802.1};
RN [1] {ECO:0000313|EMBL:KYO45802.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO45802.1};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-cysteinylglycine = glycine + L-cysteine;
CC Xref=Rhea:RHEA:28783, ChEBI:CHEBI:15377, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:61694;
CC Evidence={ECO:0000256|ARBA:ARBA00023673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28784;
CC Evidence={ECO:0000256|ARBA:ARBA00023673};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-benzyl-L-cysteinylglycine = glycine + S-benzyl-L-
CC cysteine; Xref=Rhea:RHEA:62568, ChEBI:CHEBI:15377, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:145802, ChEBI:CHEBI:145803;
CC Evidence={ECO:0000256|ARBA:ARBA00023527};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62569;
CC Evidence={ECO:0000256|ARBA:ARBA00023527};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001585};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa
CC is preferably Leu, but may be other amino acids including Pro
CC although not Arg or Lys, and Yaa may be Pro. Amino acid amides and
CC methyl esters are also readily hydrolyzed, but rates on arylamides
CC are exceedingly low.; EC=3.4.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000135};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted L-cysteinylglycine + H2O = an S-substituted
CC L-cysteine + glycine; Xref=Rhea:RHEA:60444, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:58717, ChEBI:CHEBI:143103;
CC EC=3.4.13.23; Evidence={ECO:0000256|ARBA:ARBA00023511};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60445;
CC Evidence={ECO:0000256|ARBA:ARBA00023511};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|ARBA:ARBA00011643}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase M17 family.
CC {ECO:0000256|ARBA:ARBA00009528}.
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:KYO45802.1}.
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DR EMBL; AKHW03000533; KYO45802.1; -; Genomic_DNA.
DR RefSeq; XP_019335564.1; XM_019480019.1.
DR AlphaFoldDB; A0A151P9U3; -.
DR STRING; 8496.A0A151P9U3; -.
DR GeneID; 102561016; -.
DR CTD; 51056; -.
DR eggNOG; KOG2597; Eukaryota.
DR OrthoDB; 2899215at2759; -.
DR PhylomeDB; A0A151P9U3; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00433; Peptidase_M17; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR HAMAP; MF_00181; Cytosol_peptidase_M17; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR000819; Peptidase_M17_C.
DR InterPro; IPR023042; Peptidase_M17_leu_NH2_pept.
DR InterPro; IPR008283; Peptidase_M17_N.
DR PANTHER; PTHR11963:SF52; CYTOSOL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR Pfam; PF02789; Peptidase_M17_N; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00631; CYTOSOL_AP; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000313|EMBL:KYO45802.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 362..369
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 522 AA; 56125 MW; DBC5CBFD07326B02 CRC64;
MLRGLLPRCS RCCHRRGPTL WPRACSTSSS AGSRGLVLGI YANEKEEGPP QFTDAGDAFD
RRVSGKLREL LSISGPLLKK GKTRIFHGLY QDFPSVVVVG LGKKSIGVND QENWDEGKEN
IRAAVSAGCR QVQDLEIPCV EVDPCGDAQA AAEGAVLGLY EYDEFKKRKK PVVTPQLHGS
DGKEAWQKGT IYGEGQNLAR HLMEAPANYI TPIKFAELVE QKLKAANSSM KIHIRSKSWI
EEQQMGAFLS VAKGSEEPPV FLEIHYSGSA NANDPPLVLV GKGVTFDSGG ISLKPSSGMD
AMRADMGGAA TVCSAIATAA TLNLPLNIIG LAPLCENMPS GRASKPGDVV RAKNGKTIQV
DNTDAEGRLL LADALCYAHN FNARAIVNAA TLTGAMDVAL GSAATGVFTN SSWLWTHLYE
ASILTGDRVW RMPLFEHYTK QVTDCPLADL SNVGKYSRAG GACTAAAFLK EFVTVSHWAH
LDIAGVMSNK DEVPYLRKGM AGRPTRTLVE FATRLSQDNQ SA
//
