ID A0A2G8KNP8_STIJA Unreviewed; 493 AA.
AC A0A2G8KNP8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 22-FEB-2023, entry version 12.
DE SubName: Full=Putative aminopeptidase NPEPL1-like {ECO:0000313|EMBL:PIK49631.1};
GN ORFNames=BSL78_13490 {ECO:0000313|EMBL:PIK49631.1};
OS Stichopus japonicus (Sea cucumber).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK49631.1, ECO:0000313|Proteomes:UP000230750};
RN [1] {ECO:0000313|EMBL:PIK49631.1, ECO:0000313|Proteomes:UP000230750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shaxun {ECO:0000313|EMBL:PIK49631.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PIK49631.1};
RX PubMed=29023486;
RA Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT "The sea cucumber genome provides insights into morphological evolution and
RT visceral regeneration.";
RL PLoS Biol. 15:E2003790-E2003790(2017).
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:PIK49631.1}.
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DR EMBL; MRZV01000455; PIK49631.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8KNP8; -.
DR STRING; 307972.A0A2G8KNP8; -.
DR Proteomes; UP000230750; 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; 3.40.630.10; Zn peptidases; 1.
DR Gene3D; 3.40.50.10590; Zn-dependent exopeptidases; 1.
DR InterPro; IPR011356; Leucine_aapep/pepB.
DR InterPro; IPR041417; NPEPL1_N.
DR InterPro; IPR000819; Peptidase_M17_C.
DR PANTHER; PTHR11963:SF4; AMINOPEPTIDASE NPEPL1-RELATED; 1.
DR PANTHER; PTHR11963; LEUCINE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF18295; Pdase_M17_N2; 1.
DR Pfam; PF00883; Peptidase_M17; 1.
DR PRINTS; PR00481; LAMNOPPTDASE.
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:PIK49631.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000230750};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..493
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013661322"
FT DOMAIN 312..319
FT /note="Cytosol aminopeptidase"
FT /evidence="ECO:0000259|PROSITE:PS00631"
SQ SEQUENCE 493 AA; 52678 MW; E5478B55B0C4A17C CRC64;
MATLRPEMSI AAICTLLWVL TIATFNLAVN NLHPSPTDTI SMWCNNATLA ALPLKVSRHN
TSSRAHSIHK LVKSCYTGAS EEHIVIVCER QNVFPSGCAV ARAFPLFSHK SGYAKVSQRR
VIVEFVVVGS NSRSVTDSEM EALTNAAAGI RLTQSIIDQP CNQMNTDAFV EEAKRVASEV
GSEILIIRDE ELNTKGFGGI YGVGKAAVHP PALVVLSHKP PEATQSIAWV GKGIVYDTGG
LCIKSKTSMP GMKRDCGGAA AVLGAFKAAV KTGFRENLYA VLCLAENAVG PHATRPDDIH
TMYSGRTVEI NNTDAEGRLV LSDGVSYAAK DLRADIIVDV ATLTGAQGIS TGRYHAAVLC
NREEWEQACV TSGRNSGDLV FPIVFSPELH FSEFASAVAD MKNSVADRSN AQSSCAGLFI
FSHLGFEFPG VWVHLDIASP CFSGERATGY GVALLLSLFG KASHSTLLQA VSPLGCSDED
EMVENATKKI RLV
//
