ID A0A2T7P3K9_POMCA Unreviewed; 733 AA.
AC A0A2T7P3K9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Xaa-Pro aminopeptidase 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=C0Q70_10559 {ECO:0000313|EMBL:PVD27983.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD27983.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD27983.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD27983.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD27983.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|ARBA:ARBA00008766}.
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:PVD27983.1}.
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DR EMBL; PZQS01000006; PVD27983.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7P3K9; -.
DR STRING; 400727.A0A2T7P3K9; -.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg6.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR CDD; cd01085; APP; 1.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 2.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR033740; Pept_M24B.
DR InterPro; IPR032416; Peptidase_M24_C.
DR PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1.
DR PANTHER; PTHR43763:SF4; XAA-PRO AMINOPEPTIDASE 2; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF16189; Creatinase_N_2; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF16188; Peptidase_M24_C; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..733
FT /note="Xaa-Pro aminopeptidase 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015638179"
FT DOMAIN 56..182
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 386..603
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT DOMAIN 614..675
FT /note="Peptidase M24 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16188"
FT REGION 674..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 733 AA; 80757 MW; F0A31E9B8B2B42A1 CRC64;
MLSEARLILA LSTASLCHGG PIAGEGGHRT KREAGQPTLA DRLNCSQGDR VNTTQRLADM
RAAMRQLDID AFIILSDDAH GSEYPSERDE RRGFISGFTG SAGQAVVTLH QAALWTDGRY
FLEAEGALDC NWIFMRSGDA NVPSISQWVI SELANTSGVV GADPFLVSNS QWQSFEKAFV
QANITFKQVF KNPVDTAWGG YQPAPPMSNI TALPMEFAGK TWQDKITELR QSMTAKNADV
FVVTSLDETA WLFNLRGGDI SYNPVFLSYA IVEKTSVRLY LLNKNERLTQ NATDPVTSIK
LKEHLNTGDT GSCTGSSASC VEVVDYNETA IVEDVKALAT AGKKIWVTFV CNYAIFSAIP
EASRIQDRSS IALAKAMKNQ VEREGMERCY IRDSLILIKF LAFLEKEIKN GHYWTEVSAA
ERLKEMRLQG QYNRGLSFES ISGSGPNGAV IHYRPLNATN RQITTTEMYL LDSGGQYLDG
TTDVTRTMHF GTPSSHEKEC YTRVLMGAID LANLVWPQGL YGREIDMAAR APLWQVGLEY
NHGTGHGIGA YLSVHEGPGF ISLSKSSFNA QEELKPYMVF SDEPGYYENG KFGIRLETIV
MVEPTSIKAP SNKTFYRFKP MTLVPFEPNL IDTELLTKSQ ITWLNKYHEL VWNTMKDNLT
SEEERSWLWS RAQPIGEDTN STTPAATTVG SSPTGSTPAT TTVGNSPTGS SPLVTPITSA
TVFLVAAVTS LYL
//