ID A0A087XV20_POEFO Unreviewed; 1281 AA.
AC A0A087XV20;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 2.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Tripeptidyl-peptidase 2 {ECO:0000256|ARBA:ARBA00020244};
DE EC=3.4.14.10 {ECO:0000256|ARBA:ARBA00012462};
DE AltName: Full=Tripeptidyl aminopeptidase {ECO:0000256|ARBA:ARBA00032232};
GN Name=TPP2 {ECO:0000313|Ensembl:ENSPFOP00000009623.2};
OS Poecilia formosa (Amazon molly) (Limia formosa).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48698 {ECO:0000313|Ensembl:ENSPFOP00000009623.2, ECO:0000313|Proteomes:UP000028760};
RN [1] {ECO:0000313|Proteomes:UP000028760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000028760};
RA Schartl M., Warren W.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPFOP00000009623.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal tripeptide from a polypeptide.;
CC EC=3.4.14.10; Evidence={ECO:0000256|ARBA:ARBA00001910};
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; AYCK01005525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007554015.1; XM_007553953.2.
DR STRING; 48698.ENSPFOP00000009623; -.
DR MEROPS; S08.A56; -.
DR Ensembl; ENSPFOT00000009636.2; ENSPFOP00000009623.2; ENSPFOG00000009375.2.
DR GeneID; 103139378; -.
DR KEGG; pfor:103139378; -.
DR CTD; 7174; -.
DR eggNOG; KOG1114; Eukaryota.
DR GeneTree; ENSGT00390000014623; -.
DR OMA; SLRDFQC; -.
DR OrthoDB; 2441948at2759; -.
DR Proteomes; UP000028760; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008240; F:tripeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04857; Peptidases_S8_Tripeptidyl_Aminopeptidase_II; 1.
DR Gene3D; 1.25.40.710; -; 1.
DR Gene3D; 2.60.40.3170; -; 1.
DR Gene3D; 6.10.250.3080; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034051; TPP_II_domain.
DR InterPro; IPR022232; TPPII_C_art.
DR InterPro; IPR046939; TPPII_C_sf.
DR InterPro; IPR048384; TPPII_GBD.
DR InterPro; IPR048383; TPPII_Ig-like-1.
DR InterPro; IPR022229; TPPII_Ig-like-2.
DR InterPro; IPR046940; TPPII_Ig-like_sf.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR PANTHER; PTHR43806:SF14; TRIPEPTIDYL-PEPTIDASE 2; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF12580; TPPII; 1.
DR Pfam; PF12583; TPPII_C; 1.
DR Pfam; PF21316; TPPII_GBD; 1.
DR Pfam; PF21223; TPPII_Ig-like-1; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000028760};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 35..500
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 523..635
FT /note="Tripeptidyl-peptidase II first Ig-like"
FT /evidence="ECO:0000259|Pfam:PF21223"
FT DOMAIN 655..743
FT /note="Tripeptidyl-peptidase II galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21316"
FT DOMAIN 779..964
FT /note="Tripeptidyl peptidase II second Ig-like"
FT /evidence="ECO:0000259|Pfam:PF12580"
FT DOMAIN 1026..1083
FT /note="Tripeptidyl peptidase II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12583"
FT REGION 1009..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1170..1190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1029
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 44
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 264
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 449
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1281 AA; 140933 MW; F214C082FAB3D8A5 CRC64;
MAAHSTDEPF PFHGLLPKKE TGAASYLTRF PDYDGRGVLI AILDTGVDPG APGMQVTTEG
KPKIVDIIDT TGSGDVNMTT AVEPKDGTIT GLSGRTLKIP PAWVNPSGKF RIGVKNGYEF
FPKALKERIQ KERKEKMWDP AHRAALAEAC RKTEEFDLAH PTPSQMEKLQ KEDLQCQSEL
LASLEKKYSD PGPVYDCVLW HDGVTWRAVV DTSECGELSQ CTVLGSYREK QEYATLGNAE
MLNYSVNVYD EGNTLCIVTS GGAHGTHVAS IAAGYFPEEP ERNGVAPGAQ ILALKIGDTR
LSTMETGTGL IRAMIEVINY KCDLVNYSYG EATHWPNSGR ICEVITEAVQ KHNVIFVSSA
GNNGPCLSTV GCPGGTTSSV IGVGAYVTPD MMVAEYSLRE KLPPNQYTWS SRGPSTDGAL
GVSISAPGGA IASVPNWTLR GTQLMNGTSM SSPNACGGIA LILSGLKQSG IPPSVPAVRR
ALENTAQKVD DIEVFAQGHG IIQVDKALDY LTQHASLPTS RLGFSVSVGS QRGIYLREPA
QVLAPSDHGV GIEPIFPENT ENSERISLQL HLALTCAAPW VQCPSHLELM NQCRHVNVRI
DPVGLREGVH YTEVCGYDTA APTCGPLFRV PITVIIPAKV TDSRNQEVRF SDVHFRPGQI
RRHFITVPQG ASWAEITLTS HSGDVSSKFV LHAVHLVKQK AYRANEFYKF SSLLERGSLT
EAFPVLSGRV VEFCIARWWA SLGDVTVDYS ISFHGLSTSP SPLHIHASEG VTSFDVSSPM
RYEEVSPTVT LKSWVQPLRP LNSKIKALGV RDVLPNNRQL YEIILTYSFH QPKSGEVTPS
CPTLCELLYE SEFDSQLWML FDQNKRLLGS GDAYPHQYSL KLEKGDYTVR LQVRHEQSSE
LERLKDLPFV VSHRLSNTLS LDVYESHRAA LMAKKKANSV TLCPGATQPF YVTPLPDDKI
PKGTSPGCYL SGSLIVPKSE YGKKAGQASA KRQGKFKKDI VPVIYHLIPA PNKSKNGGKE
KDKDGDKEKD LKEEFAEAVR DLKIQWMTKL DSSSIYDELR ENYSDYLPLH VQRLHQLDSE
KERVKRLREV VSAAEIVMSH IDQTALAVYF TMKTDPRPDA ASIKTDMEKQ KSSLLDALCR
KGCALADQLL LPSTLQSGAG AVATEQAAVG EEEEEVGEQL ASSSDDPVDN TSNALMDTFW
EVQKWAELTD SKVLTFSYKH ALANKMYGRA LKYASKMVEE KPSKENMKNC VQLMRHLGWT
HCTAFSENWL PVMYPADYSP F
//
