ID H3AV91_LATCH Unreviewed; 1266 AA.
AC H3AV91;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
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:ENSLACP00000013562.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000013562.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000013562.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; AFYH01057237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01057238; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01057239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01057240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01057241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01057242; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01057243; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01057244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01057245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01057246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H3AV91; -.
DR STRING; 7897.ENSLACP00000013562; -.
DR Ensembl; ENSLACT00000013658.1; ENSLACP00000013562.1; ENSLACG00000011941.1.
DR eggNOG; KOG1114; Eukaryota.
DR GeneTree; ENSGT00390000014623; -.
DR HOGENOM; CLU_003084_1_0_1; -.
DR InParanoid; H3AV91; -.
DR OMA; SLRDFQC; -.
DR TreeFam; TF105647; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000011941; Expressed in chordate pharynx and 6 other cell types or tissues.
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; 2.20.25.690; -; 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; 1.
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:UP000008672};
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..726
FT /note="Tripeptidyl-peptidase II galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21316"
FT DOMAIN 783..969
FT /note="Tripeptidyl peptidase II second Ig-like"
FT /evidence="ECO:0000259|Pfam:PF12580"
FT DOMAIN 1026..1086
FT /note="Tripeptidyl peptidase II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12583"
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 1266 AA; 139723 MW; D34A186C3E27594B CRC64;
MASRTADEPF PFHGLLPKKE TGAASFLSRF PELDGRGVLI GILDTGVDPG APGMQVTSDG
KPKIIDIIDT TGSGDVNTST VIEPKDGTII GLSGRTLKIP TSWINPSGNY HIGIKNGFEF
YPKPLKERIQ KERREKLWDP VHRVALAEAC RKQEEFDGTH SNLSQADKLI KEELQCQVEL
LNSLEKKYND PGPVYDCLVW HDGETWRACM DTSECGDLSN CTVLRSYREA QEYASLGNSE
MLNYSFNIYE EGNVLSVVTS GGAHGTHVAS IAAGYFPEEP ERNGVAPGAQ ILAIKIGDTR
LSTMETGTGL IRAMIEAIRN KCDLVNYSYG EATHWPNSGR VCEVINEAIY KHNIIYVSSA
GNNGPCLSTV GCPGGTTSSV IGVGAYVSPD MMIAEYSLRE KLPANQYTWS SRGPCTDGAL
GVSFSAPGGA IASVPNWTLR GTQLMNGTSM SSPNACGGIA LVLSGLKASG VAYTVHSVRR
ALENTAMKVE NIEAFAQGHG IIQVDKAYDY LIQNASFSTS NLGFTVSVNN NRGIYLREPV
QVAAPSDHGV GIEPVFPENT DNNERISLQL HLALTCSASW IQCPPHLELM NQCRHVNVRV
DPHGLREGVH HTEVCGYDTT TPNAGPLFRV PVTVVIPTRL DAASCYELAY KDVHFKPGEI
RRHFIEVPQG ATWAEVTVSS CSADVSSKFV LHAVQLLKLK AYRANEFYKF SSLPEKGSLV
EAFPVLLTLS AGPCSVTATG EYWGAVQEIS RKLKVNYSGV LSAAPDLWIY HASEGISRFD
VLSTLKYEDL SVSINLKSWV QTLRPVSAKT RPLGFRDILP NNRQLYEMVL MYNFHQPKTG
EVTPSCPLLC ELLYESEFDS QLWMLFDQNK RLMGSGDAYP HQYSLKLEKG DYTVRLQVRH
EQISELERLK DLPFVVSHRL SSTLSLDIYE NHANALLGKK KSNSLTLPPS CSQPFFVTSL
PDDKVPKGAG PGCYLLGTLT LSKTELGKKA GQAAAKRQGK FKKDVISVHY HLIPSPIKAK
NGSKEKDTEK DRDVKEEFSD AVRDLKIQWM AKLDTIALFS ELKESYPNHL PLYIAQLHQL
DSEKERIKRL NEIVAAADTV ITHIDQTALA VYLAMKNDPR PDASTIKSDM EKQKSSLIDA
LCRKGCALAD RLIQLQSQEG AAAGDEGSAQ DTPDCLLKTL GDCFWEIQKW TELTDSKILT
FAYKHALVNK MYGRALKFAT KLVEEKPTKE NWKSCLLLMK LLGWSHCVSF TENWLPVMYP
LDYTVF
//
