ID A0A093QH57_PHACA Unreviewed; 729 AA.
AC A0A093QH57;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Seprase {ECO:0000313|EMBL:KFW88273.1};
DE Flags: Fragment;
GN ORFNames=N336_06924 {ECO:0000313|EMBL:KFW88273.1};
OS Phalacrocorax carbo (Great cormorant) (Pelecanus carbo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Suliformes; Phalacrocoracidae;
OC Phalacrocorax.
OX NCBI_TaxID=9209 {ECO:0000313|EMBL:KFW88273.1, ECO:0000313|Proteomes:UP000053238};
RN [1] {ECO:0000313|EMBL:KFW88273.1, ECO:0000313|Proteomes:UP000053238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N336 {ECO:0000313|EMBL:KFW88273.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Cell projection, invadopodium membrane {ECO:0000256|ARBA:ARBA00004341};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004341}.
CC Cell projection, lamellipodium membrane
CC {ECO:0000256|ARBA:ARBA00004485}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004485}.
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DR EMBL; KL420195; KFW88273.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093QH57; -.
DR MEROPS; S09.007; -.
DR Proteomes; UP000053238; Unassembled WGS sequence.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR PANTHER; PTHR11731:SF136; PROLYL ENDOPEPTIDASE FAP; 1.
DR PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR Pfam; PF00930; DPPIV_N; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 4: Predicted;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000053238}.
FT DOMAIN 75..441
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 523..726
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW88273.1"
FT NON_TER 729
FT /evidence="ECO:0000313|EMBL:KFW88273.1"
SQ SEQUENCE 729 AA; 84296 MW; DAFEE18F019AFE75 CRC64;
VVNTDDHPRA LTLEDYLNGN FQYKTFFPYW VSDNEYLHQS AEDDIILYNV EMNYPTTIMT
NSTMKQVNAS NYVLSSDKYF IALESNYSKL WRYSYTASYH IYDLIYRGFV TENQLPREIQ
YISWSPVGHK LVYVYQNNIY LKQSPREAPI KITSDGKQNE IFNGIPDWVY EEEMLATKYA
LWWSPSGKYL AYVQFNDSDI PVIEYSYFGE DQYPRKIIIP YPKAGAKNPT VKVFIVDTVN
AEAFGPKEVP VPAVIASSDH YFTWLTWVTD SRICVQWLKR IQNFSVLAIC DFKENSNTWD
CPESQQHIEE SQTGWAGGFF VSTPYFTSDS SSYYKIFSDK NGYKHIHYIN GSVENSIQIT
SGEWEAIYIF RVTNDAIFYS SNEFEGYPGR RNIYKISIGS KPIRKQCITC NLRKERCQYY
TARFSEHSKY YALICYGPGI PISTLFESHG DRELRVLEDN WELQSALQEI KLPKEEINKL
EVDGITLWYK MLLPPQFDRS KKYPLLIQVY GGPCSQNVKE TFSISWITYL ASKEGIIVAL
VDGRGTAYQG DKILHAVYRR LGVYEVEDQI SAVKKFIEMG FIDEKRIAIW GWSYGGYVTS
LALGSGSGVF KCGMAVAPVS SWEYYASIYT ERFMGLPVES DNLEHYKNST VMARAKNFQN
VEYLLIHGTA DDNVHFQNSA QIAKALVNAQ VDFQAMWYTD QNHGIPGLSR KHLYTHMTHF
LKQCFSMSE
//