ID A0A091HJL1_CALAN Unreviewed; 728 AA.
AC A0A091HJL1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Seprase {ECO:0000313|EMBL:KFO95312.1};
DE Flags: Fragment;
GN ORFNames=N300_10102 {ECO:0000313|EMBL:KFO95312.1};
OS Calypte anna (Anna's hummingbird) (Archilochus anna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC Trochilidae; Calypte.
OX NCBI_TaxID=9244 {ECO:0000313|EMBL:KFO95312.1, ECO:0000313|Proteomes:UP000054308};
RN [1] {ECO:0000313|EMBL:KFO95312.1, ECO:0000313|Proteomes:UP000054308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N300 {ECO:0000313|EMBL:KFO95312.1};
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; KL217462; KFO95312.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091HJL1; -.
DR STRING; 9244.A0A091HJL1; -.
DR MEROPS; S09.007; -.
DR Proteomes; UP000054308; 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: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:UP000054308}.
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:KFO95312.1"
FT NON_TER 728
FT /evidence="ECO:0000313|EMBL:KFO95312.1"
SQ SEQUENCE 728 AA; 83964 MW; 2DE4184656CA4E61 CRC64;
VVNTDGGPRA LTLEDYLNGN FQYKTFFPYW VSDNEYLHQS AEDDIILYNV EMNYPTTLMT
NSTMKQVNAS NYLLSSDKYF IALESNYSKL WRYSYTASYH IYDLMYGGFV TENQLPHKIQ
YISWSPVGHK LVYVYQNNIY LKRSPMERAI KLTNDGKENE IFNGIPDWVY EEEMLATKYA
LWWSPNGKYL AYVQFNDSDI PVIEYSYFGE DQYPRKIIIP YPKAGAKNPT VKVFIVDTIN
PEAFGPKEVP VPAVIASSDH YFTWLTWVTD SRICVQWLKR IQNFSVLAIC DFKENSNTWD
CPENQQHIEE SQTGWAGGFF VSAPYFTSDS SSYYKIFSDK NGYKHIHYIN GSVENAIQIT
SGKWEAIYIF RVTNDEIFYS SNEFEGYPGR RNIYKISTGS KPIRKQCITC NLRKERCQYY
TARFSERSKY YALICYGPGI PISTLFENHG DRELRVLEDN WELQSALQGI KLPKEEINKL
EVDGITLWYK MLLPPQFDKS KKYPLLIQVY GGPCSQNVKE TFSINWITYL ASKEGIIVAL
VDGRGTAYQG DKILHAVYRK LGVYEVEDQI SAVKKFIEMG FIDEKRIAIW GWSYGGYVTS
LALGSGSGVF KCGIAVAPVS SWQYYASIYT ERFMGLPVES DNLEHYKNST VMARAKNFQN
VEYLLIHGTA DDNVHFQNSA QIAKALVNAQ VDFQAMWYTD QNHGIPGLSS KHLYTHMTHF
LKQCFSLS
//