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Database: UniProt
Entry: A0A091HJL1_CALAN
LinkDB: A0A091HJL1_CALAN
Original site: A0A091HJL1_CALAN 
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
//
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