ID L5L6I9_PTEAL Unreviewed; 876 AA.
AC L5L6I9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Transmembrane protease, serine 9 {ECO:0000313|EMBL:ELK19344.1};
GN ORFNames=PAL_GLEAN10005988 {ECO:0000313|EMBL:ELK19344.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK19344.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR EMBL; KB030265; ELK19344.1; -; Genomic_DNA.
DR AlphaFoldDB; L5L6I9; -.
DR STRING; 9402.L5L6I9; -.
DR MEROPS; S01.358; -.
DR InParanoid; L5L6I9; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 1.
DR CDD; cd00190; Tryp_SPc; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 4.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR036364; SEA_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF7; HYALIN; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF00089; Trypsin; 4.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00192; LDLa; 1.
DR SMART; SM00020; Tryp_SPc; 3.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF82671; SEA domain; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 3.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 3.
DR PROSITE; PS00134; TRYPSIN_HIS; 2.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Hydrolase {ECO:0000256|RuleBase:RU363034};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:ELK19344.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|EMBL:ELK19344.1};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..318
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 386..618
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 613..875
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 324..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 185..197
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 205..220
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 876 AA; 93383 MW; E87F46A1FE647193 CRC64;
MEPTVGESQL VPRAAKDVPT RDAVCCRVAL CAAVAASIVI VTLAVLVASL SIQGVDVEHT
AELRGIRYSR SLQQEASDYY RMLTPTLEML FARSFWKTEL EASCVGCTVL GYRDGNASVL
VRFRLHFLLL ALRSLDLGLE RELLQQGLRA RLQGHGIPLA AHGTLVSAML TGKKHTPDVT
LSGRCPESAF SCGNGQCVTT VNPECDDKVD CSDGSDEARC VVKPEMLQKA TVELLDQALC
ASLYGHSLTD RMMCAGYLGG KVDSCQGDSG GPLVCEEPSG RFFLAGIVSW GIGCAEARRP
GVYARVTKLR DWILEAIATA SKPLSPTVVP GPATPSTAGP TSPESQVVGT PTQASLAPSS
APVDSATTSK PPECGARPAL EKPARIVGGF GAAAGEVPWQ ASLKEGSRHF CGATVVGDRW
LLSAAHCFNH TKVELVRAHL GTVSLSGVGG SPVKMGLKRA VLHPQYNAGI LDFDAAVLEL
ARPLVFGKYV QPICLPLATQ KFPAGRKCMI SGWGSTQEGN ATKPDALQRA SVGIIDQKAC
SALYNFSLTD RMLCAGFLEG QVDSCQGDSG GPLACEETPG VFYLAGIVSW GIGCAQAKRP
GVYVRIARLK GWILDTIAAG GGEWPWQVSL WLQRREHRCG AVLVAEKWLL SAAHCFDVGT
GEAMDRAPGG QGRGVARHGD QANACPHAPR SYGDPKQWAA FLGTPFLSGA DGRLERVARI
YKHPFYNLYT LDYDVALLEL ATPVRRSRLV RPICLPDPAP RPRDGTRCVI TGWGSVREGG
RRRPAPSGVR GLRSRACRRY YPVQISSRML CAGSPHGGVD SCSGDAGGPL ACREPSGRWV
LTGVTSWGYG CGRPHFPGVY TRVAAVRGWI GQNIQE
//
