ID A0A182PDL4_9DIPT Unreviewed; 1418 AA.
AC A0A182PDL4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Scavenger receptor class A {ECO:0008006|Google:ProtNLM};
OS Anopheles epiroticus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI005019-PA, ECO:0000313|Proteomes:UP000075885};
RN [1] {ECO:0000313|Proteomes:UP000075885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Howell P., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles epiroticus epiroticus2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AEPI005019-PA}
RP IDENTIFICATION.
RC STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI005019-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000256|ARBA:ARBA00024195}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR STRING; 199890.A0A182PDL4; -.
DR EnsemblMetazoa; AEPI005019-RA; AEPI005019-PA; AEPI005019.
DR VEuPathDB; VectorBase:AEPI005019; -.
DR OrthoDB; 4252799at2759; -.
DR Proteomes; UP000075885; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07066; CRD_FZ; 1.
DR CDD; cd00112; LDLa; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
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; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
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; PF01392; Fz; 1.
DR Pfam; PF00057; Ldl_recept_a; 2.
DR Pfam; PF15494; SRCR_2; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00192; LDLa; 2.
DR SMART; SM00202; SR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS50068; LDLRA_2; 2.
DR PROSITE; PS50287; SRCR_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 823..945
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 1031..1080
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 1155..1406
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 139..184
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 201..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 901..942
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 905..929
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 966..984
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 978..993
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 996..1008
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1003..1021
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1015..1030
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1418 AA; 154127 MW; 9EDC0968314DD28E CRC64;
MASSFANCSY APDPSAADGN PFNYGERSLL DDREKRGVTR ASSLALPNHS LLDLLEQKQK
LYDTIHLTPP PKGNGTRRHS SDSFPMIENE NFQIPQRQQS KKSSQGLPPP VPKRTFQGNF
PRKPPDSFEV QKRASLLALD SYQQQQQQQQ QQVQQLHQQL QQQLQQQQQQ AQQQQTYAQF
ARAERICKSA FEDQPFSYYP APKSAKSSSG ATGTGNTAAG GGSTCHTSVS ATSFDDLGEP
DDFVLFSKKM ASIESNRSSS DSNKSQTTID TGYVSANETD RSVLTGGSCS SAKGGGASSF
RSRFSSEDTQ SSLDSFLSSE LHRTDTIDSL PLNDSPFSLK KNVFNFDLKT SPLIRGSSTV
SPNSIDEKLD SCSPRSIESK GSRKLPTVPT RKGPPSGVVM QPKLPPPGGA TTGGSSRMTP
PLPPSRSQQA FETRKLQKLQ QQQQQQTQLN NVASTHKTAL ESLQELYSRP LGIRRNIHRP
PPLSQQQMVG VGKGSLLGQR QDSNDGFSIT SSPGFQNKAM ESSLLQQPHA TSKFNRSTIR
GKPPMDTTAS GLGGTNIIPN NLTAIMNAAG STPGGTTSTG PTSMAASTAG GSANVSSDGI
GGIAGVSTST IRSVPPRVSM RQDSSISSDS FSQTSSPSYN SKIMEAPLLS HAAKMPKVSK
PIAKNLDEIT KDSPADVNGT AAIIKSASTP ASLQTIVRLS NGSNVSLQHK KFQILKTRKN
SNPYVTSGRL KFRLCQILLN AVGLLAIAGG LAAYFNAYPT IKFVNQTITR TAVPPAPPGN
SLTGAGGAVS SVPASGSGPA SAAGTPGRTA LDIPGGFRGD RNPAPGVCLP VIVKFCQQHR
VPYNYTVFPN YIGHFAQPEA QIEIDLFEAL VDVQCYELVP LFLCSLFVPK CGYSGATIPP
CKSLCTETMR RCSFFFDVFG LELPEYLRCS IFNDAVSDQE ECVGMAEYKE SIIRSRRPMA
CSGFLCDKRR CIPSDWKCDG HVDCQDQTDE AHCDFCGDDA IHCGKGQCMS QKHVCDGTPN
CPYGQDERNC IRLSERNGDL GRGTLEVYKA DLKQWAPACV KNWDPATSPT MICSLLGYSS
VNSSRTAMRG SNRTLISTKD ASSMWRMYQK KDVNLIKEFN SCDINSRYPV AELTCSNFEC
GKVRNRKYYK ASKRIVGGLT SNPGDWPFIA AILGGPEEVF YCAGVLIADQ WVLTASHCIG
NSPTSHTMRN VNDWTIQLGI TRRKSHTYYG QKVKVKTVIP HPMYNLHIPH DNDIALFQLA
TRVAFHEHLL PVCLPPPHIR ELPTGINCTV VGWGKREERN STPNGASYEP TLNEVNVPIV
SRDLCIDWLE TFNVTEGMIC AGYQEGGRDA CQGDSGGPLL CPYPNEKDRW FVGGIVSWGV
RCAHPKLPGV YANVPKFIPW IMAQIHNHSI LQTDTVGR
//
