ID A0A182TIE9_9DIPT Unreviewed; 1231 AA.
AC A0A182TIE9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Scavenger receptor class A {ECO:0008006|Google:ProtNLM};
OS Anopheles melas.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=34690 {ECO:0000313|EnsemblMetazoa:AMEC002866-PA, ECO:0000313|Proteomes:UP000075902};
RN [1] {ECO:0000313|Proteomes:UP000075902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM1001059 {ECO:0000313|Proteomes:UP000075902};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA Gargeya S., 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 melas CM1001059_A (V2).";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMEC002866-PA}
RP IDENTIFICATION.
RC STRAIN=CM1001059 {ECO:0000313|EnsemblMetazoa:AMEC002866-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 AlphaFoldDB; A0A182TIE9; -.
DR STRING; 34690.A0A182TIE9; -.
DR EnsemblMetazoa; AMEC002866-RA; AMEC002866-PA; AMEC002866.
DR VEuPathDB; VectorBase:AMEC002866; -.
DR Proteomes; UP000075902; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00112; LDLa; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.170.140.10; Chitin binding domain; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR Gene3D; 3.10.250.10; SRCR-like domain; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR002557; Chitin-bd_dom.
DR InterPro; IPR036508; Chitin-bd_dom_sf.
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; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24258; SERINE PROTEASE-RELATED; 1.
DR PANTHER; PTHR24258:SF128; TEQUILA, ISOFORM G; 1.
DR Pfam; PF01607; CBM_14; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF00530; SRCR; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00494; ChtBD2; 1.
DR SMART; SM00192; LDLa; 2.
DR SMART; SM00202; SR; 2.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57625; Invertebrate chitin-binding proteins; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 2.
DR SUPFAM; SSF56487; SRCR-like; 2.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50940; CHIT_BIND_II; 1.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 2.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50287; SRCR_2; 2.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Membrane {ECO:0000256|SAM:Phobius};
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};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 177..232
FT /note="Chitin-binding type-2"
FT /evidence="ECO:0000259|PROSITE:PS50940"
FT DOMAIN 676..787
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 836..935
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 988..1223
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 85..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 644..662
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 656..671
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 756..766
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 904..914
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 1231 AA; 136500 MW; 3D2310A429F1A525 CRC64;
MRQRIWNRPR LVLLALAVLI GGWCNMVVVG IYDPRTAPHS RHHVHMMPEM HGAYSQVHHH
RAQDPTPQQY VQTDLYQYVQ PQRQHPSLVA GPQQQQQQQH GPSGPQYQPG VPLAPYPTET
QRSPAYGRSQ AYTQQPAPVR LAPRFGYGEE DRLIGETAPA AKLIRQPVHT LLKDFNGLEC
PEGRTGHFPY VMDCRQFLSC WKGRGFILNC APGTLFNPNT RECDHPSKDC GPGTAFNPLI
LTCDHLRNVD CDKSENVIVD YDRPTSRPVA SGPTSHYYPS HIPAGSQPVP AVVNPHQQSR
PTVTAPQQQT PPRQPPATGD RAPAHPDVEQ IDTDHQPTES NFDEDYGEQP DADGEEPVYD
GFDLRSNFGA PEPVDRRRPK ASRTQATTTA KPYPVYIRPP SRQPESLHRD PDVVQSVQRP
VYAALPLEQT TPVPTSTTSR PLRTPFPTVR KEDIEIQQHL DALKLMLTPY MKEHKDTVAL
NTTKLSTMMT TTTTTTEPPP IVQVIGLPAP TPRNSYKPSS AAAPYVLPRA SEVNDFFYGA
SEPVPLASWP LPPPYITEPV EGPAKKQPES VVYPIYRRTT PTTTTTTASP PPAPAIRSRF
GDNRPSWRPL IVPHATTTKT PTTTPPAPTT STTPRDPCYG KFNCGNGVCI DEAEVCDGRD
GCGNRADEQV CDHIGYELKL SKKAQGSVEV RVYDRWGYVC DDGFTLEAGN VVCRELGFAG
GAIEIKSHSY FPPNGTDPDE PEQQYGPFFM MDAVRCQGNE SSLRECSFNG WGVSDCNREE
VVGVVCRTPV MSCPQDYWLC HASEECIPVQ FLCDNVRDCA DGSDESPDHC KAPLAVRLVA
GPTDREGRVE INYHGTWGTV CDDDFGVREA RVICRQLGFN GTAEVRKSVY PPGVGQIWLD
QVACNGTEPS IEDCVHWHWG EHNCGHTEDV GVRCGVYVPT KARAARLRAT RPNPRFDFVE
RSRKIHPDTC GRVLIDPTLR KPTYGARVVH GSETVYGHHP WQASLRVKTM HWCGAVLITR
YHVLTAAHCL IGYPKSTYRV RIGDYHTAAY DNAELDIFIE NTYIHEQFRE GHHMSNDIAV
VVLKTPVRFN DYVQPICLPA RDAPYLPGQN CTISGWGATE AGSKDSSYDL RAGTVPLLPD
SVCRRPEVYG DSLIDGMFCA GTLEPGVDSC DGDSGGPLVC PNSEGLHTLT GIVSWGKHCG
YANKPGVYLK VAHYRDWIEQ KLNQSLHQHG V
//
