GenomeNet

Database: UniProt
Entry: A0A1W4WAL0_AGRPL
LinkDB: A0A1W4WAL0_AGRPL
Original site: A0A1W4WAL0_AGRPL 
ID   A0A1W4WAL0_AGRPL        Unreviewed;      2240 AA.
AC   A0A1W4WAL0;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Uncharacterized protein LOC108734135 {ECO:0000313|RefSeq:XP_018321049.1};
GN   Name=LOC108734135 {ECO:0000313|RefSeq:XP_018321049.1};
OS   Agrilus planipennis (Emerald ash borer) (Agrilus marcopoli).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia;
OC   Buprestoidea; Buprestidae; Agrilinae; Agrilus.
OX   NCBI_TaxID=224129 {ECO:0000313|Proteomes:UP000192223, ECO:0000313|RefSeq:XP_018321049.1};
RN   [1] {ECO:0000313|RefSeq:XP_018321049.1}
RP   IDENTIFICATION.
RC   TISSUE=Entire body {ECO:0000313|RefSeq:XP_018321049.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC       pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR   RefSeq; XP_018321049.1; XM_018465547.1.
DR   STRING; 224129.A0A1W4WAL0; -.
DR   EnsemblMetazoa; XM_018465547.1; XP_018321049.1; LOC108734135.
DR   GeneID; 108734135; -.
DR   KEGG; apln:108734135; -.
DR   InParanoid; A0A1W4WAL0; -.
DR   OrthoDB; 3090466at2759; -.
DR   Proteomes; UP000192223; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00112; LDLa; 5.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 5.
DR   Gene3D; 3.30.70.960; SEA domain; 1.
DR   Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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; IPR000082; SEA_dom.
DR   InterPro; IPR036364; SEA_dom_sf.
DR   InterPro; IPR001190; SRCR.
DR   InterPro; IPR017448; SRCR-like_dom.
DR   InterPro; IPR036772; SRCR-like_dom_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   PANTHER; PTHR24270:SF66; CUB AND LDLA DOMAIN, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR   Pfam; PF00057; Ldl_recept_a; 5.
DR   Pfam; PF01390; SEA; 1.
DR   Pfam; PF15494; SRCR_2; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00192; LDLa; 5.
DR   SMART; SM00202; SR; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 5.
DR   SUPFAM; SSF82671; SEA domain; 1.
DR   SUPFAM; SSF56487; SRCR-like; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS01209; LDLRA_1; 4.
DR   PROSITE; PS50068; LDLRA_2; 5.
DR   PROSITE; PS50024; SEA; 1.
DR   PROSITE; PS50287; SRCR_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000192223};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT   DOMAIN          380..505
FT                   /note="SEA"
FT                   /evidence="ECO:0000259|PROSITE:PS50024"
FT   DOMAIN          1872..1921
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          1970..2229
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          103..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          557..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          694..736
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          768..800
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          829..879
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1065..1124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1227..1262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1374..1399
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1466..1494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..126
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        324..341
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        358..375
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..577
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        595..610
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        612..629
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        694..711
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        849..864
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1087..1124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1238..1262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1477..1491
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        1701..1716
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1727..1745
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1739..1754
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1779..1794
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1819..1834
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1856..1871
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   2240 AA;  248889 MW;  05729A71AD5AE22F CRC64;
     MDADSSYGGS DTAHDGTLGQ DSNSMDTSHS NPSHDPTNTN SRSSPDSSNY YKNEISLPVN
     CDEGDFQKNG KTPTLPQYLS TANFNIDATL ENHNNLEELN KKYRSSQRLN ETPKSSKKDK
     AGLDNPAYLD DENVKVNNDD TMGYRNGNLN SSPKLGHEDE PQAEAVNLEL INLKPNGKDV
     TGPYENGKGI SGIPVKKDNF ESGTPYDEYF VPVNEHRKYM SYFPFDTTTR NKGRNSVTFA
     ETTVSSTTGV DDFGLSVTTP ERGIVEYPDW LNVQENSRYQ HSFISPLIGS GFSTYFKTDS
     NVLVLVGIIG NPEAHPIEEG RHFGGSSSTD SIKTAGGLFG SNSDGRTMEA EKAPITPSPP
     SSTVPSLPPT TPKPLSEVTV PRTIQSQFKI DNLQYEPELG NKNSSEFKEL AEAIEEELKS
     ILFSRDVLNY GSAEIQLKVL EFSPGSVVVK FRVGWVMKDG VHNAKDPIDR DALEKKLRDA
     LAYNHGYIAN YRIADDSVTV ETVIDLCKTN NNNGCEYNCS FSYKIEDFIC ECPEGEYIQE
     DGKKCGQQHH LTTEHIDHNH GFEHSNEGDD KEHEQVAATF ETSSVPHTEK EVKAETTVSP
     ATQPYATSSH EPEGVSEEHE HQEEHEQHEH VTPIITLIST QTHTTIQEPV QETSAHEDDN
     IQEEYHPLQL PVTTTTTTET PVTYGNVNEV IPLSTEKDLK EEEEQSTEIK DVNEPEQATT
     GLVDSHSHSE EDTGLQTSVH VITTTAQSIS ETTTHSQSPM YWENETNQPI QETSLPSRTE
     SVNEHQEEEE QEEENTSTHV LYTTSTPIHE ESEEEEEKHV ATEVHLPVAN ESYSSERTEP
     ANVSHALEET ESAVETTTEP RIQTPKPFET EESEHGNNET SVSHATSFEQ ITTASSVAES
     VTVNPTTTEN LISIHSSLPH QLIENYTTTS PVVTVSESVS VTNTYNEMDN ASDSDRQPKF
     DITLGHTPVE PEMEYHTHDH EDEDERETIP FMHQEVQLVT TDRIKTEEAT ISSVEEQSSH
     TENSSLPFGL VHKEENNSMM AINETDGVLT TTFTPYTSEE SLFVHHTSPP SFLESSEEED
     ETQSTLMEDS NESSSTALSA SSEEMKVEPT QTTTSSEMEL TSFQETSTST EYTFSGRSFE
     SNHPALFAND HNNVTYLEDN STMSKQININ ETLHRPLSTF ENDNLNGEDE RQEFTTSTVA
     PRLDNDEKNV TNPLDPNVTD VALGVLPLEE DKSGRSQNSS RSTDNTEINT TTNTNETENT
     SVPEMIADDH NTISSTTYSI AAVENSTQES TNNTSPTEKP LNDTDIEVHK WEDTTTTVSN
     VSEEYNQKNE SSTVSFENLT TENDINDEEQ STSLSLFNAV EPITLKYEQS TNLSSNENAV
     NESAAEPSHL METSNGTNEN NDTTISQLES YVNGTNEIHT NNATSNSDED LIAMETTTTS
     LQKPKMFSNV PVEESTMNNN ETVANYSSIS EAPDSSKTIP EPKENETSTE SHSFGDDMLI
     TTASHNETSH LYEVHEVTDD ITTPTPTRTF NYSPLPVIPL TDSEPIENEK INIESDNLYS
     SNLNDISDEK EKYSSKYYYS DKKKEFSKTV DAPTTESIQG SNNTDQEEDH LIATDFVSHI
     TITDKPNNAT IAPINNLSST QTTNTIIEST EPVYNVTSEV KPVVEGYTLS SFSRCSAGQF
     QCVNGTSTKG GSYCVSNSDR CDSVKDCTDG SDEVGCDQEN CKDNFQCKSG QCLKRHLVCD
     GIFNCDDNSD EENCESWKCN FDELSCGDGK RCIPLSWKCD GKSHCFDGRD EQNCHSQPCE
     SNHFYCSEQD SCIPASWRCD GVDDCKSGED EKLCECGIDQ FKCQTGGGCI QAENRCDGIE
     QCPDLSDEWN CLRLRETNDT SSYLEALVSN NSWQPICADF WNTTYSDLAC QSMGYAKATS
     TNYKLLEKSS SGSQFLKLNP SERYGASLSA QLIKTDSCDN VVTLTCQENV CGNNNGLDTS
     SFGSKNENGN EKGWPSIALL FNRRYQIQCT ANIVTPNWVI ASYACLYSVS GQPPSSNPYD
     WELLAGGNHF FDSSAENSSI QSLSVKNIIP YPQAKYSQFI YRNNIALVQL MKPLDFEKNI
     SAVCLPPQNE EPNQYCITVG WSMKKPGESS LKEYLRYLPD LNQNKRDCNS SDHYNGRFTT
     DLLCVDHLTT DEPCEDDQGA PLMCFSESSQ NWELRGLLSL DGNCQKFHRP SLFTSTSGEI
     GTWIENTIGT KPKPFNNKLQ
//
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