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Database: UniProt
Entry: A0A151JY52_9HYME
LinkDB: A0A151JY52_9HYME
Original site: A0A151JY52_9HYME 
ID   A0A151JY52_9HYME        Unreviewed;      2645 AA.
AC   A0A151JY52;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Low-density lipoprotein receptor-related protein 1B {ECO:0000313|EMBL:KYN40104.1};
GN   ORFNames=ALC56_05512 {ECO:0000313|EMBL:KYN40104.1};
OS   Trachymyrmex septentrionalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=34720 {ECO:0000313|EMBL:KYN40104.1, ECO:0000313|Proteomes:UP000078541};
RN   [1] {ECO:0000313|EMBL:KYN40104.1, ECO:0000313|Proteomes:UP000078541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tsep2-gDNA-1 {ECO:0000313|EMBL:KYN40104.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN40104.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex septentrionalis WGS genome.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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; KQ981533; KYN40104.1; -; Genomic_DNA.
DR   STRING; 34720.A0A151JY52; -.
DR   Proteomes; UP000078541; 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:InterPro.
DR   CDD; cd00112; LDLa; 5.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 5.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
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; IPR017448; SRCR-like_dom.
DR   InterPro; IPR001254; Trypsin_dom.
DR   PANTHER; PTHR24252:SF8; ACROSIN; 1.
DR   PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR   Pfam; PF00057; Ldl_recept_a; 5.
DR   Pfam; PF15494; SRCR_2; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00192; LDLa; 5.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 5.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS01209; LDLRA_1; 4.
DR   PROSITE; PS50068; LDLRA_2; 5.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; Lipoprotein {ECO:0000313|EMBL:KYN40104.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Receptor {ECO:0000313|EMBL:KYN40104.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078541};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        241..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2422..2639
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          505..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          580..905
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          918..942
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1007..1045
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1291..1348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1639..1659
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1699..1747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2057..2083
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..52
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        512..555
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..769
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        832..849
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        859..878
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        886..905
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        921..942
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1007..1024
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1302..1348
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2061..2083
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        2119..2134
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2145..2163
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2157..2172
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2177..2189
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2184..2202
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2196..2211
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2235..2250
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2252..2264
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2259..2277
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2271..2286
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   2645 AA;  292768 MW;  9CBEC95A5362150F CRC64;
     MSNAAGTDNP AFANEDECVS GSKLENGGQQ QAASNQDRKS SADSAPVENG HQQSFISQHY
     VEPIKPSSEP CYKTETRIEV PADNTEKTVP EPKLNGVHGN GNNNDASFLN NSATSVQIND
     SGKKEQIEAV NLELVSMRPY TGNNIQTKGQ EACEVPADPY EEYFVPVNEH RKYIRGPEAE
     VETTVAGVRF DLGPGVGREG LSLRDPAAGL VDYSHWLTAL RGEKLYVTKD KRSRNSYWRR
     MAWGCALLVI VIAVIIAILA ATGVFPIPAT EPLENVEANN TRQFNEVQTA GSREYVKDPP
     LSPPPLTSTF PPWPTTDETL FDIVPDALDG TLRLDDFNWN DDFSDIKSRV YRQVSSEIEE
     HLGNILRQAG STSIITVYDI NKEGEIRFRI SHPPRNAPEE SQEYIEDVLR KNGNMIGEYH
     LNRLHVGKLI DQCEYGNLEC TGNCKYDYPS GIFVCTCKLG EILHHDGKTC VDDSDLSNVE
     MDDVMPQSTT EPIDDFQGRS RDPGAINFEP RHPNTWKNTD FKTGSTETDT STAKSKTKYV
     NPEQSDISIE QQTEFTPTTK HSVFENDDSH WNHEYVHHSK ETTIEAGPPI KVSQESSAKL
     EPTSEPEPTI EPEFSAEPEP NAEPEPNAEP EPSAEPEPSA EPEPSAEPEP SAEPEPTAEP
     EPSAEPEPTA EPEPSAEPEP TAEPEPSAEP EPTAEPEPSA EPEPTAEPEP SAEPEPTAEP
     EPSAEPEPTA EPEPSAEPEP TAEPEPTAEP EPTAEPEPSA EPEPTAEPEP TISPEITVTP
     ELTVKPEPEP TPILSAAVPN PASELEPTAK PEIAPEIEFT IEAESITERE STAKLIPVTE
     SATTINETDS EVKSKTESQH LTTEPYLKSK TDISDQPEFS VKPISHDDTS ESSTQTSPSD
     DAGTTNVFKS LIELTDKNDY SKNNETPITT VKSNENPTDN DTPLQIIPLT SKDINDNVNT
     KTTTIQSYGK NEITESTIIE AGLTTLDYRD LKQNGDVNVI ATKSENHAES VTEQFTQNPN
     LQEDKENDST TKTNFDTNLS NIQNDSSAAS GHDLITKQKS DIDLNVFEQV SLTTAATTVP
     VTSVEEKTES TTKFINNDRH SSTGHIHTIE INGVNNRNPE TNNYTKVHET TTIPETTPIN
     IFTQPILGYR EELVPEPALQ PNTPDSNEKN VIEHMPTTIF PKVPENFAHN VEPLREPIMK
     SADDEHIMLI PKSEQPVEIH AIIPELIPEQ ATNKSLKAEN STTKENKSVE GTISIDSSTI
     HTNENIVLAS NNKHAVRPDE IQEHLTSHPL HPAVFPENSV DHFTGKSDDR PAEDMSPFLP
     DVHKEKESLK KPRLDKDEQD GPNPFETHID DVITHRPLTR NNADRVNETE TKDLLIDVNS
     KNNEEKVDII KKITQNHEIN TTNDVDNSTN TNNTESKILN ALHQTNTAKS VDNDGTKGIT
     DQENGGFSED KELKVIPLAV ENKSVDSISQ TTLQPIDKKT EPEVVTSAGK KVQEIEGITI
     ESGVTSSEKP EENAVEDHYN DITDEALSKG YQHDNTGIPI KVIESSKKAV LKNIDPIKIS
     YDPYSSITTF DVIKKKNGTN EKISSDTTQS SMVTKTDEAV NNQMEDGRLT TQEPVLPIEI
     QQEMSTTTDK VEITTVINNG KHEENNTESP NVGQSDEKET VTTQITTTQA TLETKTTAQI
     PILPEELQTT ESDILSTTLS EEVPSVDKKT ETADKTVSTD DANNATKKNE AEKESAVTPS
     NVMDTSERSM AATTVYESNV SLGTGRKIEY DKNGQIIESA TESIKIETTP MISTIEKDIA
     DGVEGTSPMP NDITTTEDVR PVTEMLDDTE PMIDYRILFT TVPPRPILLD PELSEEALRV
     IPLEKSQESK KKPIDKKGFD KHKYKKEKDL SLEDQNEDNV LTERFDQTIL SQTEPSTITT
     ADREELHDSV VSSDIYPNVP RFTVADKEGN IVPISKWKDT AARTENKDVI AETKPKNYPS
     FIPVSEEIIE SVPVTEPYVI MRNYTRPMII INDAEKTAAN ETTVEGQTNV RANETTGQNA
     TFFSDQVFSD HEEAKVDHVT EESTTQTSTL KVESENTTAS SPSEFPFPGS LVKCSTSQFQ
     CVNGTSRNGA YCVPQSAKCD SENDCSDGSD EWNCTAEGCS SNFRCANGHC LKRHLVCNKI
     VDCDDGSDEH NCENWQCQSD EFRCPNGRCI PGLWQCDGRP DCEGHQDEYN CAETCGNNEY
     LCPTEKWCIP QVWHCNGVAD CVNGEDEKLC DCALDQFKCQ TGGCIPRNQI CDGIENCPDY
     SDEWSCLITN ITTDRNLTNA ETDSNTASEA NRVPFLKIRQ YNGDYQLVCS DGWSEEFSDS
     YCQALGFAGS DETLESFAWD RSQKILRLKT NPNYRLPLVT NLEEVGFCVS DKVMQVSCQE
     FTCGLHYTEE STARLTDPPE RWSSTALLKK SEDGTVCTAS IIGPVHALTS YSCIYSRHKE
     KSGWQLFTNG IMLKGNTVKN IIPYPRVKYN QFLYNNDIAL IELGEPLVFS RNISAICLPR
     QPIQPEQICV TVGWAFPRNG EINLQQYLKF MPRPLNNSDK CNATSHYAGF ITKHDICMDK
     NPCYNDEGTP LMCASESQGA PGRWEIQGLL SHRRECLGSH PAIYSSLEPA LPWLRETVPA
     LQTQS
//
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