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Database: UniProt
Entry: E1ZV38_CAMFO
LinkDB: E1ZV38_CAMFO
Original site: E1ZV38_CAMFO 
ID   E1ZV38_CAMFO            Unreviewed;      2187 AA.
AC   E1ZV38;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Sortilin-related receptor {ECO:0000313|EMBL:EFN74947.1};
GN   ORFNames=EAG_04005 {ECO:0000313|EMBL:EFN74947.1};
OS   Camponotus floridanus (Florida carpenter ant).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Formicinae; Camponotus.
OX   NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN   [1] {ECO:0000313|EMBL:EFN74947.1, ECO:0000313|Proteomes:UP000000311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX   PubMed=20798317; DOI=10.1126/science.1192428;
RA   Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA   Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA   Wang J., Liebig J.;
RT   "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT   saltator.";
RL   Science 329:1068-1071(2010).
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; GL434403; EFN74947.1; -; Genomic_DNA.
DR   STRING; 104421.E1ZV38; -.
DR   EnsemblMetazoa; XM_025406280.1; XP_025262065.1; LOC105257277.
DR   InParanoid; E1ZV38; -.
DR   OMA; YLCPTEK; -.
DR   Proteomes; UP000000311; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd00112; LDLa; 5.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 5.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   PANTHER; PTHR24270:SF61; CD320 ANTIGEN; 1.
DR   PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR   Pfam; PF00057; Ldl_recept_a; 5.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00192; LDLa; 5.
DR   SUPFAM; SSF57424; LDL receptor-like module; 5.
DR   PROSITE; PS01209; LDLRA_1; 2.
DR   PROSITE; PS50068; LDLRA_2; 5.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; Membrane {ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000313|EMBL:EFN74947.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000311};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        194..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          821..849
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1236..1261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1458..1486
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1864..1891
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        821..843
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1240..1254
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1460..1486
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1869..1886
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        1978..1993
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2002..2020
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2014..2029
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2034..2046
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2041..2059
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2053..2068
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2092..2107
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2109..2121
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2116..2134
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2128..2143
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   2187 AA;  245660 MW;  D26DBDBDDEE50D6C CRC64;
     MSDAAGTDNP AFASEDECGS KAENGGQQRE VTLDQDRKSS PADCAPLENG QRSFISQHYV
     EPIKANSEPC FKTETRIELP AENTDKNVSE PKLNGVHGNG NNNDASFLNN STTSVQVNES
     GKKEQIEAVN LELVSMRPYT GNNIQTKGQE ACEVPADPYE EYFVPVNEHR KYIRGEKLYV
     TKDKRSKNSY WKQLLCGFTI LGVVIAMIII VLAATGVIFT QDPTENVEES TRQFDINIAE
     NKEYVKDPPL SPPPLTSTFP PWPTTDETLY QIIPDALNGI LRLDDFNWSD DLSDPKSRVY
     RETTAEIEEH LGNILHRENS KSIIKVYNIS NEGEIKFRIS HPPMDTPAEN QEYIEKALRK
     NSNMIGQYHL SRLQVVRLID QCEHGNLQCV ESCKYDYSKG IFMCTCSPEK MLDQDGKSCV
     DNDLSNVEMD DIIPQSSTES IHDFVQGRSR DPNTAEFEIR HSNTWENPDL KTGLAGTETS
     TLESRIEHDH QLDQKSIIYQ SESTPTTKRI FENDYFNWSH EHSHHSMDTI FEEPAVEPKS
     TAEPEPIAEP ESAAEPEPAA EPEPSAEPEP SAEPEPSAEA EPTAQPEPTA EPKPTVELTA
     EPEPATEAEP TVKLIVPPEF KPTEPVSESI SEFSTKPEIV PKIESVTESI TEKETTTEPV
     SIIESTATTI DEADDVTSKT ELHYLMSTES HLESNTEISN QSGSIIKSVL DDANTTDISK
     SFTDLLRENN NSKIDESSIT TIKTSENPID DDIYKVIPLT LTKLNNNKSI DTNDNVEIKT
     ELTTMQSYTN KDDKINESTT IEASFTTLSY EDLKQDSDII SNQSRNENSN TEQFTQNPGL
     QEEKENESTT EINLNVNLSD GSTIIKEFDS TTMSIISIEN RTESITRTTV NDKYFHTIEI
     NDVGNRNQEM YNNSKVHETT MIPETTSTDM STQSISNYSK GHVPEITLQS NTQDSNEKNV
     IEHMPTTIFP KVPKNFVHNV EPLKEPIAKP PKDEYIMLIS KSEQPVEIHA IIPQLTPEQS
     VQFTPNESLK TENSTEINNG VVINEELNAK KPEEDIFSID SSTVRNDKNI VYTNNNEYIH
     SDEVQHSTNH PLHPEILPEN SVNFAGKSDV NDDRHVEDMS PFLPDIHKEK ENARKAPRLD
     KDEQDVPNPF ETHIDDVITH RPLIHINADD IKRKLNETET KDLLNDVNLH SVNNEEKLDI
     TEETVKTINT TDDVKNIIKN DLNMSEIINN TNILHQDNNF SKSDKNEQDI SSPDIDDVTK
     NATNQKQSNF SIMEENDNKT LKVIPLRIED KVVDSILQTA MQSADNKTSE SAKVNTITEK
     KVKDLSLIES GTTSLEKPEE NAVEDQYNDI TDESLSKGYR HDNIDKDIPI KVMEESKEAI
     LNNVDDSIKT SYNRVPLLIT PGNVKERNET ITQSLLNTTI KGASERQIED ARLTTQEPVL
     PIEIQQEMST TIATDKTEIT TVLDNDKREE NNTEQPNTDR PDEKEVDKIT QITTTQSTLE
     TKTTAQIPIL PEELQTTEND ILTTTSISEE KEMNQEVIDK TKSQISTENV KDETKKNITD
     EKENVTSVET DIDINNTSSE KSMTATTMYE NNITVGSDRE IDDENINDPN RTMENSTENV
     KIETTLIFTT EKSVISSTDR TSSDVTTTED VRPVTEMLDD TQPETEFNYR MLFITTPKSI
     SIDPELSEES LKVIPLEKSQ ESKKKVIDKK GFDKYKYKKE KDLSLEEQSE NNALTEKSSS
     TILSQTDSSK IITKNYGQSN DSIASSDLDP SVLRFGVFEK EDNESKKVSP ILLKDSGNVD
     EGSDIEDKGV ITKPKNYPSF IPVSEEIIES IPVTEPYIVM RNYTRPTIVP SSFETEESTA
     MNETAIEGRT NDPETDLSRT HLRPDETTGE PVTFFSDQLF GDAEEIDRVT KEPSTIRLIV
     GPTTPFDMDV ENTTIIASTS FSGSMPTTIL SKCITSQFQC ANGTSRNGAY CIPLSAKCDS
     KNDCSDGSDE LNCEDCSGNF RCGSGECLKK HFVCNNIVDC DDGSDERDCE NSKCQSDEFR
     CSNGKCIPAS WVCDGRSHCE DHRDEYNCTE NCQDNQYLCP TEKLCIPQTW RCNGIDDCKG
     GEDEKLCDCD PDQFKCQTGG CVSSSEICDG VKNCPDYSDE WGCLINITTE TNINIENMAN
     ETSDGVSLLK IRYIYIKCMN INRLFFF
//
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