ID A0A182WFZ0_9DIPT Unreviewed; 2074 AA.
AC A0A182WFZ0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Sortilin-related receptor {ECO:0000256|ARBA:ARBA00013467};
DE AltName: Full=Low-density lipoprotein receptor relative with 11 ligand-binding repeats {ECO:0000256|ARBA:ARBA00029896};
DE AltName: Full=Sorting protein-related receptor containing LDLR class A repeats {ECO:0000256|ARBA:ARBA00032450};
OS Anopheles minimus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=112268 {ECO:0000313|EnsemblMetazoa:AMIN009288-PA, ECO:0000313|Proteomes:UP000075920};
RN [1] {ECO:0000313|Proteomes:UP000075920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MINIMUS1 {ECO:0000313|Proteomes:UP000075920};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., 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 minimus MINIMUS1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMIN009288-PA}
RP IDENTIFICATION.
RC STRAIN=MINIMUS1 {ECO:0000313|EnsemblMetazoa:AMIN009288-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004212}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004212}. Early endosome membrane
CC {ECO:0000256|ARBA:ARBA00004158}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004158}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004115}. Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004530}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004530}. Endosome, multivesicular body membrane
CC {ECO:0000256|ARBA:ARBA00004545}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004545}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004614}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004614}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000256|ARBA:ARBA00004393}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004393}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Recycling endosome membrane
CC {ECO:0000256|ARBA:ARBA00004480}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004480}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the VPS10-related sortilin family. SORL1
CC subfamily. {ECO:0000256|ARBA:ARBA00007041}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR STRING; 112268.A0A182WFZ0; -.
DR EnsemblMetazoa; AMIN009288-RA; AMIN009288-PA; AMIN009288.
DR VEuPathDB; VectorBase:AMIN009288; -.
DR OrthoDB; 5840at2759; -.
DR Proteomes; UP000075920; Unassembled WGS sequence.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007034; P:vacuolar transport; IEA:UniProt.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00112; LDLa; 9.
DR CDD; cd15482; Sialidase_non-viral; 1.
DR Gene3D; 2.10.70.80; -; 1.
DR Gene3D; 3.30.60.270; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 9.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR031777; Sortilin_C.
DR InterPro; IPR031778; Sortilin_N.
DR InterPro; IPR006581; VPS10.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR12106; SORTILIN RELATED; 1.
DR PANTHER; PTHR12106:SF27; VPS10 HOMOLOG 1-RELATED; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00057; Ldl_recept_a; 8.
DR Pfam; PF00058; Ldl_recept_b; 2.
DR Pfam; PF15902; Sortilin-Vps10; 1.
DR Pfam; PF15901; Sortilin_C; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00060; FN3; 5.
DR SMART; SM00192; LDLa; 9.
DR SMART; SM00135; LY; 5.
DR SMART; SM00602; VPS10; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF57424; LDL receptor-like module; 9.
DR SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 1.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS01209; LDLRA_1; 6.
DR PROSITE; PS50068; LDLRA_2; 9.
DR PROSITE; PS51120; LDLRB; 3.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 2000..2020
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 697..740
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 798..843
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 844..888
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 1417..1510
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1514..1609
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1614..1704
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DISULFID 990..1002
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 997..1015
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1009..1024
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1051..1066
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1071..1083
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1078..1096
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1090..1105
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1135..1150
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1175..1190
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1219..1231
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1226..1244
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1238..1253
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1284..1296
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1291..1309
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1303..1318
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1392..1407
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 2074 AA; 233776 MW; F0E082D9762CB32E CRC64;
MNTSITTTNL NDSHGQLIVH WLGEGTDVMI CLAREPPDTD MKSPPPPPSR IFMSNDYGDT
FEDKTAHFML NISGVLTNST VEQFFTHQKY NTIVFIDPRN QAIFTSEDYG ATITKQKLDF
TPSDVSFYDA DRRTFLVLDK RDPQRKLYYT TDFGASFTLL QSYVKSFLWS SGDGVPIHLY
VERKEPTNTS SVIFFNAADL YTGNRQFNVL IEKVEDFHIN KDFMFASQRL PNSTQLLISY
KRGKFVKADF QTELDIRGYH VADVEGRRIM ISVVHSERVS HLYVSESNDD MTDIKFVPSL
ENIFTFIPDL NWRSSWLVKS SETAFTDLYR VEGLKGIYIA SKINRMPVAE TITPDYLMSV
ITFDHGTTWR SIKAPETDDE GASVTIMSSK TAPGVIMASG VVGKSLKGHP GVYISRDAGL
TWKQILKNYY FFNMGDHGGI LVAVKYFKSK GETNEILYST DEGERWHSTP FIGNQLKVYG
LMREAEANGT IFTLFGSEQE EHRWLIIKLD LKNAFTSNCT EKDYKFWTPG SYSGDYFMPC
VLGRQDTYQR RRPHANCHNG LGYERPIRQE VCECNSWDFE CDYGFVRSGQ KRSFCVRNQT
MTQFDPYAVP KSCKPGAYYN RTRGYRKIEG DVCVDGFSSQ FLPQSIPCPV EQSDEFLIIA
QREKISRIDL RNNNTRSEFA IPGLKNVIAI EFDLKRNCVF WADILTDVIG RQCLNGNSTP
ETLVDNGLSS VEGMSYDWIS EVLYFVDGMR LMIEALRVPP PGTIPPAGSP RTPNVRRTIM
DSKYLNKPRG IVVHPMEGYL FWTDWNSIRP SISRANMDGT DVRELFTKPQ VAWPNGVTID
YMAERLYWVD ASKDYIASSD LDGKNFHKVM QQDPFVQHPF AVAVLKDLMY WDDWKQNSVF
SADKDHGIMA KLLADNMANL MDMKVYGHTI QVGTNACSKN DRCSHICVGG PKRTYSCLCP
DGMELEKDKC ICPAGTLPQG NGCARTGKTC GPKYFSCNNA RCIPQIYKCD GEDDCEDRSD
EEGCPAEKPV CPPHMFTCKL DQQCIPKHYV CDFDKDCKDG SDEENCAKQQ CMKGEFTCGN
GRCIKPGWLC DGEDDCRDGS DEKDCQKKNV TLVECRSDEF RCNATNTCLP NQWRCDTEQD
CPDGSDEAHC VNNTCESWMF TCANDGKCIY KTWQCDGAKD CADGSDELDC PSIIGDTGSP
KPEAPTKKPG INMMPGQECH DWMFKCKNER CVPYWWKCDG VNDCEDHSDE DGCSETAKPT
IGDGSTIVTH LSTPTPTRRK DRTCGLHEFR CDSGTCIPKR FVCDGYNDCT AGEDEANCPS
HKLCSNNNFR CRTDGMCLPM TRFCNGVQDC VDGSDEECSF KPTTSVTTNR NCSTNPGVFT
CDNTCFALML QCDGKPDCYD GTDEENCSGS RKGRHYQVTQ ISVDQRSLNS SSFLIFWWIM
LQTNVTYEYL PSIYYNNEWK NVTNWITDTS YRFTNLKPYT TYTVTTYVRA KGQSKITPPY
IYYEIATTEG IPTPPLSVSV IQQNGSRVLV SWDPPQEVNG RLEGYTVNFR SQSKNVTPVQ
NVKVSASETS VVIDKDFKPH VVYEFWVKAR NGKHESLSSV MVPLTFDGTS FVEKITRIEV
LNKTAKSVTL RWKPVTNADG YMVVPILPQT YPVLPTIKVQ NATVITLDNM VPGTQYVIKV
AAYVKNFFGQ HETTIVSFGG TPLPALNVEL KEKTNDYALL EWNEPKGLDT SKLVYAARIN
TTSRSIKLTG LMPCQSYLVS VGIVGPIGPG PLGRNPLKLE TAYNRTLPPK ELTVVINETS
QEMTIEWQHS CALDLGAYPS YIIKVRELTL NKTSLVTVQP SSNKTIVHVF REIPKGAAYE
ISVSTDIPNA QAVSMIAYSA PLPAPDQLQV WEERNGTFVV YWKAVKDFAD DGYSYEIIVH
EGKGINNSVP PNLTIPAKEP PAFIQPDQLT WMNYEGAFTV GVRLKTDQGL YSEIVETETF
IKHGPLLMGS PTMSAVRSSW KWIVPTIVVV VLIAVLAYGF QRHRRLQSSF SRFANSHYDT
RTGATRIGCT LDDDEHEHQE VPRSFSDDEP LVIA
//
