ID A0A232FMC4_9HYME Unreviewed; 2070 AA.
AC A0A232FMC4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
GN ORFNames=TSAR_000711 {ECO:0000313|EMBL:OXU31670.1};
OS Trichomalopsis sarcophagae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU31670.1, ECO:0000313|Proteomes:UP000215335};
RN [1] {ECO:0000313|EMBL:OXU31670.1, ECO:0000313|Proteomes:UP000215335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alberta {ECO:0000313|EMBL:OXU31670.1,
RC ECO:0000313|Proteomes:UP000215335};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXU31670.1};
RX PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL Curr. Biol. 27:2007-2013(2017).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OXU31670.1}.
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DR EMBL; NNAY01000039; OXU31670.1; -; Genomic_DNA.
DR STRING; 543379.A0A232FMC4; -.
DR Proteomes; UP000215335; 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; 3.
DR CDD; cd00112; LDLa; 9.
DR Gene3D; 2.10.70.80; -; 1.
DR Gene3D; 3.30.60.270; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 4.
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; 2.
DR Pfam; PF00057; Ldl_recept_a; 9.
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; 3.
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; 4.
DR PROSITE; PS01209; LDLRA_1; 3.
DR PROSITE; PS50068; LDLRA_2; 9.
DR PROSITE; PS51120; LDLRB; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000215335};
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 1973..1996
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 826..870
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 871..915
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 1425..1521
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1525..1615
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1620..1707
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1712..1804
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DISULFID 1018..1030
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1025..1043
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1037..1052
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1057..1069
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1064..1082
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1076..1091
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1096..1108
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1103..1121
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1115..1130
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1159..1174
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1202..1217
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1237..1249
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1244..1262
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1256..1271
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1293..1305
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1300..1318
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1312..1327
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1354..1369
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1382..1394
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1389..1407
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1401..1416
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 2070 AA; 233082 MW; 88AF224F73071F21 CRC64;
MVLVNALNDS HQQLMVHWVG EGSDVIICLA RDSNPLPRFF QTVQPAVAVN PSAVYISYDY
GDTFQNKTDS FRVSDEPDAK YATLDKFYNH PTHNNLCVFA DSANKLIFIT HNHGHDIERI
KLDFSPSEIA FYDNQEYDAS ALVLLVLDKT TSMRKLYMTT NRGKTWNLVH EYVKAFFWTN
SRPKNLLIER TEPSGQNNVI DLGHNAWKWS KRNYTEVISN VEDFQIRGDY MFATKKPANN
NTQGLDLFVS YKSQPFVPAQ FDTDPGRREY HVADVSYDRI FVAVSHTETL VNLYISEIID
HRAAKFILSL PNILTFFPNN TWKDSWLSDV ADEAFTELYK VEGLRGIYIA SQVQGTPKLN
SIGPEHLLSL ISYDHGVTWN KVKAPESNHK GLYNQCNPET CSLHLSQKFS QLYPVSRAAS
IMSSKSAPGI IMATGVIGTS LKGHPALYVS RDAGLTWKQV LQDYYFFNMG DHGGVLVAVK
YFKTRGETRD ISYSIDEGET WQTLEFNEKM LRVYGLMTEP GENTTVFTMF GSGSGQHQWL
IIKVDLSKVF ARNCTDDDFK FWSPAAPKEI SSTCVLGRKE TYKRRSARAN CYTGQNFDRP
VKTEICPCDA VDYQCDFGFI RQSKPQWPSY TCVRNKSLEN YDPYAVPATC APGKFYNRTK
GYFKIPDDDC VGGRAKVFEP DEIPCPMLEL PEFLLVAQRE RISRIDLKEQ KLEVLPVHDL
KNVIAIEFDI KNNCLYWADI VNDTIGRQCF KSGKSAPEIL VETDLSSIEG MALDWVSNVL
YFVDGVRMRI QIIRTDMSSM GRMRRTILGP NNVQKPRGIA VHPMAGYMFW TDWAPGNASV
NRANLDGTNV KQLFHNRVEW PNGITIDHIA ERIYWVDARQ DYIGSSDFEG NGFKKIIHND
ERVSHPFAVA VFKDNMYWDD WKQSMIFVAD KDHGFGVSTI IGQLAGLMDL KVFAHSVQSG
TNKCANNTLC SHICLGAPND GYVCLCPDGM VMQDGKCMCP GGVTPYANST CPRVANSCAA
NQFACDSGVC IPEFWKCDGD NDCGDHSDEN YCNKVKCQPN TFTCDGEKCI PRYWVCDLDR
DCKDGKDEMN CTYSNCTDSQ FRCDNGRCIS HRWLCDGEDD CRDGSDEKNC STSIPPSTCK
SDEISCKSDN NCVPKTWKCD GETDCEDASD EDDCTSVECE VWQFDCNASD KSHRCIYKSW
VCDGDTDCQN GSDEANCTSS ESHSPTPTPS LLPTNSCSEW MFMCQNKKCV PYWWKCDSVD
DCGDDSDEMG CGFPDTSNSG TTAATTDEHP HVCREFQFQC FNGECIETSW MCDGSKDCSS
GEDELYCSNG PIGCKEDQFK CFVDGSCVPL INICNGIQEC PDGSDERGCD HHRPSPPPTT
SCHTGFFPCD ETRCFPLSAY CNGKQDCYDG FDESNCEKNN TRVYQVLNIG VDERSTNATT
LFLYWWMPIP SNITFEFMPS IALAEPGAKW TNASRWVEDT EYQFNNLEPY TRYNMTVYVK
LKGLPTIFPP ARYLIVTTGE GVPSPPWNVT AVQRNGTRIE VTWQPPIHPN GQITGYRVYM
TPPIPPAPVY PQQKTTVIID DAFEAGKNYS FWVVAKNKEH ESESSNVATI TFDGSANIDH
IEDLKVIDKT NHSITLNWKK IDSADGYNIT PRGPPSYPLL DTYSTKSNTY VVDGLAPGTR
YTFEVTATKK KYVGKASSIT GMTKDQPLPT VTILEPHLLK SHGTTVKLSW DPPKGTRKVK
WQYAVHYALN MQDVYKAPKL ITTNLTATIR DLEACEYYIF AVGVKGDYGA GSLSQPVTVA
THFNAKAPPK RLRITVTEMT LNKTKVFTLA ATNETVLKHP FRDIKYGGRY NISISTDVEG
AIPSPWVIYN APPILPPHQL TVRFAEGNYE IYWQERQLPE SIAKTTKYHY EVLVNEGERT
INESTAAIFK TNQPPYIYQN AKLDKIYAFA VRLVTEEGYR NLSWTPPMNA SSILSLAIPI
CLLVIALGAA LAYFVIRHRR LSNSFTQFAN SHYDTRRGQA TFPGTVDAGL AEEEDSPVIR
GFSDDEPLVI AVLSYQNTKK NEKNDNNNNY
//
