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Database: UniProt
Entry: T1K437_TETUR
LinkDB: T1K437_TETUR
Original site: T1K437_TETUR 
ID   T1K437_TETUR            Unreviewed;      1323 AA.
AC   T1K437;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=SSD domain-containing protein {ECO:0000259|PROSITE:PS50156};
GN   Name=107360306 {ECO:0000313|EnsemblMetazoa:tetur05g01210.1};
OS   Tetranychus urticae (Two-spotted spider mite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Trombidiformes; Prostigmata; Eleutherengona; Raphignathae;
OC   Tetranychoidea; Tetranychidae; Tetranychus.
OX   NCBI_TaxID=32264 {ECO:0000313|EnsemblMetazoa:tetur05g01210.1, ECO:0000313|Proteomes:UP000015104};
RN   [1] {ECO:0000313|Proteomes:UP000015104}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=London {ECO:0000313|Proteomes:UP000015104};
RA   Rombauts S.;
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:tetur05g01210.1}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cholesterol(in) = cholesterol(out); Xref=Rhea:RHEA:39747,
CC         ChEBI:CHEBI:16113; Evidence={ECO:0000256|ARBA:ARBA00034049};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the patched family.
CC       {ECO:0000256|ARBA:ARBA00005585}.
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DR   EMBL; CAEY01001565; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_015782415.1; XM_015926929.1.
DR   EnsemblMetazoa; tetur05g01210.1; tetur05g01210.1; tetur05g01210.
DR   GeneID; 107360306; -.
DR   eggNOG; KOG1933; Eukaryota.
DR   HOGENOM; CLU_002359_0_0_1; -.
DR   OMA; NIFIMVH; -.
DR   OrthoDB; 2786103at2759; -.
DR   Proteomes; UP000015104; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005319; F:lipid transporter activity; IEA:InterPro.
DR   GO; GO:0030301; P:cholesterol transport; IEA:UniProt.
DR   Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR   InterPro; IPR004765; NPC1-like.
DR   InterPro; IPR032190; NPC1_N.
DR   InterPro; IPR003392; Ptc/Disp.
DR   InterPro; IPR000731; SSD.
DR   NCBIfam; TIGR00917; 2A060601; 1.
DR   PANTHER; PTHR45727; NPC INTRACELLULAR CHOLESTEROL TRANSPORTER 1; 1.
DR   PANTHER; PTHR45727:SF2; NPC INTRACELLULAR CHOLESTEROL TRANSPORTER 1; 1.
DR   Pfam; PF16414; NPC1_N; 1.
DR   Pfam; PF02460; Patched; 1.
DR   SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR   PROSITE; PS50156; SSD; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015104};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..1323
FT                   /note="SSD domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004591208"
FT   TRANSMEM        306..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        395..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        652..671
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        683..709
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        715..737
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        758..780
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        792..816
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        867..884
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1129..1146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1153..1172
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1178..1199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1220..1242
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1254..1277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          651..816
FT                   /note="SSD"
FT                   /evidence="ECO:0000259|PROSITE:PS50156"
FT   REGION          1294..1323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1294..1308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1309..1323
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1323 AA;  147993 MW;  DA39D410A887D94F CRC64;
     MDSKITITSI LVTLILKIVT GESSLTQPTT SPLQAQALPS SPEAKCVLGG ICGHGGTFQS
     PIPCYEPHTP QPIANETYRA TLKELCPNLF LNNDNPPVCC SLEQIDALEK SYEAPNQFLG
     RCPSCFYNWK QIFCEMTCSS RQSQFINITK VVPLESSPEK LQVQNTTYFM SETFAKGLHQ
     SCKSVQTPLN LPALTIMCGI TDDGECTYRK WLNFMGLSHR SGGHSPVQIN FTFTQETQIT
     TNDGLKFYPM SAQPIPCHKS IGLGFDPCSC SDCEQTCAID VLPRSARKLP PPPEPFTFFG
     HPAAAIIGYL LFALIFSTSS VYFINLFLKK NKSLSHDFIG PIAAATPPAS PSREVASISS
     DGKSTEEKLS LGLQFELFFE KWFTRWGIYV ADHPIPIMVI SLVASIILAC GLATIKVTTD
     PVDLWVSAGS QARQDMEYFQ SNFFKFHRIE QIIATPTDNS YFRANYTSNG KVKSDRFGPA
     FRRQFLKDVL ALQKEIENMQ VTNGDHTVSL KDVCYKPLGS TCATQSVFTY FHDDPNEIDD
     ENYLHKVVSC PSNPTILSDD KFLCMKNGSI PLIYPEATLG GFNNNTYREA QALIIIFPIL
     NFPDPKQNSD AIAWEQGFLD LVKNYSNPNV KIAFKAEKSI EDEIDRQSQS DVVTIGVSYL
     IMFVYILLAL GENSNINTLL IDARFTLGFV GVLIVLLSVM SSLGFFFYLG IPATLIIVEV
     IPFLVLAVGV DNIFILVQTF QRDERRPDET INQQIGRVVG EIAPSMLLSS LSMSSCFFIG
     ALTPMPAVRI FALYAAVALV INFILQMTCF LSIFVLDTRR QASNRLDVFC CIKTKKSTKS
     SNLNNGMLYG FFRDIYSPFL LKDVTRFIVL IIFGGWFCAS IVSLDQIHIG LEQEVSMPDD
     SYMMDYFAFY KSYFQVGPPV YFMITDGYNY SDPVAQNRLC GESTCDKDSV LKILNYFSTK
     TSESYLASRP SFWLSDYNQY LRSDTCCKKY ENGSQCLTNE LECETCLDDM RIRPMGKEFD
     QYLPFFLNQN PGEECLSGGK ALFSGSVKLV KDSKGDLRAG PTFLMAYRKS LKTSKDFYES
     LRISRQIADK LTKKLQKSGL TKATVRTYSF TDVFYEQYLT MWSDTARSLS LSIGAVFIVT
     YLFFGLDFYS ASIVAFTIIM IIVNLMGMMH WWDISLNAIS LVNLVVGVGI SVEFCSHLVR
     TYTISPAATR MQRAHEALST MGSSILSGIT LTDCGILVLA FAKSKIFQIF YFRMYLGIIL
     LGTLHSLIFL PVLLSIIGPP LNEQRLTLMA NKSKSSSSFQ VASELSSSKY RENDSKKEQN
     EKC
//
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