ID A0A2G5SST3_9PELO Unreviewed; 1381 AA.
AC A0A2G5SST3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 22-FEB-2023, entry version 13.
DE RecName: Full=SSD domain-containing protein {ECO:0000259|PROSITE:PS50156};
GN Name=Cni-ncr-1 {ECO:0000313|EMBL:PIC18097.1};
GN Synonyms=Cnig_chr_X.g24114 {ECO:0000313|EMBL:PIC18097.1};
GN ORFNames=B9Z55_024114 {ECO:0000313|EMBL:PIC18097.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC18097.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesterol(in) = cholesterol(out); Xref=Rhea:RHEA:39747,
CC ChEBI:CHEBI:16113; Evidence={ECO:0000256|ARBA:ARBA00034049};
CC -!- SIMILARITY: Belongs to the patched family.
CC {ECO:0000256|ARBA:ARBA00005585}.
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:PIC18097.1}.
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DR EMBL; PDUG01000006; PIC18097.1; -; Genomic_DNA.
DR STRING; 1611254.A0A2G5SST3; -.
DR Proteomes; UP000230233; Chromosome x.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030301; P:cholesterol transport; IEA:UniProt.
DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR InterPro; IPR032190; NPC1_N.
DR InterPro; IPR003392; Ptc/Disp.
DR InterPro; IPR000731; SSD.
DR PANTHER; PTHR45727; NPC INTRACELLULAR CHOLESTEROL TRANSPORTER 1; 1.
DR PANTHER; PTHR45727:SF1; NPC INTRACELLULAR CHOLESTEROL TRANSPORTER 1 HOMOLOG 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 Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000230233};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1381
FT /note="SSD domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013895800"
FT TRANSMEM 282..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 626..649
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 661..684
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 696..715
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 736..761
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 773..798
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 851..870
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1124..1147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1154..1175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1227..1248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1254..1280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 625..798
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
SQ SEQUENCE 1381 AA; 155346 MW; 4C07B843C598D42A CRC64;
MNILLIFCLL FGSIFHHGHA GCIMRGLCQK HTDDAYGPCV TNDTNVEPIL FDKEHPAYEK
MMEFCPHMMK GDNKLCCTPS QAEGLTKQIA QARHILGRCP SCFDNFAKLW CEFTCSPNQQ
DFVSISEMKP IEKKEGFESE YQPADAYVNT VEYRLSTEFA EGMFASCKDV TFGGQPALRV
MCTSTPCTLH NWLDFIGTQN LDLSIPINTK FILYDPAKTP QSDRSIFMNV NFTGCDQSAR
PGWPACSKSE CNKEEYAKMI NLDDGKTSGQ SCNVHGIACL NIFVMLAFIG SLAVLLCVGF
VFTSYDEEYT NLRQNQAGQE SPKRNRIRRT GAWIHNFMEN NARDIGMMAG RNPKSHFFIG
CAVLIFCLPG MIYHQESTNV VDMWSSPRSR ARQEETVFNA NFGRPQRYQQ IMLLSNREFQ
TNGKLYGPVF HKDIFEELFD ILNAIKNIST KDAEGRTVTL DDVCYRPMGP GYDCLIMSPT
NYFQGAKKNL ELKKEEIASD EDDAFDYFSS EGTTDEWMNH IAACIDQPMS QKTKSGLSCF
GTYGGPSAPN MVFGRNTTNY QAANSVMMTF LVTQRTEPEI QRAELWEKEF IQFCKDYREK
SPKVTFSFMA ERSIPDEIEK DAKDEIVTVV IALAFLIGYV TFSLGRYFVC ENQLWSILVH
SRICLGMLSV IINLLSSFCS WGIFSMFGIH PVKNALVVQF FVVTLLGVCR TFMVVKYYAQ
HRVSMPYMSP DQCPEIVGMV MAGTMPAMFS SSLGCAFSFF IGGFTDLPAI RTFCLYAGLA
VLIDVVLHCT IFLALFVWDT QRELNGRPEF FLPFKIKDLL GAYLVGRQRA TDTFMSQFFH
YSFAPFLMHR ITRIVTGVIF VASFIATIIL SSKISVGFDQ SMAFTEKSYI STHFRYIDKY
FDVGPPVFFT VDGELDWHKP EVQNKFCTLP GCNDTSFGNI MNYAVEHTDQ TFLSGEMYNW
IDSYLEWINR KSPCCKVYVH DPNTFCSTNR NKTALDDKAC RSCMDYDDIA NSYPKNHIMY
QRPSTEVFYK HLRHFLEDTP NMECAFGGRA SFKDAISFTS RGRIQASQFM TFHKKLSMSN
SSDFIKAMEN ARMVSRRLER SIDDTAHVFA YSKIFPFYEQ YSTIMPILTT QLFITVVGVF
GIICVTLGID VKGAACAVIC QVSNYFHIVA FMYLANIPVN ALSATNLVMS SGILIEFSVN
VLKGYACSLR PRAKDRAEST VGSIGPIILS GPVVTMTGST LFLSGAHLQI ITVYFFLLFL
ITIVSSAVHA LIILPILLAF GGSRGHGSSE ASTNGDDEPV EVGMMSGTGE SHAMEEGIPN
RPTLLNTTHL LDPLLKSETN EIDLKAIDII TIDRSYPSTP SSLPCTSRLP RAHIEPDLRS
L
//
