ID A0A0V1KQC5_9BILA Unreviewed; 1330 AA.
AC A0A0V1KQC5;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Niemann-Pick C1 protein {ECO:0000313|EMBL:KRZ49234.1};
GN Name=NPC1 {ECO:0000313|EMBL:KRZ49234.1};
GN ORFNames=T02_16030 {ECO:0000313|EMBL:KRZ49234.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ49234.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ49234.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ49234.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) 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 -!- 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}.
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:KRZ49234.1}.
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DR EMBL; JYDW01000325; KRZ49234.1; -; Genomic_DNA.
DR Proteomes; UP000054721; 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; 2.
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:UP000054721};
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..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1330
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006881190"
FT TRANSMEM 283..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 370..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 639..657
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 677..700
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 706..728
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 784..806
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1121..1140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1147..1168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1174..1195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1216..1239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1251..1274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 638..807
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
SQ SEQUENCE 1330 AA; 149125 MW; 0ABBCC2B79E7209A CRC64;
MNFLMKMLFC RCGLFLTALL VVRFQSAEAE NDGHCVWYKV CSDKDAEFKK NCLYNGTPQP
LLDKKAINTV ISLCPDLVGD DENPVLCCDA EQVEILDKSV STVLPYFSRC PSCSRNFLQM
WCQSTCSPKQ SLFMEVTDTV NETRGISVSG VHYLMKEEFA TGIFSSCRNV LDPSTNQRAM
NIMCGGLMDD ECTVAEWLDF LGNPSKNPMA PFEIVFERYK QASVNISGKI MYPLNATVFS
CAQATDNNTT PCSCQDCPTV CSEMIPYPSY EKKRCFIGHM DCLVFVALLT CCSVTVVIVC
IAVVHHVLLE KEAVKSSSLN DKMPIGVSCG QQALLNADDV SSCAKIGAWL ENKIEDKFHR
WGVFCTRHPC LVFFFGITVS LICTSGLCYM QVTTDPVQIW SAPGSRARLE KDYFDRVFDP
FYRIEQLIIV PRNQAQFVAA DPLDNVEFHW GPVFRKEFLH EILQLQKQIE NLTVQVENKP
VTLKDICVQP LAPEKTECLI QSVVSYFQSN ATNLDDEYYE EGFLLSNWLS HLRSCLRNPI
QVMDTTMFKM SCLGEYGGPI FPYVALGGFE GSDYISSKAA IVTILVNNYD DPKANEKAQA
WEKIFINFIK NYKSDNLSIS FKAERSIEDE IERESRSDVS TILISYCVMF VYIVLALGQY
DIRGYNFLHL LVQSKILLGL LGVMIVMLSV VSSLGFFAYV GIPTTLISIE VVPFLVLAVG
VDNIFILVQA FQRGHGKGNE DVEEQIGRIT AEVVPTMLLS SFSESFCFFL GALSSMPAVK
VFSLYAALAI FFDFFLQITC FLALFTTDVR RQRSGRLEIC CCVRVEPSDD VSDGFLHSII
RQYYSPCLLW KPMRVLMLVI FSAWFFSSVA VIDKIELGLD EKLSMPEDSY MLNYFKSMNQ
YLAVGPPVYF VLKGDFNYAD VGMQNQICGS AGCNENSLYG QLFRAATYSN RSYIAAPVTS
WLDDYFDWLR PLGSPPCCRL FSENRTFCPA TFETAEPEVC HSCVSSYTNG RPAPDAFSTF
LPLFLFDNPT VSCSKGGHAA YAKSVRLNGS RVVSSNFMTY HTVLRTSDDF IQALRNSRAI
AANITKAINK NIHNSSNRIE VFPYSVYYVF YEQYLTLVWD ATMQLIFSIA SIFFVSALLL
GLDFWSAFAI CLTISMIVIN LMGLMYWWKI SFNAVSLVNL VMAVGISVEF CAHITRAFST
SIRLTRVERA KEALENVGYS VLSGITLTKF GGIVVLAFSH SQIFQVFYFR MYLGIVLFGA
AHGLIFLPVF LSFAGPPLNK LKIHQKQCQD MFGVRKGGHH AIGNSSLASS SGSFGQDFVS
SVNAHPFLQN
//