ID A0A091N4K7_9PASS Unreviewed; 1259 AA.
AC A0A091N4K7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Niemann-Pick C1 protein {ECO:0000313|EMBL:KFP84336.1};
DE Flags: Fragment;
GN ORFNames=N310_04300 {ECO:0000313|EMBL:KFP84336.1};
OS Acanthisitta chloris (rifleman).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC Acanthisitta.
OX NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP84336.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP84336.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP84336.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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}.
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DR EMBL; KK842053; KFP84336.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091N4K7; -.
DR Proteomes; UP000053537; 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:UP000053537};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 241..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 335..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 603..624
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 636..660
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 666..688
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 709..730
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 742..767
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 819..838
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1079..1098
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1105..1126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1132..1150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1171..1197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1209..1232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 602..767
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP84336.1"
FT NON_TER 1259
FT /evidence="ECO:0000313|EMBL:KFP84336.1"
SQ SEQUENCE 1259 AA; 140541 MW; A5EB974768CE3040 CRC64;
VLPQTCVWYG ECGVASGDKR YNCAYDGPPI ALPEDGYDLM QELCPGLFFG NVSTCCDVRQ
LQTLKSNLQL PLQFLSRCPS CFYNLINLFC ELTCSPNQSD FLNVTSTIPY YDPVLKENKS
SITELQYFIG ERFANAMYNA CKDVEAPSSN VKALGLLCGK DVKDCNATNW IEYMFSKDNG
QTPFSIIPVF SDVLVHGMNP MNNETKGCNE AVDDSTGPCS CQDCSIVCGP KPQPPPLPPP
WLLFGLDAVY VIMWISYMGF LLIFFALVFG VWCYRRRHFV SEYTPIDSNA AFSVNSHRDN
GKITCGERLG ERFENGLRMT FTSWGAFCVR NPRPVILFSV VFIAMCCSGF VYIKATTNPV
DLWSAPSSQA RKEKEYFDTH FGPFFRTEQV IIQAPKSSPH TYSPYPSGED VPFGPPLAID
ILHQVLDLQD AIVNITASVD NETVMLKDIC LAPLAPYNNN CTILSVLNYF QNSHSVLNHF
TGDEFYVYAD YHTHFLYCVR APASLNDTSL LHDPCLGTFG GPVFPWLVLG GYDDDNYNNA
TALVITFPVN NYYNDSRKLM KALAWEKEFI NFLKNYNNSN LTISFSAERS IEDEINRESN
SDIGVVLISY IVMFVYISIA LGHIQSCRRL LVDSKISLGI AGILIVLSSV ACSIGIFSYF
GIPLTLIVIE VIPFLVLAIG VDNIFIIVQT LQRDERLQGE TLDKQIGRVL GDVAPSMFLS
SFSETVAFFL GTLSTMPAVR TFSLFAGMAV LIDFILQVTC FVSLLGLDIK RQERNRLDIL
CCIKSSEETG GVQRSESMLF LFFKNVFSPY LLKDWMRPIV IAVFVGVLSF STAVIHNVEI
GLDQSLSMPD DSYVIDYFSQ FSKYLHAGPP VYFVLEEGHN YTSLEGQNMV CGGMGCNNDS
LVQQVFNAAE IGSYTRIGYA PSSWIDDYFD WVKPQSSCCR VYNTTGQFCN ASVSDPSCTR
CRPLTQEGKQ RPQGQDFMTF LPMFLSDNPN PKCGKGGHAA YNSAVNFINN KSDVGATYFM
TYHTVLKTSS DFIDAMRKAR IIADNITETM GIKEKNYRVF PYSVFYVFYE QYLTIVHDAI
FNLCVSLGSI FIVTSVLLGF EVWAAVVVSI TIAMIIINMF GVMWLWGISL NAVSLVNLVM
SCGIAVEFCS HVTRAFTVST KGSRVERAEE ALSHMGSSVF SGITLTKFGG IVVLAFSKSQ
IFKVFYFRMY LAMVVLGATH GLIFLPVLLS YIGPSVNKAK TRAAQERTRG TEQERLLYF
//
