ID A0A3L8T1M5_CHLGU Unreviewed; 1285 AA.
AC A0A3L8T1M5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=SSD domain-containing protein {ECO:0000259|PROSITE:PS50156};
GN ORFNames=DV515_00000203 {ECO:0000313|EMBL:RLW13350.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW13350.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW13350.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW13350.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW13350.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
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:RLW13350.1}.
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DR EMBL; QUSF01000001; RLW13350.1; -; Genomic_DNA.
DR STRING; 44316.ENSEGOP00005000239; -.
DR Ensembl; ENSEGOT00005000264; ENSEGOP00005000239; ENSEGOG00005000196.
DR OMA; WWFDVES; -.
DR Proteomes; UP000276834; 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:UP000276834};
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..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..1285
FT /note="SSD domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018174500"
FT TRANSMEM 267..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 361..379
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 629..650
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 662..686
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 692..714
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 768..793
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 845..864
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1105..1124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1131..1152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1158..1176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1197..1223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1235..1258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 628..793
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
SQ SEQUENCE 1285 AA; 143047 MW; 0A311314E21BC8E2 CRC64;
MGTPPGSPGR SGLGLLVLLL LLSPVRVLPQ VCVWYGECGV ASGDKRYNCA YDGPPIALPE
DGYDLMQELC PGLFFGNVST CCDVHQLQTL KNNLQLPLQF LSRCPSCFYN LINLFCELTC
SPNQSDFLNV TSTIPYYDPV SKENKSSVTE LQYFIGDRFA NAMYNACKDV EAPSSNVKAL
GLLCGKDVKD CNATNWIEYM FSKDNGQTPF NIIPIFSDVP VHGMSPMNNA TKGCNESMDD
STGPCSCQDC SIVCGPKPQP PPLPPPWLLF GLDAVYVIMW ISYMGFLLIF FALVFGVWCY
RRRHFVSEYT PIDSNVAFSV NSHRDNGNIT CGESLGESFE NGLRMTFTSW GAFCVRNPRP
VILFSVVFIA MCCSGFVYIK ATTNPVDLWS APSSQARKEK EYFDTHFGPF FRTEQVIIQA
PKSHPDTYSP YPSGEDVPFG PPLTKDILHQ VLDLQDAIVN ITASYDNETV MLKDICLAPL
APYNNNCTIL SVLNYFQNSH SVLDHTVGDE FFVYADYHTH FLYCVRAPAS LNDTSLLHDP
CLGTFGGPVF PWLVLGGYDD DNYNNATALV ITFPVNNYYN DSKKLMKALA WEKEFINFLK
NYNNSNLTIS FSAERSIEDE INRESNSDIS VVLISYIVMF VYISIALGHI QSCRRLLVDS
KITLGIAGIL IVLSSVACSI GIFSYFGIPL TLIVIEVIPF LVLAIGVDNI FIMVQTLQRD
ERLQGETLDK QIGRVLGDVA PSMFLSSFSE TVAFFLGTLS TMPAVRTFSL FAGMAVLIDF
ILQVTCFVSL LGLDIKRQES NRLDVLCCIK SSEEMSGVQR SENMLFLFFK NLFSPYLLKD
WMRPIVIAVF VGILSFSAAV MHNVEIGLDQ SLSMPDDSYV IDYFSNISKY LHAGPPVYFV
LEEGHNYTSL EGQNMVCGGT GCNNDSLVQQ VFNAAEIGSY TKIGYAPSSW IDDYFDWVKP
QSSCCRVYNT TGQFCNASVS DPSCTRCRPL TQEGKQRPQG EDFMTFLPMF LSDNPNPKCG
KGGHAAYNSA VNFINNKTEV GATYFMTYHT VLKTSSDFID AMRKAQIIAD NITETMGIKE
KNYRVFPYSV FYVFYEQYLT IVHDAIFNLC ISLGSIFLVT TVLLGFEVWA AVVVSITIAM
IIVNMFGVMW LWGISLNAVS LVNLVMSCGI AVEFCSHVTR AFTISTKGSR VERAEEALSH
MGSSVFSGIT LTKFGGIVVL AFSKSQIFKI FYFRMYLAMV LLGATHGLIF LPVLLSYIGP
SVNKAKTRAA QERTRGTERE RLLYF
//
