ID A0A401PYQ4_SCYTO Unreviewed; 1114 AA.
AC A0A401PYQ4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=SSD domain-containing protein {ECO:0000259|PROSITE:PS50156};
GN ORFNames=scyTo_0018579 {ECO:0000313|EMBL:GCB78236.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB78236.1, ECO:0000313|Proteomes:UP000288216};
RN [1] {ECO:0000313|EMBL:GCB78236.1, ECO:0000313|Proteomes:UP000288216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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:GCB78236.1}.
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DR EMBL; BFAA01013071; GCB78236.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401PYQ4; -.
DR STRING; 75743.A0A401PYQ4; -.
DR OMA; QHIAKWI; -.
DR Proteomes; UP000288216; Unassembled WGS sequence.
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:SF3; NPC1-LIKE INTRACELLULAR CHOLESTEROL TRANSPORTER 1; 1.
DR Pfam; PF16414; NPC1_N; 1.
DR Pfam; PF02460; Patched; 1.
DR Pfam; PF12349; Sterol-sensing; 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:UP000288216};
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..1114
FT /note="SSD domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019190354"
FT TRANSMEM 283..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 358..382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 548..569
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 581..605
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 611..634
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 688..712
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 754..780
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 967..990
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1002..1025
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 547..712
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
FT REGION 1063..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1114 AA; 122308 MW; 3A4403DEE2159FC1 CRC64;
MLVKVFTVLL SLNLRPFMAA CTSIHQAGHC AFYEDCGKNP EVSGSLLPAR VPCVYNGPAL
KVSGQHLELL KTVCPMLYTG AQSTHACCSM KQLNMLDKSL SLSKTLLSRC PSCVQNFINL
YCQNTCSPNQ SLHINVTRTF NSNDSGIIRE AVLEYQCYYG RRFADGAFNS CKNVRIPSTG
GFAIAPMCGK YGSLLCNTER WLSFQGDSSN GLAPLDIEFV LLDNETADVD GGIVPYAGNF
WRCNESTVPN GQACSCLDCV ESCPVIPTPT PAPGPWTIGA LDGALAVCLA AFGLSALLFA
TFLISRCHMA GRSRAGAGPP KSPQLHPVAA KWSHRISGAT QLSLTRTFRV WGTMVARYPI
AVICIALALV VVMSAGLVFL TLTTNPVELW SAPNSRARRE KDFHDANFGP FFRTNQIIIT
AGNHSSYTYD SVLFGPNAFS GIFSKEIILE LLDFQTRLQA ISVWSKAAQR NITIKDICYA
PLKPHNPRST DCAVNSLLQY FQNNRTRINA IASQTMAGIT GTVDWRDHFL YCIKSLEDEI
NRTTAEDIPI FAISYLVIFV YIALALGEYT SWRTVMIDSK VTLGLGGVLV VLGAVLSSMG
FYAYIGVPSS LIILEVVPFL VLAVGADNIF ILVLQYQRDE RQAGERREEQ IGRVLGDVAP
SMLLCSFSES ICFFLGALTK MPAVRTFALY AALAVFFDFL LQMTAFVALM SLDARREEKD
RFDICCCAHS KQKRTKKKNE GLLLPFMREH YAPFLLHPVT SIIVIVLFLF MLCTGIFLML
HVRVGLDQEL ALPADSYMLK YFAALNKYFE VGVPVYFVTT AGYNFTTVDG MNGICSSVGC
DNNSMTQKIQ YATEFPQVPT EEEFNQYLPI FLDDAPILQC SKGGLGAYGN AVKRGENGEI
LASRFMAYHT PLKNSQEYTA ALKVARELAA NITDSMRRIP GTDPNFEVFP YTAKRDKVER
AKEATAYMGS AVFAGVAMTN LPGIIVLYFA QSQLIQIFFF RLNLVITLLG LLHGLVFLPV
LLSYFGPDVS PAATLQQRTA TESLSGKIYS NSYFQNFGFE GPADGKKDQP MPQSNGTAKM
EEHPVTKGDE DPSAGEFTST GSCPDVTEPT VTSL
//
