ID A0A2P5ACQ5_PARAD Unreviewed; 1291 AA.
AC A0A2P5ACQ5;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Patched {ECO:0000313|EMBL:PON34306.1};
GN ORFNames=PanWU01x14_345550 {ECO:0000313|EMBL:PON34306.1};
OS Parasponia andersonii (Sponia andersonii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX NCBI_TaxID=3476 {ECO:0000313|EMBL:PON34306.1, ECO:0000313|Proteomes:UP000237105};
RN [1] {ECO:0000313|Proteomes:UP000237105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:PON34306.1}.
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DR EMBL; JXTB01000669; PON34306.1; -; Genomic_DNA.
DR STRING; 3476.A0A2P5ACQ5; -.
DR OrthoDB; 2786103at2759; -.
DR Proteomes; UP000237105; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015918; P:sterol 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: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:UP000237105};
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 274..293
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 371..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 581..599
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 614..637
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 649..669
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 717..743
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 791..815
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1113..1132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1138..1161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1168..1189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1209..1229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1241..1264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 580..743
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
SQ SEQUENCE 1291 AA; 141653 MW; 110A2499B51668DA CRC64;
MYKQVLLIAY SVNAEGSDRR LLLTPDAVTG ERHSEGYCAM YDICGKRSDG KVLNCPLGSS
SVKPDELLSS KIQSLCPTIT GNVCCTEAQF DTLRTQVQQA IPFLVGCPAC LRNFLNLFCE
LTCSPNQSLF INVTSVSKVN NNLTVDGIDF YITDAFGEGL YDSCNDVKFG TMNSRALEFI
GAGAKNFKEW FAFIGRRAQA NMPGSPYAIA FQSSISESSG MKPMNVSTYS CGDVSLGCSC
GDCPASPVCS SSVPPPSQKE GSCSVRIGSL KAKCIDIAVA ILYIILVSAF LGWRLFYLNG
QKKPACRTKP VWNAIEGGEL HSVNRQKEEN PSIQMLEDDP QIRNGVQLSV VQGYMSNFFR
IYGTWVAKNP IIVLCSSLAI VLILCLGLIR FKVETRPEKL WVGPGSKAAE EKQFFDSHLA
PFYRIEQLIL ANIPDDNGKS PSIVTENNIK LLFEIQKKVD GLRANFSGSA ISLSDICMKP
LDQDCATQSV LQYFKMDPDN YDNFGGVEHL KYCFEHYSSA DKCMSAFKAP LDPSTALGGF
SGNNYSEDEL LQMVQSKNLT LSFSSESSIE EELKRESTTD AITIVISYLV MFAYISLTLG
DTPRLSFFYI SSKVLLGLSG VVLVMLSVLG SVGFFSAIGV KSTLIIMEVI PFLVLAVGVD
NMCILVHAVK RQPMELPLEE RISNALVEVG PSITLASIAE VLAFAVGSFI PMPACRVFSM
FAALAVLLDF LLQVTAFVAL IAFDFLRTED KRVDCFPCMK VASYANSDKG IGQRKSGLLA
RYMKEIHAPI LSLWGVKIVV ISVFVAFTLA SIALCTRIEP GLEQKIVLPQ DSYLQGYFNS
VSEYLRIGPP LYFVALCTRI EPGLEQKIVL PQDSYLQGYF NSVSEYLRIG PPLYFVVKNY
NYSSESRHTN QLCSINKCDS NSLLNEIAKA SSTPKASYIA KPAASWLDDF LVWISPEAFG
CCRKFTNSTY CPPDDQPPCC SSSGGSCSLG GVCKDCTTCF RHSDLQNDRP STTQFKDKLP
WFLNALPSAA CAKGGHGAYT TSVELKDYES GIIQASSFRT YHTPLNKQID YVNSMRAARE
FSSRISDSLK MEIFPYSVFY MFFEQYLDIW KTALINLSIA IGAVFIVCLV ITCSFWSSAI
ILLVLAMIVV DLMGVMAILG IQLNAISVVN LVMSVGIAVE FCVHMTHAFS VSSGDKNQRV
KEALGTMGAS VFSGITLTKL VGVIVLCFSR TEVFVVYYFQ MYLALVLLGF LHGLVFLPVV
LSIFGPPSRS LLIDQQQEGR PSGASSRQTV S
//
