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Database: UniProt
Entry: W5NC12_LEPOC
LinkDB: W5NC12_LEPOC
Original site: W5NC12_LEPOC 
ID   W5NC12_LEPOC            Unreviewed;      1509 AA.
AC   W5NC12;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Dispatched RND transporter family member 2 {ECO:0000313|Ensembl:ENSLOCP00000018171.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000018171.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   The Broad Institute Genome Assembly & Analysis Group;
RG   Computational R&D Group;
RG   and Sequencing Platform;
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000018171.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the dispatched family.
CC       {ECO:0000256|ARBA:ARBA00038046}.
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DR   RefSeq; XP_006643132.2; XM_006643069.2.
DR   STRING; 7918.ENSLOCP00000018171; -.
DR   Ensembl; ENSLOCT00000018203.1; ENSLOCP00000018171.1; ENSLOCG00000014758.1.
DR   GeneID; 102696811; -.
DR   KEGG; loc:102696811; -.
DR   CTD; 85455; -.
DR   eggNOG; KOG3664; Eukaryota.
DR   GeneTree; ENSGT00940000159551; -.
DR   InParanoid; W5NC12; -.
DR   OMA; MPVTIVW; -.
DR   OrthoDB; 2875706at2759; -.
DR   Proteomes; UP000018468; Unassembled WGS sequence.
DR   Bgee; ENSLOCG00000014758; Expressed in testis and 4 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0035195; P:miRNA-mediated post-transcriptional gene silencing; IEA:Ensembl.
DR   GO; GO:0007224; P:smoothened signaling pathway; IBA:GO_Central.
DR   Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR   InterPro; IPR000731; SSD.
DR   PANTHER; PTHR45951:SF2; PROTEIN DISPATCHED HOMOLOG 2; 1.
DR   PANTHER; PTHR45951; PROTEIN DISPATCHED-RELATED; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        182..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        513..531
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        538..555
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        567..592
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        613..632
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        644..667
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1010..1029
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1035..1057
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1064..1088
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1108..1130
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          535..667
FT                   /note="SSD"
FT                   /evidence="ECO:0000259|PROSITE:PS50156"
FT   REGION          103..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1216..1247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1289..1323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1394..1456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1469..1509
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1226..1240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1289..1307
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1406..1420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1432..1446
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1495..1509
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1509 AA;  165749 MW;  A6BD229E3253A05A CRC64;
     MDACSVSEEN AHVIIMDSSP AEGPEQETSL SEIPEVALCP PESPDREPRL TLIHTDGDRL
     SSPGHPRTAS LSQLYHQVSQ GCSHQSPLLK RCRYCGHRQP VTSSLCPERH SGPASPRPDC
     SSATVKTADS CSPSHVPSCH DTIHCHWLQG SHDAGNHQAM QHHVVTVRHE RLYRIPRSYS
     QLVADCPVAL LITCAVVFLG CSLAGILTGP LPDFSDPLSG FEPRGTEIGR RLSAWNRLQE
     NTGPEKTLSL SPRQLTEQRV ISYDEEGGGG TGKSRDWPSP RQRRMLDWDF TQDTFFCDSP
     GEKYAQLVFR SGNSASLWSL QAIHSMCEME QARIRSHALF QDLCKHRGGE DGEGDTGMRE
     CCPSWSLGNY LAVLSNATSC LGLSAAQVSE SLQLLRQCAP YYHDGSLAPA CAEKGKLGQC
     STVPSQCKHS SAIYQILHYL VDKDFLGPQT IGYKVPSLKY SLLFLPVEKG DHMMDMYLDN
     LEGRDLTNDN TTITGMDLGI KKQLFQYYLA RDSVYPVLAV VMLFLTMAFY LHSLFLSAMS
     LAAILGSLMS SYFFYKVAFR LTFFPFLNLA ALLVLLGSCA NQAFIFADLW SLQLSQKPPA
     SLEKRVKRAL QEAGYLILVS GLTSSAAFYS GYMSSITAVR CFAVYLGTAT LISSLSSLVW
     LPCILILHER YAVAAAAVEA PAGKTCCALS PGGFWDTSSR KRCLFSLGQK LRGLRRGLTD
     TSDLLFIKIL PCGVVKFRYI WVCWFAVLAA GGTYITCVDP GMKLPTLESK AAQLFRSSHP
     FERYDAEYSH QFMFERLKSG EEKPMTITLV WGVLPTDNGD HLDPKSNGSL VLDPEFNMSS
     PDAQSWLRDL CPRIQNQSFY LPISSSSEEE KQGDSVCFVE RLLRWVSIRQ CSESEGAYSL
     CCNDILFPYL PGVFEHCLGM MAAEKEAEGF LFDTGGPRFD SEGRITALIL EFTTTHLHSY
     NYSQSAHFYQ QIEAWFHREI SGAPPGLRNG WFVSQLALYD LQQCLSSETL VVTGFSVALV
     FAMLLLTTWN IPLSIYGSAA VGGSVFVTAG LLVLLEWQLS GLEALFISAA AGLSVDFAAN
     YCVSYSLSPH PDRLGRVAHS LKRMGCPAAI GAGAFFCMGI IMLPATALLF RKLGIFLLLV
     KCVACGFATF FFQSLCCFFG PQKNCGQIFW PCTTASGHYK ADSESGNLLS TAAAGSSNSA
     ANGAFGCGGR SRVRRSFGKA EGGGQLCPSQ QRQRQRQGGG GGRESEQYEL QPLACQLSDS
     FENSTCTSKL SNRPSVLSEE IQFRSLSPRK DLEEFNTEDD SEELTSRHLK TFPPPPALQT
     SSPYKENTLR PVVVPPSEMV QERLLCRRCR GQAGGIKHWN VSLSSSSSME DIIISSQPPD
     MDHRHSLSIE GAMSSPFKRH PHRRLLSSQS QSSFEGLEDS NETCLSDVEP GPATPQPTTE
     AQAESQPGYL NGKRDTLRLS LKETVFEASS QGIGRGRTSQ GELPVILPNS KPDLPDVWIK
     REGRSGDGS
//
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