ID A0A158NJC6_ATTCE Unreviewed; 1361 AA.
AC A0A158NJC6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=SSD domain-containing protein {ECO:0000259|PROSITE:PS50156};
GN Name=105620753 {ECO:0000313|EnsemblMetazoa:XP_012057634.1};
OS Atta cephalotes (Leafcutter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=12957 {ECO:0000313|EnsemblMetazoa:XP_012057634.1, ECO:0000313|Proteomes:UP000005205};
RN [1] {ECO:0000313|Proteomes:UP000005205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21347285; DOI=10.1371/journal.pgen.1002007;
RA Suen G., Teiling C., Li L., Holt C., Abouheif E., Bornberg-Bauer E.,
RA Bouffard P., Caldera E.J., Cash E., Cavanaugh A., Denas O., Elhaik E.,
RA Fave M.J., Gadau J., Gibson J.D., Graur D., Grubbs K.J., Hagen D.E.,
RA Harkins T.T., Helmkampf M., Hu H., Johnson B.R., Kim J., Marsh S.E.,
RA Moeller J.A., Munoz-Torres M.C., Murphy M.C., Naughton M.C., Nigam S.,
RA Overson R., Rajakumar R., Reese J.T., Scott J.J., Smith C.R., Tao S.,
RA Tsutsui N.D., Viljakainen L., Wissler L., Yandell M.D., Zimmer F.,
RA Taylor J., Slater S.C., Clifton S.W., Warren W.C., Elsik C.G., Smith C.D.,
RA Weinstock G.M., Gerardo N.M., Currie C.R.;
RT "The genome sequence of the leaf-cutter ant Atta cephalotes reveals
RT insights into its obligate symbiotic lifestyle.";
RL PLoS Genet. 7:e1002007-e1002007(2011).
RN [2] {ECO:0000313|EnsemblMetazoa:XP_012057634.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (APR-2016) to UniProtKB.
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; ADTU01017546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01017547; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01017548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; ADTU01017549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_012057634.1; XM_012202244.1.
DR STRING; 12957.A0A158NJC6; -.
DR EnsemblMetazoa; XM_012202244.1; XP_012057634.1; LOC105620753.
DR GeneID; 105620753; -.
DR KEGG; acep:105620753; -.
DR eggNOG; KOG1933; Eukaryota.
DR InParanoid; A0A158NJC6; -.
DR OrthoDB; 2786103at2759; -.
DR Proteomes; UP000005205; 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 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 Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005205};
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..47
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 48..1361
FT /note="SSD domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007629219"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 414..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 686..707
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 719..743
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 749..771
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 826..850
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 900..920
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1168..1187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1194..1214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1220..1241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1262..1282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 685..850
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
FT REGION 1311..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1333..1347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1361 AA; 151542 MW; D3FC8AB4FB118421 CRC64;
MHWTRVTTAT AGTAAYRNLI GAAVTRNVLQ PLLFLLTLSS FVSLVVSEEN DHCIWYGECY
TDASMHIKNC IYDGPAKPLN SEGQKLLAKH CPHLLVDEGK GINTCCDTKQ LTTLDSNIQL
ASNFLKRCPS CLDNLAKHFC DFTCGVNQSK FINVTEKGVA DGVEYVNKIN IYITNKYLDG
TFNSCNKVSV PSTGQLALDL MCGEWGASRC TPLKWFHFMG DAENNVFVPF QITYINTDNP
VGSFTPLDPP ITPCNKALNK NTPACSCVDC EQSCPTPPPM PPLPMPFSIF SYDGYEVIMT
IIFVCGSCLF LLLMMCFSHR KRIVARGEEV GRQVGRRLAA GLHHSGDGAR IALAADQEDS
PLQSKRSSVI SSDELPAGFD QEQSTFIEKL GAGTDKFLQE FFCKWGTVCA SRPWLILFLG
FLLIVGLGHG IKYMKVTTDP VELWASPHSR SRIEREYFDK HFEPFYRNEQ IIITSVGLPN
VVHNTSNGPI VFGPVFNDTF LKTIFELQEG IKSIITPNNY TLADICFAPL TGPFTGPTTV
SHCTIQSIWG YWQDDLKKFE NSEEEGNYTV NYLDHFRVCS QNAYNPECLA LYGGPVEPAI
AVGGFLSPGQ DLHNPSYEKA TAIILTLLVN NYHNKARLLP AMEWEESFIN FMKNWTATRK
PAFMDIAFTS ERSIEDELNR ESQSDIVTIL VSYIIMFGYI AVSLGQIRSC ARLLHDSKIT
LGLGGVLIVL ASVICSVGLF GFIGIPATLI IIEVIPFLVL AVGVDNIFIL VQTHQREGRR
PNESIPEHIG RTLGQVGPSM LLTSVSESCC FFLGGLSDMP AVKAFALYAG MALLVDFILQ
ITCFVSLLAL DTIRHANNRL DVCCFIRSKR DDGEEVVDGM LYKIFKVAYV PLLLQKWVRA
TVMIVFFGWL CSSIAVIPHI EIGLDQELSM PEDSFVLKYF KFLNNYLSIG PPMYFVVKDG
LNYSNTKMQN LVCGGQYCNS DSVLTQIFTA SKQSNRTYIA KPASSWMDDY IDWSGLASCC
KYFPKNNSFC PHTGRQCSVC NITLNEYNRP VPVDFNKYVS FFLQDNPDET CAKGGHAAYG
HGVNYITDPT TGMSTVGASY FMAYHTILKT SADYFESMRA ARVVAANITN MLNYNLKGHN
ENTTVEVFPY SVFYVFYEQY LTMWPDTLQS IGISLLAIFV VTFLLMGLDI FSSLVVLITI
TMIVINIGGL MYWWHITLNA VSLVNLVMAV GIAVEFCSHL VHSFSVSVQA TRVERVADAL
TNMGSSVFSG ITLTKFGGII VLGFAKSQIF QVDFFFTYIL SGVMSRRRRG RAREFASGSE
TRRHKRDKPD SPLLQNDNQQ RASTSYASVN SIDVTDHHVT F
//
