LipidDB-3702-00876

Lipid Modification Database

Tag

Content

LipidDB ID

LipidDB-3702-00876

Entry Name

UniProt Accession

Q9XIE2; Q8VXW5;

Theoretical PI

8.08

Molecular Weight

165082.05

Genbank Protein ID

AAD39329.1; AEE33632.1; AAL67129.1; DAA00876.1;

Genbank Nucleotide ID

AC007258; CP002684; AY074515; BK001007;

Protein Name

ABC transporter G family member 36

Protein Synonyms/Alias

ABC transporter ABCG.36; AtABCG36; Pleiotropic drug resistance protein 8; Protein PENETRATION 3;

Gene Name

ABCG36

Gene Synonyms/Alias

PDR8; PEN3; At1g59870; F23H11.19;

Created Date

16-MAY-2006

Lipid Modification Sites
Position	Sequence Form	Peptide	References	Modification Type
442	Canonical	FESFGFKCPERKGTA	[1]	S-Palmitoylation
1460	Canonical	FAFIFAFCIRTLNFQ	[1]	S-Palmitoylation

Organism

Arabidopsis thaliana (Mouse-ear cress)

NCBI Taxa ID

3702

Reference

[1] Predicted from GPS-Lipid

Functional Description

Key factor that controls the extent of cell death in the defense response. Neccessary for both callose deposition and glucosinolate activation in response to pathogens. Required for limiting invasion by nonadapted powdery mildews. Confers resistance to cadmium (Cd) and lead (Pb), probably as an efflux pump of Cd2+ or Cd conjugates, and possibly, of chemicals that mediate pathogen resistance.

Sequence Annotation

Transmembrane: 540 560 Helical.
Transmembrane: 575 595 Helical.
Transmembrane: 621 641 Helical.
Transmembrane: 659 679 Helical.
Transmembrane: 685 705 Helical.
Transmembrane: 713 733 Helical.
Transmembrane: 772 792 Helical.
Transmembrane: 1216 1236 Helical.
Transmembrane: 1239 1259 Helical.
Transmembrane: 1299 1319 Helical.
Transmembrane: 1326 1346 Helical.
Transmembrane: 1356 1376 Helical.
Transmembrane: 1384 1404 Helical.
Transmembrane: 1441 1461 Helical.
Domain: 171 444 ABC transporter 1.
Domain: 522 735 ABC transmembrane type-2 1.
Domain: 867 1119 ABC transporter 2.
Domain: 1192 1406 ABC transmembrane type-2 2.
Nucleotide-binding: 204 211 ATP 1.
Nucleotide-binding: 912 919 ATP 2.
Modified residue: 1 1 N-acetylmethionine.
Modified residue: 43 43 Phosphothreonine.
Modified residue: 45 45 Phosphoserine.

Protein Length

1469 AA.

Protein Sequence
(Canonical)

MDYNPNLPPL GGGGVSMRRS ISRSVSRASR NIEDIFSSGS RRTQSVNDDE EALKWAAIEK  60
LPTYSRLRTT LMNAVVEDDV YGNQLMSKEV DVTKLDGEDR QKFIDMVFKV AEQDNERILT  120
KLRNRIDRVG IKLPTVEVRY EHLTIKADCY TGNRSLPTLL NVVRNMGESA LGMIGIQFAK  180
KAQLTILKDI SGVIKPGRMT LLLGPPSSGK TTLLLALAGK LDKSLQVSGD ITYNGYQLDE  240
FVPRKTSAYI SQNDLHVGIM TVKETLDFSA RCQGVGTRYD LLNELARREK DAGIFPEADV  300
DLFMKASAAQ GVKNSLVTDY TLKILGLDIC KDTIVGDDMM RGISGGQKKR VTTGEMIVGP  360
TKTLFMDEIS TGLDSSTTFQ IVKCLQQIVH LNEATVLMSL LQPAPETFDL FDDIILVSEG  420
QIVYQGPRDN ILEFFESFGF KCPERKGTAD FLQEVTSKKD QEQYWVNPNR PYHYIPVSEF  480
ASRYKSFHVG TKMSNELAVP FDKSRGHKAA LVFDKYSVSK RELLKSCWDK EWLLMQRNAF  540
FYVFKTVQIV IIAAITSTLF LRTEMNTRNE GDANLYIGAL LFGMIINMFN GFAEMAMMVS  600
RLPVFYKQRD LLFYPSWTFS LPTFLLGIPS SILESTAWMV VTYYSIGFAP DASRFFKQFL  660
LVFLIQQMAA SLFRLIASVC RTMMIANTGG ALTLLLVFLL GGFLLPKGKI PDWWGWAYWV  720
SPLTYAFNGL VVNEMFAPRW MNKMASSNST IKLGTMVLNT WDVYHQKNWY WISVGALLCF  780
TALFNILFTL ALTYLNPLGK KAGLLPEEEN EDADQGKDPM RRSLSTADGN RRGEVAMGRM  840
SRDSAAEASG GAGNKKGMVL PFTPLAMSFD DVKYFVDMPG EMRDQGVTET RLQLLKGVTG  900
AFRPGVLTAL MGVSGAGKTT LMDVLAGRKT GGYIEGDVRI SGFPKVQETF ARISGYCEQT  960
DIHSPQVTVR ESLIFSAFLR LPKEVGKDEK MMFVDQVMEL VELDSLRDSI VGLPGVTGLS  1020
TEQRKRLTIA VELVANPSII FMDEPTSGLD ARAAAIVMRA VRNTVDTGRT VVCTIHQPSI  1080
DIFEAFDELM LMKRGGQVIY AGPLGQNSHK VVEYFESFPG VSKIPEKYNP ATWMLEASSL  1140
AAELKLSVDF AELYNQSALH QRNKALVKEL SVPPAGASDL YFATQFSQNT WGQFKSCLWK  1200
QWWTYWRSPD YNLVRFIFTL ATSLLIGTVF WQIGGNRSNA GDLTMVIGAL YAAIIFVGIN  1260
NCSTVQPMVA VERTVFYRER AAGMYSAMPY AISQVTCELP YVLIQTVYYS LIVYAMVGFE  1320
WKAEKFFWFV FVSYFSFLYW TYYGMMTVSL TPNQQVASIF ASAFYGIFNL FSGFFIPRPK  1380
IPKWWIWYYW ICPVAWTVYG LIVSQYGDVE TRIQVLGGAP DLTVKQYIED HYGFQSDFMG  1440
PVAAVLIAFT VFFAFIFAFC IRTLNFQTR                                    1469

FASTA
(Canonical)

>LipidDB-3702-00876|Q9XIE2
MDYNPNLPPLGGGGVSMRRSISRSVSRASRNIEDIFSSGSRRTQSVNDDEEALKWAAIEK
LPTYSRLRTTLMNAVVEDDVYGNQLMSKEVDVTKLDGEDRQKFIDMVFKVAEQDNERILT
KLRNRIDRVGIKLPTVEVRYEHLTIKADCYTGNRSLPTLLNVVRNMGESALGMIGIQFAK
KAQLTILKDISGVIKPGRMTLLLGPPSSGKTTLLLALAGKLDKSLQVSGDITYNGYQLDE
FVPRKTSAYISQNDLHVGIMTVKETLDFSARCQGVGTRYDLLNELARREKDAGIFPEADV
DLFMKASAAQGVKNSLVTDYTLKILGLDICKDTIVGDDMMRGISGGQKKRVTTGEMIVGP
TKTLFMDEISTGLDSSTTFQIVKCLQQIVHLNEATVLMSLLQPAPETFDLFDDIILVSEG
QIVYQGPRDNILEFFESFGFKCPERKGTADFLQEVTSKKDQEQYWVNPNRPYHYIPVSEF
ASRYKSFHVGTKMSNELAVPFDKSRGHKAALVFDKYSVSKRELLKSCWDKEWLLMQRNAF
FYVFKTVQIVIIAAITSTLFLRTEMNTRNEGDANLYIGALLFGMIINMFNGFAEMAMMVS
RLPVFYKQRDLLFYPSWTFSLPTFLLGIPSSILESTAWMVVTYYSIGFAPDASRFFKQFL
LVFLIQQMAASLFRLIASVCRTMMIANTGGALTLLLVFLLGGFLLPKGKIPDWWGWAYWV
SPLTYAFNGLVVNEMFAPRWMNKMASSNSTIKLGTMVLNTWDVYHQKNWYWISVGALLCF
TALFNILFTLALTYLNPLGKKAGLLPEEENEDADQGKDPMRRSLSTADGNRRGEVAMGRM
SRDSAAEASGGAGNKKGMVLPFTPLAMSFDDVKYFVDMPGEMRDQGVTETRLQLLKGVTG
AFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIEGDVRISGFPKVQETFARISGYCEQT
DIHSPQVTVRESLIFSAFLRLPKEVGKDEKMMFVDQVMELVELDSLRDSIVGLPGVTGLS
TEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRAVRNTVDTGRTVVCTIHQPSI
DIFEAFDELMLMKRGGQVIYAGPLGQNSHKVVEYFESFPGVSKIPEKYNPATWMLEASSL
AAELKLSVDFAELYNQSALHQRNKALVKELSVPPAGASDLYFATQFSQNTWGQFKSCLWK
QWWTYWRSPDYNLVRFIFTLATSLLIGTVFWQIGGNRSNAGDLTMVIGALYAAIIFVGIN
NCSTVQPMVAVERTVFYRERAAGMYSAMPYAISQVTCELPYVLIQTVYYSLIVYAMVGFE
WKAEKFFWFVFVSYFSFLYWTYYGMMTVSLTPNQQVASIFASAFYGIFNLFSGFFIPRPK
IPKWWIWYYWICPVAWTVYGLIVSQYGDVETRIQVLGGAPDLTVKQYIEDHYGFQSDFMG
PVAAVLIAFTVFFAFIFAFCIRTLNFQTR

Gene Ontology

GO:0009507; C:chloroplast; IDA:TAIR
GO:0009941; C:chloroplast envelope; IDA:TAIR
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0016020; C:membrane; IDA:TAIR
GO:0005739; C:mitochondrion; IDA:TAIR
GO:0005886; C:plasma membrane; IDA:TAIR
GO:0005774; C:vacuolar membrane; IDA:TAIR
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0016887; F:ATPase activity; IEA:InterPro
GO:0015086; F:cadmium ion transmembrane transporter activity; IDA:TAIR
GO:0070574; P:cadmium ion transmembrane transport; IDA:GOC
GO:0015691; P:cadmium ion transport; IMP:TAIR
GO:0071366; P:cellular response to indolebutyric acid stimulus; IMP:TAIR
GO:0052544; P:defense response by callose deposition in cell wall; IMP:TAIR
GO:0042742; P:defense response to bacterium; IMP:TAIR
GO:0009817; P:defense response to fungus, incompatible interaction; IMP:TAIR
GO:0006855; P:drug transmembrane transport; ISS:TAIR
GO:0042344; P:indole glucosinolate catabolic process; IMP:TAIR
GO:0031348; P:negative regulation of defense response; IMP:TAIR
GO:0009737; P:response to abscisic acid; IDA:TAIR
GO:0009627; P:systemic acquired resistance; IMP:TAIR

Interpro

InterPro; IPR003593; AAA+_ATPase
InterPro; IPR013525; ABC_2_trans
InterPro; IPR029481; ABC_trans_N
InterPro; IPR003439; ABC_transporter-like
InterPro; IPR027417; P-loop_NTPase
InterPro; IPR013581; PDR_assoc

Pfam

Pfam; PF01061; ABC2_membrane;
Pfam; PF00005; ABC_tran;
Pfam; PF14510; ABC_trans_N;
Pfam; PF08370; PDR_assoc;

SMART

SMART; SM00382; AAA;

PROSITE

PROSITE; PS50893; ABC_TRANSPORTER_2;

PRINTS