ABCG1_ARTBC
ID ABCG1_ARTBC Reviewed; 1101 AA.
AC D4AYW0;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=ABC transporter G family member ARB_01379 {ECO:0000305};
DE Short=ABC transporter ARB_01379 {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=ARB_01379;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P25371}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P25371}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}.
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DR EMBL; ABSU01000019; EFE31780.1; -; Genomic_DNA.
DR RefSeq; XP_003012420.1; XM_003012374.1.
DR AlphaFoldDB; D4AYW0; -.
DR SMR; D4AYW0; -.
DR STRING; 663331.D4AYW0; -.
DR PRIDE; D4AYW0; -.
DR EnsemblFungi; EFE31780; EFE31780; ARB_01379.
DR GeneID; 9520069; -.
DR KEGG; abe:ARB_01379; -.
DR eggNOG; KOG0061; Eukaryota.
DR HOGENOM; CLU_000604_57_1_1; -.
DR OMA; IDHKYGL; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR CDD; cd00055; EGF_Lam; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01061; ABC2_membrane; 1.
DR Pfam; PF19055; ABC2_membrane_7; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF07974; EGF_2; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Disulfide bond; EGF-like domain; Endoplasmic reticulum;
KW Glycoprotein; Membrane; Nucleotide-binding; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..15
FT /evidence="ECO:0000255"
FT CHAIN 16..1101
FT /note="ABC transporter G family member ARB_01379"
FT /id="PRO_5003053620"
FT TOPO_DOM 16..320
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..845
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 846..866
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 867..880
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 881..901
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 902..935
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 936..956
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 957..961
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 962..982
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 983..988
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 989..1009
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1010..1015
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 1016..1036
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1037..1050
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1051..1071
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1072..1077
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 1078..1098
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1099..1101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 84..122
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 375..617
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 677..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 407..414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 93..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 112..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1101 AA; 121049 MW; C95E308BBF4844C8 CRC64;
MAWLALLGLL PLLPAIQPTW QANGYEINST ADSFVTAATP FTLRSARPPE CPPCFNCQLP
AFKCHQFGKC NKFNGKCDCP PGFGGDDCAE PLCGSLPDGR DRTPRKGSTC QCKDGWSGIN
CNMCETNDAC NAMMPEREGG VCYRHHNGGE TVAENYQMCE VTNRKIRDML KEKKPQVTFS
CKKEDKTCNF QFWVDQLESF YCSLDTCKWN MDITENQNLT TYQCDNIKCG CVPDRMLCET
TGVSLEPLFG QLTGPAKFTS TSTKGGSNKD GSAFSEPVID KVISDLFGDK SILLDCYSSE
CLYKTAVPGY KPPVKVINTP LIAGVIAGCS LFIVGVILLI WYLSRRKAYN QYHALADDSD
DEGSKLMADH KPASLQFENI SYYINGQQIL SGIRGIAKPG QVTAIMGASG AGKTTFLDIL
ARKNKRGVVH GDIYVNGEKF NDSEYKKVVG FVDQEDTMLP TLTVHETILN SALLRLPRDM
SDAAKQQRVY EVEKQLGIHH IKDQLIGSEE GKGRGISGGE KKRVSIACEL VTSPSILFLD
EPTSGLDAFN AFNVIECLVN LAKSYNRTVI FTIHQPRSNI VALFDQLILL GKGKTVFSGP
YSSCQSYFDN IGYSCPPGFN IADYLVDLTM HASQSRSTEE PAVNVDSHDN NFRTASSSLR
AVKSVASASN ASIDNASAVD SAQESLLRPK DKRRSSLKQR QDRQLYTRKR GSGLESPPDP
QTDNEDGHVM SLAERAQQWL PLSRQQGQVP PQILQDPDHL PPIASGFVTD LDVLVSYYAN
SNVANAVRDE ISSSVQDALA ANGQANSQQA SDAVTGQMTG YARVGLIRQF IILSSRTWKN
LYRNPMLMLT HYATAILLAV LSGYLFYGLT DDIKGFQNRL GLFFFLLALF GFSTLTSLTV
FSSERLLFVR ERANGYYSPV TYFTAKVLFD IVPLRLIPPI IMGVIVYPMV GLIPDWPEFS
KFILVLVLFN LAAAGICLLI GIVFRDPGVA NLIGSLVMLF SLLFAGLLLN HDAIPASALW
LQTLSIFHYA FEALIVNEVT FLTLIDHKYG LDIEVPGASI LSAFGFNNLA LWNDVAGLGV
ISGVSIIMAY AAMHFLLVEK R
