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Database: UniProt
Entry: D4AYW0
LinkDB: D4AYW0
Original site: D4AYW0 
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   10-APR-2019, entry version 44.
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)
OS   (Trichophyton 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.,
RA   Feuermann M., Pedruzzi I., Priebe S., Groth M., Winkler R., Li W.,
RA   Kniemeyer O., Schroeckh V., Hertweck C., Hube B., White T.C.,
RA   Platzer M., Guthke R., Heitman J., Woestemeyer J., Zipfel P.F.,
RA   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
CC       family. Eye pigment precursor importer (TC 3.A.1.204) subfamily.
CC       {ECO:0000305}.
DR   EMBL; ABSU01000019; EFE31780.1; -; Genomic_DNA.
DR   RefSeq; XP_003012420.1; XM_003012374.1.
DR   SMR; D4AYW0; -.
DR   STRING; 63400.XP_003012420.1; -.
DR   EnsemblFungi; EFE31780; EFE31780; ARB_01379.
DR   GeneID; 9520069; -.
DR   KEGG; abe:ARB_01379; -.
DR   eggNOG; ENOG410IN8P; Eukaryota.
DR   eggNOG; KOG0061; Eukaryota.
DR   eggNOG; COG0842; LUCA.
DR   eggNOG; COG1131; LUCA.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013525; ABC_2_trans.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01061; ABC2_membrane; 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; Complete proteome; Disulfide bond; EGF-like domain;
KW   Endoplasmic reticulum; Glycoprotein; Membrane; Nucleotide-binding;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL        1     15       {ECO:0000255}.
FT   CHAIN        16   1101       ABC transporter G family member
FT                                ARB_01379.
FT                                /FTId=PRO_5003053620.
FT   TOPO_DOM     16    320       Lumenal. {ECO:0000305}.
FT   TRANSMEM    321    341       Helical. {ECO:0000255}.
FT   TOPO_DOM    342    845       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    846    866       Helical. {ECO:0000255}.
FT   TOPO_DOM    867    880       Lumenal. {ECO:0000305}.
FT   TRANSMEM    881    901       Helical. {ECO:0000255}.
FT   TOPO_DOM    902    935       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    936    956       Helical. {ECO:0000255}.
FT   TOPO_DOM    957    961       Lumenal. {ECO:0000305}.
FT   TRANSMEM    962    982       Helical. {ECO:0000255}.
FT   TOPO_DOM    983    988       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    989   1009       Helical. {ECO:0000255}.
FT   TOPO_DOM   1010   1015       Lumenal. {ECO:0000305}.
FT   TRANSMEM   1016   1036       Helical. {ECO:0000255}.
FT   TOPO_DOM   1037   1050       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1051   1071       Helical. {ECO:0000255}.
FT   TOPO_DOM   1072   1077       Lumenal. {ECO:0000305}.
FT   TRANSMEM   1078   1098       Helical. {ECO:0000255}.
FT   TOPO_DOM   1099   1101       Cytoplasmic. {ECO:0000305}.
FT   DOMAIN       84    122       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      375    617       ABC transporter. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00434}.
FT   NP_BIND     407    414       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00434}.
FT   CARBOHYD     28     28       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    218    218       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   DISULFID     93    110       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    112    121       {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
//
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