ID A0A0R0ITC7_SOYBN Unreviewed; 1192 AA.
AC A0A0R0ITC7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KRH45418.1, ECO:0000313|EnsemblPlants:KRH45418};
GN Name=100809752 {ECO:0000313|EnsemblPlants:KRH45418};
GN ORFNames=GLYMA_08G270300 {ECO:0000313|EMBL:KRH45418.1};
OS Glycine max (Soybean) (Glycine hispida).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3847 {ECO:0000313|EMBL:KRH45418.1};
RN [1] {ECO:0000313|EMBL:KRH45418.1, ECO:0000313|EnsemblPlants:KRH45418}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH45418};
RC TISSUE=Callus {ECO:0000313|EMBL:KRH45418.1};
RX PubMed=20075913; DOI=10.1038/nature08670;
RA Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA Stacey G., Shoemaker R.C., Jackson S.A.;
RT "Genome sequence of the palaeopolyploid soybean.";
RL Nature 463:178-183(2010).
RN [2] {ECO:0000313|EnsemblPlants:KRH45418}
RP IDENTIFICATION.
RC STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH45418};
RG EnsemblPlants;
RL Submitted (FEB-2018) to UniProtKB.
RN [3] {ECO:0000313|EMBL:KRH45418.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Callus {ECO:0000313|EMBL:KRH45418.1};
RA Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA Jackson S.;
RT "WGS assembly of Glycine max.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CM000841; KRH45418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R0ITC7; -.
DR EnsemblPlants; KRH45418; KRH45418; GLYMA_08G270300.
DR Gramene; KRH45418; KRH45418; GLYMA_08G270300.
DR OMA; NALAFWR; -.
DR Proteomes; UP000008827; Chromosome 8.
DR ExpressionAtlas; A0A0R0ITC7; baseline and differential.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd18577; ABC_6TM_Pgp_ABCB1_D1_like; 1.
DR CDD; cd18578; ABC_6TM_Pgp_ABCB1_D2_like; 1.
DR CDD; cd03249; ABC_MTABC3_MDL1_MDL2; 2.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24222; ABC TRANSPORTER B FAMILY; 1.
DR PANTHER; PTHR24222:SF62; ABC TRANSPORTER B FAMILY MEMBER 13-LIKE; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008827};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1192
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014521856"
FT TRANSMEM 121..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 203..223
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 621..654
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 666..683
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 753..780
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 848..869
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 889..910
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 35..264
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 299..536
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT DOMAIN 625..911
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 944..1180
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
FT REGION 565..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1192 AA; 130873 MW; 6C94E0B44277B8E7 CRC64;
MCSWCFCACF LCLLWKDYQC HRLSLPFSQR SFPRSFQEVA CWMHTGERQA AKMRMAYLRS
MLNQDISLFD TEASTGEVIS SITSDIIVVQ DALSEKVGNF MHYISRFIAG FTIGFVRVWQ
ISLVTLAIVP LIALAGGLYA YVTIGLIGKV RKSYVRAGEI AEEVIGNVRT VQAFAGEERA
VRSYKVALMN TYRNGRKAGL AKGLGLGSMH CVLFLSWALL VWFTSVVVHK NIANGGNAFT
TMLNVVISGL SLGQAAPDIS AFIRAKAAAY PIFEMIERDT MSKASSENGK KLSKLEGHIQ
FKDVCFSYPS RPDVVIFNNF CIEIPSGKIL ALVGGSGSGK STVISLIERF YEPLSGQILL
DGNNIRELDL KWLRQQIGLV NQEPALFATS IRENILYGKD DATLEEVNQA VILSDAQSFI
NNLPDGLDTQ VGERGIQLSG GQKQRIAISR AIVKNPSILL LDEATSALDS ESEKSVQEAL
DRVMVGRTTV IVAHRLSTIR NADMIVVIEE GGKVVEIGNH EELISNPNNN VYASLVQIQE
KAFSQSHISG DPYLGGSSRY LGGSSRHLGE SSSRATSFRG SFRSDKESTS KAFGDEAEGS
VGSSSRHVSA RRLYSMIGPD WFYGVFGTLG AFIAGAQMPL FALGISHALV SYYMDWHTTR
HEVKKVALLF CGAAVLTITA HAIEHLSFGI MGERLTLRAR EKMFSAILKS EIGWFDDINN
TSSMLSSRLE TDATFLRTVV VDRSTILLQN VGLVVASFII AFMLNWRITL VVLATYPLII
SGHISEKLFM QGFGGNLSKA YLKANMLAGE AVSNIRTVAA FCAEQKVLDL YAHELVEPSK
RSFNRGQIAG IFYGISQFFI FSSYGLALWY GSVLMEKELS SFKSIMKSFM VLIVTALAMG
ETLALAPDLL KGNQMVASIF EVMDRKTGIL GDVGEELKTV EGTIELKRIH FCYPSRPDVV
IFNDFNLKVL AGKNIALVGH SGCGKSSVIS LILRFYDPTS GKVMIDGKDI KKLNLKSLRK
HIGLVQQEPA LFATSIYENI LYGKEGASEA EVIEAAKLAN AHSFISALPE GYATKVGERG
VQLSGGQKQR VAIARAVLKN PEILLLDEAT SALDLESERV VQQALDKLMK NRTTVIVAHR
LSTITNADQI AVLEDGKIIQ RGTHARLVEN TDGAYYKLVS LQQQQHIQEH ND
//
