ACBP4_ORYSJ
ID ACBP4_ORYSJ Reviewed; 336 AA.
AC A3AYR1; Q7XPW9;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Acyl-CoA-binding domain-containing protein 4 {ECO:0000305};
DE Short=Acyl-CoA binding protein 4 {ECO:0000303|PubMed:21128943};
DE Short=OsACBP4 {ECO:0000303|PubMed:21128943};
GN Name=ACBP4 {ECO:0000303|PubMed:21128943};
GN OrderedLocusNames=Os04g0681900 {ECO:0000312|EMBL:BAS91681.1},
GN LOC_Os04g58550 {ECO:0000305};
GN ORFNames=OsJ_16661 {ECO:0000312|EMBL:EAZ32450.1},
GN OSJNBa0032F06.12 {ECO:0000312|EMBL:CAE03429.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=21128943; DOI=10.1111/j.1469-8137.2010.03546.x;
RA Meng W., Su Y.C., Saunders R.M., Chye M.L.;
RT "The rice acyl-CoA-binding protein gene family: phylogeny, expression and
RT functional analysis.";
RL New Phytol. 189:1170-1184(2011).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24738983; DOI=10.1111/nph.12809;
RA Meng W., Hsiao A.S., Gao C., Jiang L., Chye M.L.;
RT "Subcellular localization of rice acyl-CoA-binding proteins (ACBPs)
RT indicates that OsACBP6::GFP is targeted to the peroxisomes.";
RL New Phytol. 203:469-482(2014).
CC -!- FUNCTION: Binds medium- and long-chain acyl-CoA esters with high
CC affinity. Can interact in vitro with palmitoyl-CoA, linoleoyl-CoA and
CC linolenoyl-CoA (PubMed:21128943). Binds phosphatidic acid (PA) and
CC phosphatidylcholine (PC) in vitro. May play a role in the biosynthesis
CC of phospholipids (PubMed:24738983). {ECO:0000269|PubMed:21128943,
CC ECO:0000269|PubMed:24738983}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000305|PubMed:24738983}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves. Expressed at low levels
CC in roots and seeds. {ECO:0000269|PubMed:21128943}.
CC -!- INDUCTION: Induced by salt and drought stresses. Down-regulated by cold
CC stress, wounding and infection with the rice blast fungus Magnaporthe
CC oryzae. {ECO:0000269|PubMed:21128943}.
CC -!- SIMILARITY: Belongs to the ACBP family. {ECO:0000305}.
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DR EMBL; AL606641; CAE03429.1; -; Genomic_DNA.
DR EMBL; AP008210; BAF16206.1; -; Genomic_DNA.
DR EMBL; AP014960; BAS91681.1; -; Genomic_DNA.
DR EMBL; CM000141; EAZ32450.1; -; Genomic_DNA.
DR RefSeq; XP_015637218.1; XM_015781732.1.
DR AlphaFoldDB; A3AYR1; -.
DR SMR; A3AYR1; -.
DR STRING; 4530.OS04T0681900-02; -.
DR PaxDb; A3AYR1; -.
DR PRIDE; A3AYR1; -.
DR EnsemblPlants; Os04t0681900-02; Os04t0681900-02; Os04g0681900.
DR GeneID; 4337434; -.
DR Gramene; Os04t0681900-02; Os04t0681900-02; Os04g0681900.
DR KEGG; osa:4337434; -.
DR eggNOG; KOG0817; Eukaryota.
DR HOGENOM; CLU_050309_0_0_1; -.
DR OMA; MKARSKW; -.
DR OrthoDB; 1575996at2759; -.
DR Proteomes; UP000000763; Chromosome 4.
DR Proteomes; UP000007752; Chromosome 4.
DR Proteomes; UP000059680; Chromosome 4.
DR ExpressionAtlas; A3AYR1; baseline and differential.
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:0000062; F:fatty-acyl-CoA binding; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR000582; Acyl-CoA-binding_protein.
DR InterPro; IPR035984; Acyl-CoA-binding_sf.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR Pfam; PF00887; ACBP; 1.
DR Pfam; PF12796; Ank_2; 1.
DR PRINTS; PR00689; ACOABINDINGP.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 2.
DR SUPFAM; SSF47027; SSF47027; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS51228; ACB_2; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 2: Evidence at transcript level;
KW ANK repeat; Endoplasmic reticulum; Glycoprotein; Lipid-binding; Membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..336
FT /note="Acyl-CoA-binding domain-containing protein 4"
FT /id="PRO_0000442034"
FT TRANSMEM 12..32
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000255"
FT DOMAIN 90..178
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT REPEAT 251..280
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 284..313
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REGION 40..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 120..124
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT BINDING 142
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT BINDING 146
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT BINDING 165
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000250|UniProtKB:P07107"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 46
FT /note="S -> F (in Ref. 1; CAE03429 and 2; BAF16206)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="E -> D (in Ref. 1; CAE03429 and 2; BAF16206)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 336 AA; 35901 MW; ED16F71911DF3FD9 CRC64;
MGGDWQELAQ AAVIGLLFAF LVAKLISTVI AFKEDNLRIT RSTPTSPSAA DTPAAPAPPP
ASLDGGHGDT SDGSGSDSDS DWEGVESTEL DEEFSAASAF VAASAASGTS VPEQAQLQLY
GLYKIATEGP CTAPQPSALK LKARAKWNAW HKLGAMPTEE AMQKYITVVD ELFPNWSMGS
STKRKDEDTT VSASSSKGPM GPVFSSLMYE EEDQGNDSEL GDIHVSAREG AIDDIAKHLA
AGVEVNMRDS EGRTPLHWAV DRGHLNSVEI LVNANADVNA QDNEGQTALH YAVLCEREDI
AELLVKHHAD VQIKDEDGNT VRELCPSSWS FMNLAN
