YIP4A_ARATH
ID YIP4A_ARATH Reviewed; 281 AA.
AC O64614; Q0WWQ2; Q8LEI4;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Protein YIP4a {ECO:0000303|PubMed:23832588};
DE AltName: Full=YPT/RAB GTPase-interacting protein 4a {ECO:0000303|PubMed:23832588};
DE Short=YIP4a {ECO:0000303|PubMed:23832588};
GN Name=YIP4A {ECO:0000303|PubMed:23832588};
GN OrderedLocusNames=At2g18840 {ECO:0000312|Araport:AT2G18840};
GN ORFNames=MSF3.22;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-240.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, SUBUNIT, AND
RP INTERACTION WITH YIP4B AND ECH.
RC STRAIN=cv. Columbia;
RX PubMed=23832588; DOI=10.1105/tpc.113.112482;
RA Gendre D., McFarlane H.E., Johnson E., Mouille G., Sjoedin A., Oh J.,
RA Levesque-Tremblay G., Watanabe Y., Samuels L., Bhalerao R.P.;
RT "Trans-Golgi network localized ECHIDNA/Ypt interacting protein complex is
RT required for the secretion of cell wall polysaccharides in Arabidopsis.";
RL Plant Cell 25:2633-2646(2013).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=30770391; DOI=10.1242/dev.168559;
RA Gendre D., Baral A., Dang X., Esnay N., Boutte Y., Stanislas T., Vain T.,
RA Claverol S., Gustavsson A., Lin D., Grebe M., Bhalerao R.P.;
RT "Rho-of-plant activated root hair formation requires Arabidopsis YIP4a/b
RT gene function.";
RL Development 146:0-0(2019).
CC -!- FUNCTION: Together with YIP4B, involved in the regulation of cell
CC elongation during root and hypocotyl growth (PubMed:23832588). YIP4A
CC and YIP4B are central trafficking components in Rho-of-plant (ROPs,
CC e.g. ARAC4/ROP2, ARAC5/ROP4 and ARAC3/ROP6) small GTPases-dependent
CC root hair formation, thus contributing to activation and plasma
CC membrane accumulation of ROPs during hair initiation (PubMed:30770391).
CC The ECH/YIP4 complex is involved in the modulation of the trans-Golgi
CC network (TGN)-mediated trafficking of some proteins and cell wall
CC components (e.g. pectin and hemicellulose) to the cell wall in dark-
CC grown hypocotyls and in secretory cells of the seed coat
CC (PubMed:23832588). {ECO:0000269|PubMed:23832588,
CC ECO:0000269|PubMed:30770391}.
CC -!- SUBUNIT: Homodimer and heterodimer with YIP4B (PubMed:23832588).
CC Component of a trans-Golgi network (TGN)-localized ECH/YIP4 complex
CC made of ECH, YIP4A and YIP4B (PubMed:23832588). Interacts directly with
CC ECH (PubMed:23832588). {ECO:0000269|PubMed:23832588}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:23832588}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in developing root hair cells.
CC {ECO:0000269|PubMed:30770391}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:23832588). The
CC double mutant yip4a yip4b exhibits disturbed trans-Golgi network (TGN)-
CC Golgi association and cell elongation defects leading to reduced roots
CC and hypocotyls growth associated with an abnormal cell wall composition
CC and a mislocalization of trans-Golgi network (TGN)-localized proteins
CC SYP61 and VHA-a1 (PubMed:23832588, PubMed:30770391). The double mutant
CC yip4a yip4b has also a reduced number of root trichoblasts displaying
CC Rho-of-plant (ROPs e.g. ARAC4/ROP2, ARAC5/ROP4 and ARAC3/ROP6) patches
CC and leading to an almost complete absence of root hairs
CC (PubMed:30770391). Strongly reduced ROP2 plasma membrane localization
CC (PubMed:30770391). {ECO:0000269|PubMed:23832588,
CC ECO:0000269|PubMed:30770391}.
CC -!- SIMILARITY: Belongs to the YIP1 family. {ECO:0000305}.
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DR EMBL; AC003673; AAM14883.1; -; Genomic_DNA.
DR EMBL; AC005724; AAD08953.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06812.1; -; Genomic_DNA.
DR EMBL; BT024504; ABD19685.1; -; mRNA.
DR EMBL; AY085403; AAM62630.1; -; mRNA.
DR EMBL; AK226288; BAE98446.1; -; mRNA.
DR PIR; T01612; T01612.
DR RefSeq; NP_565442.1; NM_127440.4.
DR AlphaFoldDB; O64614; -.
DR STRING; 3702.AT2G18840.1; -.
DR TCDB; 9.B.135.1.2; the membrane trafficking yip (yip) family.
DR PaxDb; O64614; -.
DR PRIDE; O64614; -.
DR ProteomicsDB; 189844; -.
DR EnsemblPlants; AT2G18840.1; AT2G18840.1; AT2G18840.
DR GeneID; 816399; -.
DR Gramene; AT2G18840.1; AT2G18840.1; AT2G18840.
DR KEGG; ath:AT2G18840; -.
DR Araport; AT2G18840; -.
DR TAIR; locus:2044455; AT2G18840.
DR eggNOG; KOG2946; Eukaryota.
DR HOGENOM; CLU_059592_2_1_1; -.
DR InParanoid; O64614; -.
DR OMA; IKFYHVL; -.
DR OrthoDB; 1287193at2759; -.
DR PhylomeDB; O64614; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O64614; baseline and differential.
DR GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; IDA:TAIR.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR GO; GO:0045489; P:pectin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0099402; P:plant organ development; IMP:UniProtKB.
DR GO; GO:0052324; P:plant-type cell wall cellulose biosynthetic process; IMP:UniProtKB.
DR GO; GO:0015774; P:polysaccharide transport; IGI:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0051223; P:regulation of protein transport; IMP:UniProtKB.
DR GO; GO:0048364; P:root development; IMP:UniProtKB.
DR GO; GO:0048766; P:root hair initiation; IMP:UniProtKB.
DR GO; GO:0009826; P:unidimensional cell growth; IMP:UniProtKB.
DR InterPro; IPR045231; Yip1/4-like.
DR InterPro; IPR006977; Yip1_dom.
DR PANTHER; PTHR21236; PTHR21236; 1.
DR Pfam; PF04893; Yip1; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Golgi apparatus; Membrane;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..281
FT /note="Protein YIP4a"
FT /id="PRO_0000450869"
FT TOPO_DOM 1..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..172
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..228
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 281 AA; 30250 MW; 01D8E1E657017275 CRC64;
MSQGDTVPLH PSSQSDIDEI ENLINESVQS GPGTVLAARP PSPTRPSIPV SSSSSSSPFM
QSNLPPLHPS SSAQKVTHVP VPPPLPAVSN SSNFQGASAF GSPPNTLTEP VWDTVKRDLS
RIVSNLKLVV FPNPYREDPG KALRDWDLWG PFFFIVFLGL TLSWSASVKK SEVFAVAFAL
LAAGAVILTL NVLLLGGHII FFQSLSLLGY CLFPLDVGAV ICMLKDNVIL KMVVVSVTLA
WSSWAAYPFM SSAVNPRRKA LALYPVFLMY VSVGFLIIAI N
