SFH1_ARATH
ID SFH1_ARATH Reviewed; 554 AA.
AC F4JLE5; O65682; Q708J3;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Phosphatidylinositol/phosphatidylcholine transfer protein SFH1;
DE AltName: Full=Phosphatidylinositol transfer protein 1;
DE Short=AtPITP1;
DE AltName: Full=Protein CAN OF WORMS1;
DE AltName: Full=Protein SEC FOURTEEN HOMOLOGS 1;
DE Short=AtSFH1;
DE AltName: Full=Protein SHORT ROOT HAIR 1;
GN Name=SFH1; Synonyms=COW1, PITP1, SRH1; OrderedLocusNames=At4g34580;
GN ORFNames=T4L20.160;
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 [GENOMIC DNA / MRNA], DISRUPTION PHENOTYPE, FUNCTION,
RP AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=15546352; DOI=10.1111/j.1365-313x.2004.02245.x;
RA Bohme K., Li Y., Charlot F., Grierson C., Marrocco K., Okada K., Laloue M.,
RA Nogue F.;
RT "The Arabidopsis COW1 gene encodes a phosphatidylinositol transfer protein
RT essential for root hair tip growth.";
RL Plant J. 40:686-698(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
RP MUTANT COW1, FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9390433; DOI=10.1104/pp.115.3.981;
RA Grierson C.S., Roberts K., Feldmann K.A., Dolan L.;
RT "The COW1 locus of arabidopsis acts after RHD2, and in parallel with RHD3
RT and TIP1, to determine the shape, rate of elongation, and number of root
RT hairs produced from each site of hair formation.";
RL Plant Physiol. 115:981-990(1997).
RN [5]
RP GENE FAMILY, DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15728190; DOI=10.1083/jcb.200412074;
RA Vincent P., Chua M., Nogue F., Fairbrother A., Mekeel H., Xu Y., Allen N.,
RA Bibikova T.N., Gilroy S., Bankaitis V.A.;
RT "A Sec14p-nodulin domain phosphatidylinositol transfer protein polarizes
RT membrane growth of Arabidopsis thaliana root hairs.";
RL J. Cell Biol. 168:801-812(2005).
RN [6]
RP REVIEW.
RX PubMed=17051233; DOI=10.1038/nchembio835;
RA Ile K.E., Schaaf G., Bankaitis V.A.;
RT "Phosphatidylinositol transfer proteins and cellular nanoreactors for lipid
RT signaling.";
RL Nat. Chem. Biol. 2:576-583(2006).
RN [7]
RP REVIEW, AND FUNCTION.
RX PubMed=17335879; DOI=10.1016/j.advenzreg.2006.12.007;
RA Bankaitis V.A., Vincent P., Merkulova M., Tyeryar K., Liu Y.;
RT "Phosphatidylinositol transfer proteins and functional specification of
RT lipid signaling pools.";
RL Adv. Enzyme Regul. 47:27-40(2007).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=23456248; DOI=10.1007/s11103-013-0033-4;
RA Huang J., Kim C.M., Xuan Y.H., Park S.J., Piao H.L., Je B.I., Liu J.,
RA Kim T.H., Kim B.K., Han C.D.;
RT "OsSNDP1, a Sec14-nodulin domain-containing protein, plays a critical role
RT in root hair elongation in rice.";
RL Plant Mol. Biol. 82:39-50(2013).
CC -!- FUNCTION: Required for transport of secretory proteins from the Golgi
CC complex (By similarity). Catalyzes the transfer of phosphatidylinositol
CC and phosphatidylcholine between membranes in vitro. Plays a role in
CC root hair tip elongation as a key regulator of polarized membrane
CC trafficking. May promote the PtdIns(4,5)P2 synthesis and organization
CC in root hair membrane. {ECO:0000250, ECO:0000269|PubMed:15546352,
CC ECO:0000269|PubMed:15728190, ECO:0000269|PubMed:17335879,
CC ECO:0000269|PubMed:23456248, ECO:0000269|PubMed:9390433}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cell membrane
CC {ECO:0000269|PubMed:15728190}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15728190}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in roots. Detected solely
CC in root trichoblast cell files engaged in root hair growth, hydathodes,
CC shoot apical meristem, and apical cells of the root cap.
CC {ECO:0000269|PubMed:15546352, ECO:0000269|PubMed:15728190}.
CC -!- DISRUPTION PHENOTYPE: Exhibits short branched root hairs.
CC {ECO:0000269|PubMed:15546352, ECO:0000269|PubMed:15728190,
CC ECO:0000269|PubMed:23456248, ECO:0000269|PubMed:9390433}.
CC -!- SIMILARITY: Belongs to the SFH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18837.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80175.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAE82296.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAE82297.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ616026; CAE82296.1; ALT_FRAME; mRNA.
DR EMBL; AJ616027; CAE82297.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL023094; CAA18837.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161585; CAB80175.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86395.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM66125.1; -; Genomic_DNA.
DR PIR; T05278; T05278.
DR RefSeq; NP_001328041.1; NM_001342293.1.
DR RefSeq; NP_195184.2; NM_119624.3.
DR AlphaFoldDB; F4JLE5; -.
DR SMR; F4JLE5; -.
DR STRING; 3702.AT4G34580.1; -.
DR PaxDb; F4JLE5; -.
DR PRIDE; F4JLE5; -.
DR EnsemblPlants; AT4G34580.1; AT4G34580.1; AT4G34580.
DR EnsemblPlants; AT4G34580.2; AT4G34580.2; AT4G34580.
DR GeneID; 829610; -.
DR Gramene; AT4G34580.1; AT4G34580.1; AT4G34580.
DR Gramene; AT4G34580.2; AT4G34580.2; AT4G34580.
DR KEGG; ath:AT4G34580; -.
DR Araport; AT4G34580; -.
DR TAIR; locus:2139564; AT4G34580.
DR eggNOG; KOG1471; Eukaryota.
DR HOGENOM; CLU_014001_11_1_1; -.
DR InParanoid; F4JLE5; -.
DR OMA; CYEESTK; -.
DR OrthoDB; 1133487at2759; -.
DR PRO; PR:F4JLE5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JLE5; baseline and differential.
DR Genevisible; F4JLE5; AT.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0035619; C:root hair tip; IDA:UniProtKB.
DR GO; GO:0009932; P:cell tip growth; IMP:TAIR.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0010053; P:root epidermal cell differentiation; IMP:TAIR.
DR GO; GO:0048768; P:root hair cell tip growth; IMP:UniProtKB.
DR GO; GO:0048767; P:root hair elongation; IMP:UniProtKB.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR011074; CRAL/TRIO_N_dom.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF03765; CRAL_TRIO_N; 1.
DR SMART; SM01100; CRAL_TRIO_N; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF46938; SSF46938; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Coiled coil; Golgi apparatus; Membrane; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..554
FT /note="Phosphatidylinositol/phosphatidylcholine transfer
FT protein SFH1"
FT /id="PRO_0000423461"
FT DOMAIN 130..304
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT COILED 498..539
FT /evidence="ECO:0000255"
SQ SEQUENCE 554 AA; 63287 MW; 4FCD1087B4E7BAA4 CRC64;
MAETKPEIEM SEEERKIVKI SSLKKKAINA SNRFKNSFKK KGRRSSSRVM SVPIEDDIDA
EDLQALDAFR QALILDELLP SKLDDLHMML RFLRARKFDI EKAKQMWSDM IQWRKDFGAD
TIIEDFDFEE IDEVMKHYPQ GYHGVDKEGR PVYIERLGQI DANKLLQVTT MDRYVKYHVK
EFEKTFKVKF PSCSVAANKH IDQSTTILDV QGVGLKNFSK SARELLQRLC KIDNENYPET
LNRMFIINAG SGFRLLWSTV KSFLDPKTTA KIHVLGNKYH SKLLEVIDAS ELPEFFGGAC
TCEDKGGCMR SDKGPWNDPE VLKIAINREA KCSPISEDEH KHVDQGRSTS GFESLERIKK
KTDEDNVYEK QIATIDKSMD MAWLAKTQKA ENFPISKGLE CYVRKGAPKK GDGLLVGGVM
AFVMGIVAMV RLSKDVPRKL TEAALYGNSV CYEESTKSKQ NQGQFAAPVS SSEYMLMVKR
MAELEDKCMF LDLKPAHVES EKEEKLQAAL NRVQVLEQEL TETKKALEEA LVSQKEILAY
IEKKKKKKKL FFGF
