SFH12_ARATH
ID SFH12_ARATH Reviewed; 543 AA.
AC Q94A34; Q9SYY7;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Phosphatidylinositol/phosphatidylcholine transfer protein SFH12;
DE AltName: Full=Protein SEC FOURTEEN HOMOLOGS 12;
DE Short=AtSFH12;
GN Name=SFH12; OrderedLocusNames=At4g36490; ORFNames=AP22.26, C7A10.870;
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=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP GENE FAMILY.
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 TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND FUNCTION.
RX PubMed=16697077; DOI=10.1016/j.jplph.2006.03.014;
RA Mo P., Zhu Y., Liu X., Zhang A., Yan C., Wang D.;
RT "Identification of two phosphatidylinositol/phosphatidylcholine transfer
RT protein genes that are predominately transcribed in the flowers of
RT Arabidopsis thaliana.";
RL J. Plant Physiol. 164:478-486(2007).
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. {ECO:0000250,
CC ECO:0000269|PubMed:16697077}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in flowers.
CC {ECO:0000269|PubMed:16697077}.
CC -!- DEVELOPMENTAL STAGE: Detected in the mature and germinating pollen
CC grains. {ECO:0000269|PubMed:16697077}.
CC -!- SIMILARITY: Belongs to the SFH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB16843.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80315.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; Z99708; CAB16843.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161589; CAB80315.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86662.1; -; Genomic_DNA.
DR EMBL; AY050419; AAK91435.1; -; mRNA.
DR EMBL; BT000834; AAN33209.1; -; mRNA.
DR PIR; G85430; G85430.
DR RefSeq; NP_568006.1; NM_119812.4.
DR AlphaFoldDB; Q94A34; -.
DR SMR; Q94A34; -.
DR BioGRID; 15083; 2.
DR IntAct; Q94A34; 1.
DR STRING; 3702.AT4G36490.1; -.
DR PaxDb; Q94A34; -.
DR PRIDE; Q94A34; -.
DR ProteomicsDB; 234500; -.
DR EnsemblPlants; AT4G36490.1; AT4G36490.1; AT4G36490.
DR GeneID; 829801; -.
DR Gramene; AT4G36490.1; AT4G36490.1; AT4G36490.
DR KEGG; ath:AT4G36490; -.
DR Araport; AT4G36490; -.
DR TAIR; locus:2115265; AT4G36490.
DR eggNOG; KOG1471; Eukaryota.
DR HOGENOM; CLU_014001_11_1_1; -.
DR InParanoid; Q94A34; -.
DR OMA; SGMHKCT; -.
DR OrthoDB; 1133487at2759; -.
DR PhylomeDB; Q94A34; -.
DR PRO; PR:Q94A34; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94A34; baseline and differential.
DR Genevisible; Q94A34; AT.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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..543
FT /note="Phosphatidylinositol/phosphatidylcholine transfer
FT protein SFH12"
FT /id="PRO_0000423472"
FT DOMAIN 120..294
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REGION 316..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 490..526
FT /evidence="ECO:0000255"
SQ SEQUENCE 543 AA; 61826 MW; 2A14B52C613EA76B CRC64;
MTLIQDAELK PRMGSFKKRS SSKNLRYSMT KRRRSSKVMS VEIIEDVHDA EELKAVDAFR
QSLILDELLP EKHDDYHMML RFLKARKFDL EKTKQMWTEM LRWRKEFGAD TVMEEFDFKE
IDEVLKYYPQ GHHGVDKEGR PVYIERLGLV DSTKLMQVTT MDRYVNYHVM EFERTFNVKF
PACSIAAKKH IDQSTTILDV QGVGLKNFNK AARDLITRLQ KVDGDNYPET LNRMFIINAG
SGFRMLWNTV KSFLDPKTTA KIHVLGNKYQ SKLLEIIDES ELPEFLGGSC TCADNGGCMR
SDKGPWKNPE IMKRVHNGDH KCSKGSQAEN SGEKTIPEED DSTTEPASEE EKASKEVEIV
PAAHPAWNMP EAHKFSLSKK EVYAIQEACN NATTEGGRSP IFTGVMALVM GVVTMIKVTK
NVPRKLTEST LYSSPVYCDD ASMNKSAMQS EKMTVPAISG EDFMAIMKRM AELEQKVTVL
SAQPTVMPPD KEEMLNAAIS RSNVLEQELA ATKKALDDSL GRQEELVAYI EKKKKKKKLF
NYW
