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Database: UniProt
Entry: SFH3_ARATH
LinkDB: SFH3_ARATH
Original site: SFH3_ARATH 
ID   SFH3_ARATH              Reviewed;         548 AA.
AC   Q93ZE9; Q9SIK5;
DT   18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 126.
DE   RecName: Full=Phosphatidylinositol/phosphatidylcholine transfer protein SFH3;
DE   AltName: Full=Protein SEC FOURTEEN HOMOLOGS 3;
DE            Short=AtSFH3;
GN   Name=SFH3; OrderedLocusNames=At2g21540; ORFNames=F2G1.19, F3K23.30;
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;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=Q93ZE9-1; Sequence=Displayed;
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in flowers but also
CC       slightly detected in stems and immature siliques.
CC       {ECO:0000269|PubMed:16697077}.
CC   -!- DEVELOPMENTAL STAGE: First detected in the stigma papillae of the
CC       flowers at stage 11, and then in the pollen grains before and after
CC       fertilization. {ECO:0000269|PubMed:16697077}.
CC   -!- SIMILARITY: Belongs to the SFH family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD23650.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC006841; AAM15309.1; -; Genomic_DNA.
DR   EMBL; AC007119; AAD23650.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC07192.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC07193.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM61245.1; -; Genomic_DNA.
DR   EMBL; CP002685; ANM61247.1; -; Genomic_DNA.
DR   EMBL; AY057587; AAL14382.1; -; mRNA.
DR   EMBL; AK176420; BAD44183.1; -; mRNA.
DR   PIR; E84602; E84602.
DR   RefSeq; NP_001031389.1; NM_001036312.2. [Q93ZE9-1]
DR   RefSeq; NP_001318263.1; NM_001335761.1. [Q93ZE9-1]
DR   RefSeq; NP_001323475.1; NM_001335763.1. [Q93ZE9-1]
DR   RefSeq; NP_565514.1; NM_127726.2. [Q93ZE9-1]
DR   AlphaFoldDB; Q93ZE9; -.
DR   SMR; Q93ZE9; -.
DR   STRING; 3702.Q93ZE9; -.
DR   PaxDb; 3702-AT2G21540-1; -.
DR   ProteomicsDB; 232650; -. [Q93ZE9-1]
DR   EnsemblPlants; AT2G21540.1; AT2G21540.1; AT2G21540. [Q93ZE9-1]
DR   EnsemblPlants; AT2G21540.2; AT2G21540.2; AT2G21540. [Q93ZE9-1]
DR   EnsemblPlants; AT2G21540.4; AT2G21540.4; AT2G21540. [Q93ZE9-1]
DR   EnsemblPlants; AT2G21540.6; AT2G21540.6; AT2G21540. [Q93ZE9-1]
DR   GeneID; 816693; -.
DR   Gramene; AT2G21540.1; AT2G21540.1; AT2G21540. [Q93ZE9-1]
DR   Gramene; AT2G21540.2; AT2G21540.2; AT2G21540. [Q93ZE9-1]
DR   Gramene; AT2G21540.4; AT2G21540.4; AT2G21540. [Q93ZE9-1]
DR   Gramene; AT2G21540.6; AT2G21540.6; AT2G21540. [Q93ZE9-1]
DR   KEGG; ath:AT2G21540; -.
DR   Araport; AT2G21540; -.
DR   TAIR; AT2G21540; SFH3.
DR   eggNOG; KOG1471; Eukaryota.
DR   InParanoid; Q93ZE9; -.
DR   OMA; WKDDEVM; -.
DR   OrthoDB; 6048at2759; -.
DR   PhylomeDB; Q93ZE9; -.
DR   PRO; PR:Q93ZE9; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q93ZE9; baseline and differential.
DR   Genevisible; Q93ZE9; AT.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009908; P:flower development; IDA:TAIR.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd00170; SEC14; 1.
DR   Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR   Gene3D; 1.10.8.20; N-terminal domain of phosphatidylinositol transfer protein sec14p; 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   PANTHER; PTHR45657; CRAL-TRIO DOMAIN-CONTAINING PROTEIN YKL091C-RELATED; 1.
DR   PANTHER; PTHR45657:SF1; CRAL-TRIO DOMAIN-CONTAINING PROTEIN YKL091C-RELATED; 1.
DR   Pfam; PF00650; CRAL_TRIO; 1.
DR   Pfam; PF03765; CRAL_TRIO_N; 1.
DR   PRINTS; PR00180; CRETINALDHBP.
DR   SMART; SM01100; CRAL_TRIO_N; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR   SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Coiled coil; Golgi apparatus;
KW   Membrane; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..548
FT                   /note="Phosphatidylinositol/phosphatidylcholine transfer
FT                   protein SFH3"
FT                   /id="PRO_0000423463"
FT   DOMAIN          137..311
FT                   /note="CRAL-TRIO"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          465..530
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   548 AA;  62832 MW;  4AD38E72B779BA33 CRC64;
     MTDTMSAHMD RHNKLDYDGS EDEKKTKLCS LKKKAINASN KFKHSFTKRT RRNSRVMSVS
     IVDDIDLEEL QAVDAFRQAL ILDELLPSKH DDHHMMLRFL RARKFDLEKA KQMWTDMIHW
     RKEFGVDTIM EDFDFKEIDE VLKYYPQGYH GVDKDGRPVY IERLGQVDAT KLMQVTTIDR
     YVKYHVREFE KTFNIKLPAC SIAAKKHIDQ STTILDVQGV GLKSFSKAAR DLLQRIQKID
     SDNYPETLNR MFIINAGSGF RLLWSTVKSF LDPKTTAKIH VLGNKYQSKL LEIIDSNELP
     EFLGGNCTCA DKGGCMRSDK GPWNDPDIFK MVQNGEGKCP RKTLSNIEEK TISVDENTTM
     KSDSFAKNKF DAENTKFIPM IDKTVNASTW PTNLHKSNYP EPEDLYSAVK PSQRRGGEGY
     LFGGVMSLVM GLMTVVRLTK NMPRKLTEAA IYGGEVDKAE TTMVSNQEYM SMVKRMAELE
     EKCRSLDNQP AAFSPEKEQI LTAALSRVDE LELQLAQTKK TLEETMATQH VIMAYIDKKK
     KKKKFFGF
//
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