SFH5_ARATH
ID SFH5_ARATH Reviewed; 612 AA.
AC Q8GXC6; Q9FWS5;
DT 18-SEP-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Phosphatidylinositol/phosphatidylcholine transfer protein SFH5;
DE AltName: Full=Protein SEC FOURTEEN HOMOLOGS 5;
DE Short=AtSFH5;
GN Name=SFH5; OrderedLocusNames=At1g75370; ORFNames=F1B16.10;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 [5]
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).
CC -!- FUNCTION: Required for transport of secretory proteins from the Golgi
CC complex. Catalyzes the transfer of phosphatidylinositol and
CC phosphatidylcholine between membranes in vitro (By similarity).
CC {ECO:0000250}.
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=Q8GXC6-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the SFH family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG13072.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC023754; AAG13072.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE35707.1; -; Genomic_DNA.
DR EMBL; AK118304; BAC42922.1; -; mRNA.
DR PIR; B96784; B96784.
DR RefSeq; NP_177670.2; NM_106191.5. [Q8GXC6-1]
DR AlphaFoldDB; Q8GXC6; -.
DR SMR; Q8GXC6; -.
DR BioGRID; 29092; 1.
DR STRING; 3702.AT1G75370.2; -.
DR iPTMnet; Q8GXC6; -.
DR PaxDb; Q8GXC6; -.
DR PRIDE; Q8GXC6; -.
DR EnsemblPlants; AT1G75370.1; AT1G75370.1; AT1G75370. [Q8GXC6-1]
DR GeneID; 843873; -.
DR Gramene; AT1G75370.1; AT1G75370.1; AT1G75370. [Q8GXC6-1]
DR KEGG; ath:AT1G75370; -.
DR Araport; AT1G75370; -.
DR eggNOG; KOG1471; Eukaryota.
DR HOGENOM; CLU_014001_11_1_1; -.
DR OMA; VSHIFRW; -.
DR PhylomeDB; Q8GXC6; -.
DR PRO; PR:Q8GXC6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GXC6; baseline and differential.
DR Genevisible; Q8GXC6; 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 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 Alternative splicing; Cell membrane; Coiled coil; Golgi apparatus;
KW Membrane; Protein transport; Reference proteome; Transport.
FT CHAIN 1..612
FT /note="Phosphatidylinositol/phosphatidylcholine transfer
FT protein SFH5"
FT /id="PRO_0000423465"
FT DOMAIN 155..329
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REGION 16..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 555..588
FT /evidence="ECO:0000255"
FT COMPBIAS 379..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 612 AA; 69956 MW; 5827E1F14C57A7EE CRC64;
MSGSLDRFAR PCFEGVSSND ERRERRSDFE VSEDEKKTRI GNFNFKKKAA KASSKLRHSL
KKKGSSRRRS SDRTFSLTIE DIHDVEELRA VDEFRNLLVS ENLLPPTLDD YHIMLRFLKA
RKFDIGKTKL MWSNMIKWRK DFGTDTIFED FEFEEFDEVL KYYPHGYHGV DKEGRPVYIE
RLGLVDPAKL MQVTTVERFI RYHVREFEKT VNIKLPACCI AAKRHIDSST TILDVQGVGF
KNFSKPARDL IIQLQKIDND NYPETLHRMF IINGGSGFKL VWATVKQFLD PKTVTKIHVI
GNKYQNKLLE IIDASQLPDF LGGTCTCADR GGCMRSDKGP WNDPEILKML QSGGPLCRHN
SALNSFSRVS SCDKPSFSGI KASDTSTAES GSEVEEMASP KVNRELRVPK LTPVCEDIRG
TAISYPTDSS EYDSPMVDKV VDVAWMAHEK PKASKGSEDT PDSGKIRTVT YIWRWLMMFF
VNLFTLLISL ALPQREGHSQ SESSVDGPNA RESRPPSPAF ATIAERNVFS SVVNRLGDLE
KQVETLHSKR HEMPREKEEL LNTAVYRVDA LEAELIATKK ALHEALMRQD DLLAYIDREE
DEKYHKKKKV CW
