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SPNS1_ARATH
ID   SPNS1_ARATH             Reviewed;         492 AA.
AC   Q6NMN6; O49546;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Probable sphingolipid transporter spinster homolog 1;
GN   OrderedLocusNames=At5g65687; ORFNames=F6H11.180;
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=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
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;
RA   Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT   "Arabidopsis cDNA clones.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
CC   -!- FUNCTION: Probable sphingolipid transporter that plays a central role
CC       in endosomes and/or lysosomes storage. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}. Lysosome membrane {ECO:0000250}; Multi-
CC       pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Spinster (TC
CC       2.A.1.49) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB10676.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAA16689.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AB010075; BAB10676.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL021684; CAA16689.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED98088.1; -; Genomic_DNA.
DR   EMBL; BT011621; AAS47627.1; -; mRNA.
DR   EMBL; BT014809; AAT41792.1; -; mRNA.
DR   PIR; T05899; T05899.
DR   RefSeq; NP_680469.1; NM_148164.5.
DR   AlphaFoldDB; Q6NMN6; -.
DR   SMR; Q6NMN6; -.
DR   BioGRID; 21939; 1.
DR   IntAct; Q6NMN6; 1.
DR   STRING; 3702.AT5G65687.1; -.
DR   TCDB; 2.A.1.49.5; the major facilitator superfamily (mfs).
DR   iPTMnet; Q6NMN6; -.
DR   PaxDb; Q6NMN6; -.
DR   PRIDE; Q6NMN6; -.
DR   ProteomicsDB; 228316; -.
DR   EnsemblPlants; AT5G65687.1; AT5G65687.1; AT5G65687.
DR   GeneID; 836697; -.
DR   Gramene; AT5G65687.1; AT5G65687.1; AT5G65687.
DR   KEGG; ath:AT5G65687; -.
DR   Araport; AT5G65687; -.
DR   TAIR; locus:504954889; AT5G65687.
DR   eggNOG; KOG1330; Eukaryota.
DR   HOGENOM; CLU_001265_55_3_1; -.
DR   InParanoid; Q6NMN6; -.
DR   OMA; IEYSAAW; -.
DR   OrthoDB; 891881at2759; -.
DR   PhylomeDB; Q6NMN6; -.
DR   PRO; PR:Q6NMN6; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q6NMN6; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   CDD; cd17328; MFS_spinster_like; 1.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR044770; MFS_spinster-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   PANTHER; PTHR23505; PTHR23505; 1.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Endosome; Glycoprotein; Lipid transport; Lysosome; Membrane;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..492
FT                   /note="Probable sphingolipid transporter spinster homolog
FT                   1"
FT                   /id="PRO_0000415369"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        169..189
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        348..368
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        372..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        407..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        442..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          472..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         472
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19245862"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        76
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        341
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        488
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   492 AA;  53509 MW;  A55F06C28D70C0F3 CRC64;
     MTRVGQRDSP AKEEAPPATK KRFLTPGRFV TILCIINLIN YVDRGVIASN GVNGSSKVCD
     AKGVCSAGTG IQGEFNLTNF EDGLLSSAFM VGLLVASPIF AGLSKRFNPF KLIGVGLTVW
     TIAVIGCGFS YNFWMIAVFR MFVGVGEASF ISLAAPYIDD SAPVARKNFW LGLFYMCIPA
     GVALGYVFGG YIGNHLGWRW AFYIEAIAMA VFVILSFCIK PPQQLKGFAD KDSKKPSTSI
     ETVAPTDAEA SQIKTKTPKS KNLVVLFGKD LKALFSEKVF IVNVLGYITY NFVIGAYSYW
     GPKAGFGIYK MKNADMIFGG LTIICGIIGT LGGSYVLDRI NATLSNTFKL LAASTLLGAA
     FCFTAFLMKN MYAFIALFAV GEILIFAPQA PVNFVCLHCV RPNLRPLSMA SSTVLIHILG
     DVPSSPLYGK MQDHLKNWRK STLIITSILF LAAIIWGIGI FMNSVDRSNE VSEDDEVEED
     KLESKTENST LA
 
 
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