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SCAM3_ARATH
ID   SCAM3_ARATH             Reviewed;         289 AA.
AC   Q9M5P2; O22722;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Secretory carrier-associated membrane protein 3;
DE            Short=AtSC3;
DE            Short=Secretory carrier membrane protein 3;
GN   Name=SCAMP3; Synonyms=SC3; OrderedLocusNames=At1g61250; ORFNames=F11P17.4;
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 [MRNA], GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=10982391; DOI=10.1091/mbc.11.9.2933;
RA   Hubbard C., Singleton D., Rauch M., Jayasinghe S., Cafiso D., Castle D.;
RT   "The secretory carrier membrane protein family: structure and membrane
RT   topology.";
RL   Mol. Biol. Cell 11:2933-2947(2000).
RN   [2]
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   [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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=15060130; DOI=10.1074/mcp.m400001-mcp200;
RA   Marmagne A., Rouet M.-A., Ferro M., Rolland N., Alcon C., Joyard J.,
RA   Garin J., Barbier-Brygoo H., Ephritikhine G.;
RT   "Identification of new intrinsic proteins in Arabidopsis plasma membrane
RT   proteome.";
RL   Mol. Cell. Proteomics 3:675-691(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
CC   -!- FUNCTION: Probably involved in membrane trafficking. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15060130};
CC       Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle,
CC       secretory vesicle membrane {ECO:0000250}; Multi-pass membrane protein
CC       {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=Q9M5P2-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the SCAMP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB71471.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF225920; AAF36686.1; -; mRNA.
DR   EMBL; AC002294; AAB71471.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002684; AEE33811.1; -; Genomic_DNA.
DR   EMBL; AY045788; AAK76462.1; -; mRNA.
DR   EMBL; AY079336; AAL85067.1; -; mRNA.
DR   EMBL; AY086742; AAM63793.1; -; mRNA.
DR   RefSeq; NP_176320.1; NM_104806.4. [Q9M5P2-1]
DR   AlphaFoldDB; Q9M5P2; -.
DR   SMR; Q9M5P2; -.
DR   BioGRID; 27641; 10.
DR   IntAct; Q9M5P2; 7.
DR   STRING; 3702.AT1G61250.1; -.
DR   iPTMnet; Q9M5P2; -.
DR   SwissPalm; Q9M5P2; -.
DR   PaxDb; Q9M5P2; -.
DR   PRIDE; Q9M5P2; -.
DR   ProteomicsDB; 232792; -. [Q9M5P2-1]
DR   EnsemblPlants; AT1G61250.1; AT1G61250.1; AT1G61250. [Q9M5P2-1]
DR   GeneID; 842418; -.
DR   Gramene; AT1G61250.1; AT1G61250.1; AT1G61250. [Q9M5P2-1]
DR   KEGG; ath:AT1G61250; -.
DR   Araport; AT1G61250; -.
DR   TAIR; locus:2008465; AT1G61250.
DR   eggNOG; KOG3088; Eukaryota.
DR   HOGENOM; CLU_066546_3_0_1; -.
DR   InParanoid; Q9M5P2; -.
DR   OMA; IAITIGW; -.
DR   OrthoDB; 995882at2759; -.
DR   PhylomeDB; Q9M5P2; -.
DR   PRO; PR:Q9M5P2; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9M5P2; baseline and differential.
DR   Genevisible; Q9M5P2; AT.
DR   GO; GO:0005768; C:endosome; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0055038; C:recycling endosome membrane; IBA:GO_Central.
DR   GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR   GO; GO:0032588; C:trans-Golgi network membrane; IBA:GO_Central.
DR   GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR   InterPro; IPR007273; SCAMP.
DR   PANTHER; PTHR10687; PTHR10687; 1.
DR   Pfam; PF04144; SCAMP; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Coiled coil; Cytoplasmic vesicle;
KW   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..289
FT                   /note="Secretory carrier-associated membrane protein 3"
FT                   /id="PRO_0000304902"
FT   TOPO_DOM        1..124
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        125..145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        261..289
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          55..93
FT                   /evidence="ECO:0000255"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
SQ   SEQUENCE   289 AA;  32613 MW;  CD4587B62C240F82 CRC64;
     MANRYDPNPF AEEEEVNPFA NARGVPPASN SRLSPLPPEP VGFDYGRTVD IPLDRAGTQD
     LKKKEKELQA KEAELKRREQ DLKRKEDAAA RAGIVIEVKN WPPFFPLIHH DIANEIPVHL
     QRLQYVTFAT YLGLVLCLFW NIIAVTTAWI KGEGVTIWLL ALIYFIAGVP GGYVLWYRPL
     YRAFRTDSAL SFGWFFLFYM LHIAFCVFAA VAPPVVFKGK SLAGILPAID VLSGQAIVGI
     FYFIGFAFFC LESVVSIWVI QQVYMYFRGS GKQDQMRREA ARGALRAAV
 
 
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