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SEC16_KLULA
ID   SEC16_KLULA             Reviewed;        2082 AA.
AC   Q6CM10;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=COPII coat assembly protein SEC16;
DE   AltName: Full=Protein transport protein SEC16;
GN   Name=SEC16; OrderedLocusNames=KLLA0E23958g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Involved in the initiation of assembly of the COPII coat
CC       required for the formation of transport vesicles from the endoplasmic
CC       reticulum (ER) and the selection of cargo molecules. Also involved in
CC       autophagy (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SEC16 family. {ECO:0000305}.
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DR   EMBL; CR382125; CAH00116.1; -; Genomic_DNA.
DR   RefSeq; XP_455029.1; XM_455029.1.
DR   AlphaFoldDB; Q6CM10; -.
DR   SMR; Q6CM10; -.
DR   STRING; 28985.XP_455029.1; -.
DR   EnsemblFungi; CAH00116; CAH00116; KLLA0_E23915g.
DR   GeneID; 2894352; -.
DR   KEGG; kla:KLLA0_E23915g; -.
DR   eggNOG; KOG1913; Eukaryota.
DR   HOGENOM; CLU_000768_0_0_1; -.
DR   InParanoid; Q6CM10; -.
DR   OMA; ESHENGY; -.
DR   Proteomes; UP000000598; Chromosome E.
DR   GO; GO:0070971; C:endoplasmic reticulum exit site; IEA:UniProt.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0048208; P:COPII vesicle coating; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR024298; ACE1_Sec16_Sec31.
DR   InterPro; IPR024880; Sec16.
DR   InterPro; IPR024340; Sec16_CCD.
DR   PANTHER; PTHR13402; PTHR13402; 2.
DR   Pfam; PF12932; Sec16; 1.
DR   Pfam; PF12931; Sec16_C; 1.
PE   3: Inferred from homology;
KW   Autophagy; Endoplasmic reticulum; ER-Golgi transport; Membrane;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..2082
FT                   /note="COPII coat assembly protein SEC16"
FT                   /id="PRO_0000295538"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          281..450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          670..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          747..811
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..860
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1382..1472
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1520..1569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1650..1743
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1756..1787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1853..1920
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1955..2082
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..21
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..335
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        343..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        370..384
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..450
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..607
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        747..784
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        794..811
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1413..1434
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1446..1464
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1520..1566
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1650..1672
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1700..1737
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1761..1787
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1864..1908
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2026..2045
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2082 AA;  226997 MW;  510722B60D2A4D14 CRC64;
     MGPDAKKRKN QKKKLKLKQK RLHASNGSAD ESAIVPQTTD VHLESSAEAI GSVRSVNAQV
     SPQSEASQAD TPQLVHTEAI PDAVPEHNDL SDLFQQENND TIANEAAVFD SIVKEQAPDV
     PVVAAAFTND ANVGNVGTLN NAQHVSNEIT ASEKAPDSVI GSMPVEAQPS VINDPVEELF
     GNDDTVQTEG LPWQDQIIAE ELPSISAEVG RELPQQESIN DYDQQEQFPP LLHDEKNTVQ
     LDQSEREVAT IENFNEPLSQ VNDGRKAPNM VTLDALLDDD NDYLTSDNDT QGMEHEATPT
     ELVSGENSSP VQPVNDAIEK ATGDEDTDLF NSEGDDGAKE GLSWLNDQSN TQEIPSPSEE
     ATKFSFLEND DDLLDDDESL LDSDEEVIVP QPQTAQAPKK SYLPSASSPV PQSVKHSYHP
     QSNPYSPQAS SFSNSVSGQP PSFPQNPSSY TYPVASTVPA SVAPGIVKPK LINNSNSSQS
     SVSDVNELHK KLDEAKHRTD AYDFPLDLVK QEIKRGKPMH ITSPLPSIRQ PSFSSVASEK
     PLIQPPVRPQ PNNTKAPQKP FYAELPIPEL KPTRAAPIRI ASQNSFSGSS ALPSQPIAAQ
     SRRTSIDPPV NPYAPKKNVA VVNPTIAPNS VAYGINNVPS KGQNLQANIL SAPPRNTIVS
     PVGTIAHNPY TPSLKSTASS SIKETPYQPA QPRRNRVLTN ASADSAGSFN PGHIPPIPGV
     PSTESNIYSF PPQHLSTAAP TATDHLQTTF DSHNVPPVLS PTLSTTANNK KTHARSNSSI
     YAPAHHAHSS KYAPTVHPQF QQQQQQQHQQ QHQQQQQLQQ LQLLQQQQQQ QQQQQQLNGI
     PVGFPRSQVD SNYGYASQQN TNQPIASTFP IMDQSRNPSI QANGSYIVSR QFPIFHWGKS
     AKVVVGIPNT QDYISAVEPK LDSINVISND SILTLDKTLE QFPGPLIKGK SKSKDIAKWL
     DTYIEEKKLK GANDTCILLE LLKLRLDPSY SLKAVTNIIY DSSILLPYLS QPFIPKVAAP
     NAHKLDANSL IRVLTLLQTG AHDDALNLSL ALKDYAMALL LGSILGKEKW SSVVDQYLTQ
     EFEQSNERDI SSINLLATIF QVFIGNSKKV IDSFKQDPTK LEWSLNNWKL LIACILNNCE
     EVPANGKLSP IVVEFLLQFG ELLVSRGLVI AGSIAFIVAD IPMSEEPLIP FSSTTFEYIC
     CPNSFESLIL SEIYEFTYGQ KDPSFSGFTS LIPQKIIHAA GLSDYGLNSS STKYMDMAQS
     MLKSLPKNSE TTLKTLRYIE DLSNQLSSSN VGWLGKPKLS SVWGQLDKSF NKFIGGDTDI
     DESETAAIED KVFEKFTPTS SRNPSMADLS QAASYLTPAL NRSHINQLQS NNSSLIKSTT
     KILPASSLPS RETHSKYGPP PLRDMKPQSK IGELYGSHSN IEPLNSTASA RNTVHPSHFE
     EPDNYVNPSG ATSLGQKELP NSNSTPEPVL PPLAQVYPGY QIHHDLSDGN SSVSSGHRLY
     SKMGVPNQNT ASFCVPSPIV SPQSTKHQSS TSNKALPLEN LFDDTVTSGL TTESTQTGSN
     APPRFHENEQ HSVVDDIVEE IGNEIDAELD ELQHSEFSDD NNFESTEQNS ISGVEGSVSQ
     LNVTNQLPVA ENLQEEDKNQ VTDINVPVTQ AQPLNSFSPA SSISSKPSSL KNMSVDKAEP
     ANPYAPKNSF GVAPRTARKS YNPYSPSSIT ESHSMASLPQ TSTSPYNNDN NSAPVNETGG
     PEDLAMYAYG SYKLSGEDAK PQTIDSPNGQ KQEIENKTSS PPLNSFVPSN IGLGENLISV
     KSIGLPAHLQ NDSQTLPSSK IKDPVIRPVQ TSNFVPFIVS DTNTEEYYDD LVEDTEDEDE
     DEPISVKREI SERNSENQNQ KVKNDEDEDE VKTVSEDEAG KPDKKQKNES SGGWLGWFKK
     DSNEKKPIKA KLGHANNFYY DENLKRWVNK DATEEEKLKV ATPPPPPPVV KRKMSKTPEI
     KPRQGSVVGG PALRTAHAVM PTNPLTGKPL DPVKDFSDDA ETKSESPVSS KPPVSNTNVN
     LSGSKANGLD DLMALTGGVS SASSTRRKKK STRGYVNVME NL
 
 
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