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SEC31_CHAGB
ID   SEC31_CHAGB             Reviewed;        1258 AA.
AC   Q2GVT8;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Protein transport protein SEC31;
GN   Name=SEC31; ORFNames=CHGG_07916;
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX   PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
CC   -!- FUNCTION: Component of the coat protein complex II (COPII) which
CC       promotes the formation of transport vesicles from the endoplasmic
CC       reticulum (ER). The coat has two main functions, the physical
CC       deformation of the endoplasmic reticulum membrane into vesicles and the
CC       selection of cargo molecules (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The COPII coat is composed of at least 5 proteins: the
CC       SEC23/24 complex, the SEC13/31 complex, and the protein SAR1. SEC13 and
CC       SEC31 make a 2:2 tetramer that forms the edge element of the COPII
CC       outer coat. The tetramer self-assembles in multiple copies to form the
CC       complete polyhedral cage. Interacts (via WD 8) with SEC13 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC       Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the WD repeat SEC31 family. {ECO:0000305}.
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DR   EMBL; CH408033; EAQ86663.1; -; Genomic_DNA.
DR   RefSeq; XP_001225572.1; XM_001225571.1.
DR   AlphaFoldDB; Q2GVT8; -.
DR   SMR; Q2GVT8; -.
DR   STRING; 38033.XP_001225572.1; -.
DR   PRIDE; Q2GVT8; -.
DR   EnsemblFungi; EAQ86663; EAQ86663; CHGG_07916.
DR   GeneID; 4394267; -.
DR   eggNOG; KOG0307; Eukaryota.
DR   HOGENOM; CLU_003033_2_0_1; -.
DR   InParanoid; Q2GVT8; -.
DR   OMA; NRYAPAP; -.
DR   OrthoDB; 100998at2759; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR024298; ACE1_Sec16_Sec31.
DR   InterPro; IPR040251; SEC31-like.
DR   InterPro; IPR009917; SRA1/Sec31.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR13923; PTHR13923; 2.
DR   Pfam; PF12931; Sec16_C; 1.
DR   Pfam; PF07304; SRA1; 1.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00320; WD40; 6.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport; Membrane;
KW   Protein transport; Reference proteome; Repeat; Transport; WD repeat.
FT   CHAIN           1..1258
FT                   /note="Protein transport protein SEC31"
FT                   /id="PRO_0000295434"
FT   REPEAT          6..46
FT                   /note="WD 1"
FT   REPEAT          65..109
FT                   /note="WD 2"
FT   REPEAT          117..157
FT                   /note="WD 3"
FT   REPEAT          161..201
FT                   /note="WD 4"
FT   REPEAT          204..247
FT                   /note="WD 5"
FT   REPEAT          251..291
FT                   /note="WD 6"
FT   REPEAT          294..334
FT                   /note="WD 7"
FT   REPEAT          375..403
FT                   /note="WD 8; interaction with SEC13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00221"
FT   REGION          470..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          792..1153
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..492
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        795..811
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        822..847
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..866
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        871..909
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        958..993
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1003..1139
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1258 AA;  134167 MW;  01A7F0982C5C4321 CRC64;
     MVRLREIPRT AAFAWSSGPN PLLVTGTRSG AVDADFSDET KLELWELNLD ALDQGLELQP
     VASISTESRF YDIAWGAPSD EHPRGVVAGA MEDGSLQLWD AAKLLAGEEA VMSRDTKHTG
     PIKALQFNPL RPQVLATAGS KGELFVWDTN DTSTAFRLGT AAAHDIDCVA WNRKVSNILA
     TGSAGGFVTV WDLKTKKASL TLNNNRKPVS AIAWDPTNST NLLTATSDDN TPLILLWNLR
     NSQAPEKTLQ GHDQGILSLS WCQQDPGLLI SCGKDNRTLV WNPQTGERYG EFPEATNWTF
     LTRFNPGNPN LVATASFDGK ITVQTLQNTN ASVAPAAQTN TDDDDFFAKA PTELQGASFS
     LTRAPIWFER PVGVSFGYGG KLITFKKNDT PAGQPRSSKI QISSFSVDSD IGSATEKFEE
     AYKRGDIGAI CDSNAADAQT EEEKADWQVL KALSESDGRT KILEYLGFAK DDEASTSPEE
     TEVAEPKEEP KETGLAPPQP NGDDAKKKHK RVTSMWGDLD EGDDFLSDLT PAKGAKTDQP
     FQLLGEGNTT EDRVTKAIIL GNFEKAVDIC LKEDRVADAF ILANCGGKEL VDKVQTSYLA
     QKKGTPSYLR LINSVIGKNL WDVVYNADLG NWKETMVTLC TFAEPSEFPD LCEALGDRIY
     ESGSRQDASF CYLVGSKLEK VVDIWVVELQ EAEQAGLQEA SNDSTFSIHA RSLQHFIEKV
     TVFRHVIKFA DDEKELTEGW KLGSLYDKYT QYADIVAAHG QLAVAQRYLD LLPTKFPAAE
     VARNRVRLAT QKVAPQAPQV AQRQTGPISR AASRGPTPMG YQQPASIPPV GPSHTNPYAP
     PAPVQPAASS SNPYAPSTTS QFTPAGASPY APAGYAPPHP APGGYGPPQT FTQPGAPAPP
     PPRNTGPPPK IHKDPGSWND VPMVTRPPVR KTTPSVAPIT APFGAQAGLQ SPLPTGPYQR
     GAPTPPPPPP KGSAPPRSVT SPPVGPPPAG PYGARPASVT SNTPSPYAPP PAAAAAGLPS
     PMVPPPAGRT ASPYNAPPAG PPPSNRYAPA PSAQPYGQGP TPTPLAPPPA NPYAPAPAAQ
     QPMAPPPQQY TAPPPQASRP PVGPPPMSGP PPAAGGPPPA ARAAPPQQTP PPPRAAATPP
     AARHPAGDRS HIPPDAQRMV ELLSQDMQRV ASKAPATFAP QVKDTQKRLG LLFDHLNNGE
     LVRPDTVEQL TAIAEAIAGK NYDAASKGQM EIFRDKVEEC GQWMVGLKRL ISMSKATP
 
 
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