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SEC24_CANAL
ID   SEC24_CANAL             Reviewed;         928 AA.
AC   Q5AQ76; A0A1D8PEG4; Q5APN4;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Protein transport protein SEC24;
GN   Name=SEC24; OrderedLocusNames=CAALFM_C108740CA;
GN   ORFNames=CaO19.12194, CaO19.4732;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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. Golgi
CC       apparatus membrane; Peripheral membrane protein; Cytoplasmic side.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle,
CC       COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic
CC       reticulum membrane {ECO:0000250}; Peripheral membrane protein
CC       {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC       side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP017623; AOW26511.1; -; Genomic_DNA.
DR   RefSeq; XP_723419.2; XM_718326.2.
DR   AlphaFoldDB; Q5AQ76; -.
DR   SMR; Q5AQ76; -.
DR   BioGRID; 1218033; 1.
DR   STRING; 237561.Q5AQ76; -.
DR   PRIDE; Q5AQ76; -.
DR   GeneID; 3634939; -.
DR   KEGG; cal:CAALFM_C108740CA; -.
DR   CGD; CAL0000196446; SEC24.
DR   VEuPathDB; FungiDB:C1_08740C_A; -.
DR   eggNOG; KOG1985; Eukaryota.
DR   HOGENOM; CLU_004589_2_1_1; -.
DR   InParanoid; Q5AQ76; -.
DR   OrthoDB; 330236at2759; -.
DR   PRO; PR:Q5AQ76; -.
DR   Proteomes; UP000000559; Chromosome 1.
DR   GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central.
DR   GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0090110; P:COPII-coated vesicle cargo loading; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   Gene3D; 3.40.20.10; -; 1.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR007123; Gelsolin-like_dom.
DR   InterPro; IPR036180; Gelsolin-like_dom_sf.
DR   InterPro; IPR006900; Sec23/24_helical_dom.
DR   InterPro; IPR036175; Sec23/24_helical_dom_sf.
DR   InterPro; IPR006896; Sec23/24_trunk_dom.
DR   InterPro; IPR012990; Sec23_24_beta_S.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   InterPro; IPR006895; Znf_Sec23_Sec24.
DR   InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR   Pfam; PF00626; Gelsolin; 1.
DR   Pfam; PF08033; Sec23_BS; 1.
DR   Pfam; PF04815; Sec23_helical; 1.
DR   Pfam; PF04811; Sec23_trunk; 1.
DR   Pfam; PF04810; zf-Sec23_Sec24; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   SUPFAM; SSF81811; SSF81811; 1.
DR   SUPFAM; SSF82754; SSF82754; 1.
DR   SUPFAM; SSF82919; SSF82919; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport;
KW   Golgi apparatus; Membrane; Metal-binding; Protein transport;
KW   Reference proteome; Transport; Zinc.
FT   CHAIN           1..928
FT                   /note="Protein transport protein SEC24"
FT                   /id="PRO_0000295481"
FT   REGION          1..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..256
FT                   /note="Zinc finger-like"
FT   COMPBIAS        24..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         231
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         234
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         253
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         256
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   928 AA;  102062 MW;  01CA22FA55AC16B9 CRC64;
     MSGRRRAYPQ PQYATGPAEM ATPPAPNQFQ QQQPVQQPVQ QYGVDQMQGQ FQQMNVGGVG
     PTGVPPAPQY SYQQPGQPQQ SPQLSYDPYQ PQPQANTGVY GQGMGGVPPS AVPAGGAGYG
     GYGQQNNIGL GAQLNALYTT DLSRDLPPPI AELSFQPPPI TLPDNATLIP ASKTANATPE
     YFRSTLNVVP TNSSLLKKSK LPLAIVVNPY NALKIENENV PVTCDTVISR CRRCRGYINP
     FVTLAENGRR WRCNFCNLLN DIPSAFDYDE ISGQVKNKFD RVELNHSVVE FIAPKEYMAR
     APQPIVYTFI IDVSVHAIQS GLTGTITRTI LESLDRIPNE NKTARVSFIG VDSNLHYIRF
     NEGLEGTEIL VVADIDEPFL PSPGGLLVNL DENREAIEKL LLDFPSYFEN NANQGFALGP
     ALKAGHKMIS NIGGKLVCFA ATLPNIGEGK LSVRDEASVA GKAKEAKALL APADSFYKSF
     AVTCNSSQVT VDLFLTSSAY QDVATLSNLA RYTAGQTHFY PAWTSNKYED VAKLSKEVSD
     HLSQDIALEA VLRVRGSTGF RMSSFYGNFF NRSSDLCSFP TFPRDQSYLI EMSIEETINK
     PVVYFQAAVL HSTCFGERRI RVMNLALPTS SKLVDIYASA DQLAIANYFT HKAIEKALSS
     SLPEAREYLI ARVVDILNVY RKELVAGNVS GASPLQISTN LRMLPLLLFC LTKHLAFRGE
     RVPSDHRAAA LNNLGSSPIP QLIKSIYPTV YSLHNMPDTC GLPGVKEDED DEEGAGAEID
     VVLPDPINDS KASWENYGLY LIDNGSELFL WVSGNVVPGL VQDLFGTENL YEIPTGKTEL
     PEFSLEESEF NYRVRQIIGK IREQNDSIIW KNLYVVVGAS SNEPIEISQQ RDLMALRMWA
     SSCLVEDKTG SEPSYRDFLT SLKSKVSQ
 
 
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