SEC23_CRYNB
ID SEC23_CRYNB Reviewed; 763 AA.
AC P0CR39; Q55KV2; Q5KAM7;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Protein transport protein SEC23;
GN Name=SEC23; OrderedLocusNames=CNBJ2310;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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.
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. SEC23 subfamily.
CC {ECO:0000305}.
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DR EMBL; AAEY01000050; EAL18308.1; -; Genomic_DNA.
DR RefSeq; XP_772955.1; XM_767862.1.
DR AlphaFoldDB; P0CR39; -.
DR SMR; P0CR39; -.
DR EnsemblFungi; AAW45976; AAW45976; CNJ01150.
DR EnsemblFungi; EAL18308; EAL18308; CNBJ2310.
DR GeneID; 4938574; -.
DR KEGG; cnb:CNBJ2310; -.
DR VEuPathDB; FungiDB:CNBJ2310; -.
DR HOGENOM; CLU_008658_3_0_1; -.
DR Proteomes; UP000001435; Chromosome 10.
DR GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0090114; P:COPII-coated vesicle budding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd11287; Sec23_C; 1.
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; IPR037364; Sec23.
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; IPR037550; Sec23_C.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR006895; Znf_Sec23_Sec24.
DR InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR PANTHER; PTHR11141; PTHR11141; 1.
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; Transport;
KW Zinc.
FT CHAIN 1..763
FT /note="Protein transport protein SEC23"
FT /id="PRO_0000410281"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 763 AA; 85146 MW; 1E0D213B818EC233 CRC64;
MNFEDIEDKD GVRFSWNVWP SSRLEATRTV VPISALYTPL KEREDLPPVM YEPVTCKGSS
CKAILNPYCQ VDVRGKMWIC PFCLQRNPFP PHYHQDLSPN NLPPELLPKF TTIEYTLSRP
AQIPPIFLYV VDTCVDEDEL KALKETLVVS LSLLPPNALV GLITYGTMAM VHELAYADCP
KAYVFRGSKD YQPKQIADML GLNPSNRPIQ PVRPGQPMPA PAASKFLMPV QACEFQLTNI
LEQLQRDPWP VEQDKRPLRC TGVALSVAVS LLETAFPNTG ARIMLFSGGP ATDGPGMVVG
PELREPIRSH HDIDRDSVKH FKRASKFYEA LSKRASVNGH AIDIYAGCLD QVGLLEMKSL
TNATNGVMTI SDSFMTAIFK QSFLRTLGKD EQGYLKMGFN ATYDVLTTKE LKISGVIGHV
ISANKKSSCV GETEIGIGQT SAWKVCSLTP KSTLATYFEV VTPAGQALTP NQSGLIQFVT
HYQHSSGQYR LRVTTVSRVF QEGGHPSIAA SFDQEAAAVL MARIAVFKAE IDDSPDVLRW
LDRMLIRLCQ KFADYRKEDP TSFQLSPNFS IYPQFMFHLR RSQFLQVFNN SPDETAFYRH
VLNDSDVNNS LIMIQPTLMS YGFDSEPHPV LLDSVSIRPD VILLLDTFFH ILIFHGETIA
QWRKANYQEQ EDYANFKELL EAPIGDAQEL LEDRMPIPRY VVCDQGGSQA RFLLSKLNPS
TTHMSGSNYG AGPAGGQAIF TDDVSLQVFM EHLKRLAVGA STS
