SEC24_CRYNJ
ID SEC24_CRYNJ Reviewed; 920 AA.
AC P0CR40; Q55X19; Q5KMW5; Q5KMW6;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Protein transport protein SEC24;
GN Name=SEC24; OrderedLocusNames=CNB00260;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
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. 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P0CR40-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P0CR40-2; Sequence=VSP_026926;
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE017342; AAW41460.1; -; Genomic_DNA.
DR EMBL; AE017342; AAW41461.1; -; Genomic_DNA.
DR RefSeq; XP_568767.1; XM_568767.1. [P0CR40-1]
DR RefSeq; XP_568768.1; XM_568768.1.
DR AlphaFoldDB; P0CR40; -.
DR SMR; P0CR40; -.
DR STRING; 5207.AAW41460; -.
DR PaxDb; P0CR40; -.
DR EnsemblFungi; AAW41460; AAW41460; CNB00260. [P0CR40-1]
DR EnsemblFungi; AAW41461; AAW41461; CNB00260. [P0CR40-2]
DR GeneID; 3255871; -.
DR KEGG; cne:CNB00260; -.
DR VEuPathDB; FungiDB:CNB00260; -.
DR eggNOG; KOG1985; Eukaryota.
DR InParanoid; P0CR40; -.
DR OMA; TFPRDQS; -.
DR OrthoDB; 330236at2759; -.
DR Proteomes; UP000002149; Chromosome 2.
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 CDD; cd01479; Sec24-like; 1.
DR CDD; cd00201; WW; 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; 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; IPR041742; Sec24-like_trunk_dom.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_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; PF00397; WW; 1.
DR Pfam; PF04810; zf-Sec23_Sec24; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF81811; SSF81811; 1.
DR SUPFAM; SSF82754; SSF82754; 1.
DR SUPFAM; SSF82919; SSF82919; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 3: Inferred from homology;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW Metal-binding; Protein transport; Reference proteome; Transport; Zinc.
FT CHAIN 1..920
FT /note="Protein transport protein SEC24"
FT /id="PRO_0000295486"
FT DOMAIN 5..39
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT REGION 248..273
FT /note="Zinc finger-like"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..63
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_026926"
SQ SEQUENCE 920 AA; 100353 MW; 1B9090AD674B5A44 CRC64;
MSQPIMLPQG WEARWDPQAN AYIYVDQSTG RSQWEVPLNP TFPTSPTPHA PPQRHGRRAY
PSAMYAHAYD TPAPHVGPPQ PVAGYAEQGT PQFITPGFEG QQPVQQPPYA AVDHVAGQFQ
QMNIAPGAAP VAGAAAGAYQ GAGYAEKQLH STKTKTVNLI GLQPDVAALD NPPPPALLPA
NASVTSSAHS QPDPSYQRCT LNAMPTTQSL LNKSKLPLAL VMAPYRSIRE TDNDPDVPVV
EDGVIARCRR CRAYINPFVT FIEGGNRWKC CMCGLSNEVP QLFDWDQRAE KPADRWARKE
LNHAVVEFVA PTEYMVRPPQ PPVYAFVIDV SSAAIQSGMV AVAARTILES LDSLPNADNR
TKVAIIAVST SLHFFSLPAD ATEAGMLVVP DLTDVFLPKP VDLLVNLTES RPAIESLLAK
LSDMFQDSHT VGSALGSGLQ AAHQLIGKIG GKIIALGASL PTIGEGVLKA RDDPKLLGTS
KESQLLNAGN NWYKTFAIEC SKNQVSVDMF LFSGTYTDVA TLGCLPRYTA GQTYLYPGFN
ASRSEDAIKF ATEFGKVLAM PIGLEAVIRV RASRGIRMSA FHGNFFIRST DLLALPVVPQ
DQNYVIELQI EDDIKGSFVV IQTAVLHTTC YGERRIRVIT QAMPTTDSIA ELYTSADQIA
LATYLANKAV ERSMSHSLDD ARNHVTNRLG EMLTVYKNQV TSAAGGASAQ LAVPENLLLL
PLLCCALTKH VGLREGASIP PDLRAYAQCL LTTLPCQTLI PYIHPRFYSL HNMPPEAGTI
GGDDGAMILP PALNLTSEKL ERHGLFLIED GQNIFLWVGH DAVPRLIQDV FDLASYHELQ
GGKYTLPRLD NPFSERVCNV VDKTREMRRG VYRPQLYVVK SDAEPALRSW ALSLLVEDRM
DRMSSYAQYL TTVKSKVNGS
