SEC24_CHAGB
ID SEC24_CHAGB Reviewed; 947 AA.
AC Q2HH63;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Protein transport protein SEC24;
GN Name=SEC24; ORFNames=CHGG_00441;
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. 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; CH408029; EAQ92206.1; -; Genomic_DNA.
DR RefSeq; XP_001219662.1; XM_001219661.1.
DR AlphaFoldDB; Q2HH63; -.
DR SMR; Q2HH63; -.
DR STRING; 38033.XP_001219662.1; -.
DR EnsemblFungi; EAQ92206; EAQ92206; CHGG_00441.
DR GeneID; 4388273; -.
DR eggNOG; KOG1985; Eukaryota.
DR HOGENOM; CLU_004589_2_1_1; -.
DR InParanoid; Q2HH63; -.
DR OMA; TFPRDQS; -.
DR OrthoDB; 330236at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
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:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd01479; Sec24-like; 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; 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..947
FT /note="Protein transport protein SEC24"
FT /id="PRO_0000295484"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..296
FT /note="Zinc finger-like"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 947 AA; 103085 MW; 9BD39F23320BF413 CRC64;
MSAPHDGYGQ FPPQQPTEQP PYPDQGYANP ADAPPPAAGA PHAADHGKKK KRAYAAGAFD
VAAGGNAAVG GQVQGGGQFG APAPGYGGYP QPEAQPATYG AQPAAYGAQP QQPYGMPAPA
PAVGYQAPEP YYPSAGAPPV PGDVAGLASG MSAMNLGPGA HQQPQQVPAQ GRVGPLNQLY
PTDLLNQPFN VSELDLPPPP IILPPNSSVT PSPDANCLPK YVRSTVNAIP TTHSLLKKSK
LPLALIIQPY AALHDLDDPV PVVQDQVISR CRRCRSYINP FVTFLDHGHR WRCNMCNLTN
DVPQAFDWDA AAQKTVDRWQ RHELNHAVVE FVAPQEYMVR PPQPLVYLFL FDVSYAAVST
GLLATSARTI LDSLNRIPNA DRRTRLGFIA VDSSLHYFSV PKDSDENGET SMLVVSDLDE
PFLPVPQELL VPLTECRNSI ENFLTKLPEM FANNQNNGSC MGSALRAGHK LISPLGGKIV
VLSASLPNVG YGKLEMREDK KLLGTSKENG LLQTANSFYK SFAVECSKNQ VSIDMFLFSS
QYQDVASLSN LPRYTGGQTW FYPGWNAGRP EDAIKFASEF SDFLSSEIGL EAVLRVRATT
GLRMSTFYGN FFNRSSDLCA FPAFPRDQCY VVEVAIDENL TKNVVCLQTA VLHTTCNGER
RIRVMTLALP TTTNLADVYA SADQCAITTY YSHKAVEKAL GSGLDSARDM LQSKVTELLQ
TFRKELAGGS MGGGLQFPSN LRGLPALFLG LIKHVGLRKS AQIPSDLRSA ALCMLSTLPL
PLLMQYIYPR LYSLHDMPDN AGYPDPETSQ IVLPPPLNLS SERFVPFGLY LIDDGQTQFL
WVGRDAVPQL LVDVFGVTDR AQLRVGKGAL PELDNDFNER VRAVALKSRD HKAKGVGSII
VPHLYIVRED GEPSLKLWAQ TLLVEDRADQ GMSYQQWMGT LREKVST
