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Database: UniProt
Entry: G0SB06_CHATD
LinkDB: G0SB06_CHATD
Original site: G0SB06_CHATD 
ID   G0SB06_CHATD            Unreviewed;       942 AA.
AC   G0SB06;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Protein transport protein SEC24 {ECO:0000256|ARBA:ARBA00021213};
DE   AltName: Full=Protein transport protein sec24 {ECO:0000256|ARBA:ARBA00013453};
GN   ORFNames=CTHT_0048450 {ECO:0000313|EMBL:EGS19386.1};
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS   (Thermochaetoides thermophila).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX   NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN   [1] {ECO:0000313|EMBL:EGS19386.1, ECO:0000313|Proteomes:UP000008066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC   {ECO:0000313|Proteomes:UP000008066};
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA   Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
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. {ECO:0000256|ARBA:ARBA00025471}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC       membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004397}. Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004255}.
CC   -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008334}.
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DR   EMBL; GL988044; EGS19386.1; -; Genomic_DNA.
DR   RefSeq; XP_006695208.1; XM_006695145.1.
DR   AlphaFoldDB; G0SB06; -.
DR   STRING; 759272.G0SB06; -.
DR   GeneID; 18258883; -.
DR   KEGG; cthr:CTHT_0048450; -.
DR   eggNOG; KOG1985; Eukaryota.
DR   HOGENOM; CLU_004589_2_1_1; -.
DR   OMA; AVECSKQ; -.
DR   OrthoDB; 977017at2759; -.
DR   Proteomes; UP000008066; 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; 2.60.40.1670; beta-sandwich domain of Sec23/24; 1.
DR   Gene3D; 1.20.120.730; Sec23/Sec24 helical domain; 1.
DR   Gene3D; 3.40.20.10; Severin; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 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   PANTHER; PTHR13803; SEC24-RELATED PROTEIN; 1.
DR   PANTHER; PTHR13803:SF39; SECRETORY 24AB, ISOFORM A; 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; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR   SUPFAM; SSF82754; C-terminal, gelsolin-like domain of Sec23/24; 1.
DR   SUPFAM; SSF81811; Helical domain of Sec23/24; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   SUPFAM; SSF82919; Zn-finger domain of Sec23/24; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          260..297
FT                   /note="Zinc finger Sec23/Sec24-type"
FT                   /evidence="ECO:0000259|Pfam:PF04810"
FT   DOMAIN          334..575
FT                   /note="Sec23/Sec24 trunk"
FT                   /evidence="ECO:0000259|Pfam:PF04811"
FT   DOMAIN          581..664
FT                   /note="Sec23/Sec24 beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF08033"
FT   DOMAIN          675..779
FT                   /note="Sec23/Sec24 helical"
FT                   /evidence="ECO:0000259|Pfam:PF04815"
FT   DOMAIN          806..878
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          96..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..110
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   942 AA;  102515 MW;  2CF7EF636D155C39 CRC64;
     MSAPYDGYGQ QQPYPDPAQA YGAPAPGVPA PEQQPHHHHH EQHKKKKRAY AAEAFEIGSG
     ANAAVGGQLP GGGQYGVPPA AAAAAAAPAY GAYPQPVQPE LPPQPQYGMP QPAAPVGGYQ
     PLEPYYPGAG ASSVGIVAGL AGGIANMSLG PSPSSQPTPA QQQRVGPLNQ LYPTDLLNQP
     FNVAELDLPP PPIILPPNCS VTPSPNANCN PKYVRSTLNA VPTSHSLLKK SKLPFALIIQ
     PYASLHDLDD PVPIVQDQVI SRCRRCRSYI NPFVTFLDNG HRWRCNMCNL TNDVPQAFDW
     DAAAQKPVDR WQRHELNYSV VEFVAPQEYM VRPPQPLVYL FLFDVSYAAV STGLLATSAR
     TILDSLNRIP NADRRTRLGF MAVDSALHYF VIPKDGEENA ETSMLVVSDL DEPFLPVPTE
     LLVPLTECRN NIEAFLTKLP DMFANNQSNG SAMGPALRSG HKLIAPLGGK LVVLTASLPN
     LGVGKLEMRE DKKLLGTSKE GSLLQTANSF YKSFAVECSK NQVSVDMFLF SSHYQDVASL
     SNLPRYTGGQ TWFYPGWNAG RPEDAIKFAS EFSDYLSSEI GLEAVLRVRA TTGLRMNAFY
     GNFFNRSSDL CAFPAFPRDQ CYVVEVAIDE TIQKNVICLQ TAVLHTTCNG ERRIRVLTLA
     LPTTNSLADV YASADQAAIT TYFTHKAVER ALSGSLDAAR DALQSKIIEL LTTFRKELGG
     GGGGALGAGL QFPANLRALP ALFLGLIKHV GLRKSAQIPS DLRSAALCLL STLPLPLLMQ
     YIYPRMYSLH DMPDNAGLPD PETSQIVLPP AVNLSAERMV SYGLYLIDDG QTQFLWVGRD
     AVPQLLIDVF GVSDRSQLRV GKGSVPELDN EFNERVRNVI LKSRDHRSRG VGSVTVPHLY
     IVREDGEPSL KLWAQTMLVE DRADQGVGLA QWMGILREKV SS
//
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