ID F2PJ13_TRIEC Unreviewed; 1022 AA.
AC F2PJ13;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Transporter sec-24 {ECO:0000313|EMBL:EGE01880.1};
GN ORFNames=TEQG_00922 {ECO:0000313|EMBL:EGE01880.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC {ECO:0000256|ARBA:ARBA00008334}.
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DR EMBL; DS995720; EGE01880.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PJ13; -.
DR VEuPathDB; FungiDB:TEQG_00922; -.
DR eggNOG; KOG1984; Eukaryota.
DR HOGENOM; CLU_004589_1_0_1; -.
DR Proteomes; UP000009169; 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 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; 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:SF4; SECRETORY 24CD, ISOFORM C; 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 Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 295..333
FT /note="Zinc finger Sec23/Sec24-type"
FT /evidence="ECO:0000259|Pfam:PF04810"
FT DOMAIN 373..624
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 632..714
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 728..828
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT DOMAIN 855..929
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT REGION 1..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1022 AA; 111599 MW; CC9540A8B2CFE5E8 CRC64;
MTDFSMYHNL GDGAVPDDER MKSQIRTEPA APQFVPPVAQ PPSGYMQSGG APQQAYQHPH
GFTQSSPYPP SSAGYPSPQG NVQSSADMQS GMHNLTAQMG ALGVAGGGPP SSAGGTTRAH
KKKDRHAYHE FGAPAGSSQA FNGMPPGSTQ QPSQFLNQQS PQVAPPHGGF GSPQVQQQRN
SSVVGDGSVP TQGRVDPEQI PSVPRSRDVP AQYYLEHTYP TMERHVPPPS TVPFVAHDQG
NSSPKFARLT INNIPSTAEA LASTSLPLGL ILQPLAPLDE AEQPVPVLDF GDSGPLRCRR
CRAYINPFMT FRSGGNKFIC NMCTFPNEVA PEYYAPLDPS GVRVDRIHRP ELMQGTVEFL
VPKEYWNKEP VGLRWLFLLD VSQEAVSRGF LEACCDGLLS ALYGADGDGE EPESTEDGKS
KPCRNLPEGS KIGIITFDKE VHFYNLSPQL EQAQMIVMPD LEDPFVPLSE GLFADPYESK
HVISSLLTQI PTLFSFIKYP EPALLPTLNS ALSALESTGG KIVCSLSCLP TWGPGRLFMR
DQGMGPGTDA ERKLFTTEHV EWKKTATKAA ETGIGVDFFI AAGGGTYMDI ATIGHVSAVA
GGEMFFYPNF HAPRDIQKLS KEICHSITRE TGYQALLKVR CSNGLQISSY HGNFLQHTFA
SDLEMGSIDA DKAFGIMFTY DGKLDPKLDA HFQAALLYTA GNGQRRVRCI NIVAGVNDGG
METMKSLDQD AIVSILAKEA ASKVPEKALS EIRASLTEKS IDILASYRKN FSLSHPPGQL
VLPEYIQEFS MYMLSLLKSR AFKGGHEPSD RRIHDVRMLR SFGCRELSLY LYPRIIPIHN
LDPKDGFSNE HGQLQVPPSQ RASFSKIEDG GVYIVENGQI CILWIHALVS PNLLEDLFGP
GYNSLKSLDP NTSTIPVLET QLNAQVRNIL QYLSTVRGSK AMTIQLARQG IDGSEYEFAR
MLLEDRNNEA QSYVDWLVHL HRQINIELGG HRKKEDGSVA GAVGAGVEST LSGLAGLRPS
YW
//
