SEC24_DICDI
ID SEC24_DICDI Reviewed; 1013 AA.
AC Q54U61;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Protein transport protein SEC24;
GN Name=sec24; ORFNames=DDB_G0281255;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(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 sar1A or sar1B.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000040; EAL66924.1; -; Genomic_DNA.
DR RefSeq; XP_640915.1; XM_635823.1.
DR AlphaFoldDB; Q54U61; -.
DR SMR; Q54U61; -.
DR STRING; 44689.DDB0235165; -.
DR PaxDb; Q54U61; -.
DR EnsemblProtists; EAL66924; EAL66924; DDB_G0281255.
DR GeneID; 8622978; -.
DR KEGG; ddi:DDB_G0281255; -.
DR dictyBase; DDB_G0281255; sec24.
DR eggNOG; KOG1985; Eukaryota.
DR HOGENOM; CLU_004589_2_1_1; -.
DR InParanoid; Q54U61; -.
DR OMA; TFPRDQS; -.
DR PhylomeDB; Q54U61; -.
DR Reactome; R-DDI-204005; COPII-mediated vesicle transport.
DR Reactome; R-DDI-5694530; Cargo concentration in the ER.
DR Reactome; R-DDI-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR PRO; PR:Q54U61; -.
DR Proteomes; UP000002195; Chromosome 3.
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 Gene3D; 3.40.20.10; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
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 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 Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport;
KW Golgi apparatus; Membrane; Metal-binding; Protein transport;
KW Reference proteome; Transport; Zinc.
FT CHAIN 1..1013
FT /note="Protein transport protein SEC24"
FT /id="PRO_0000328078"
FT REGION 1..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..359
FT /note="Zinc finger-like"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 359
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1013 AA; 114803 MW; D565127A737C2B7A CRC64;
MTSKRQYPID QSNQLSQGQN PSPQQPLQQY PQQPYQPNPT YGNDTTQQWN QTPQQQQQPQ
QQNISPPQSQ NQNGVQNTIH TGGSKRVYPV DPQNETLLSS NFSNMNLSSQ QQQPLPQPTH
IPVPGPNTTT YNPYIQQPQQ QPQQQPQQQP QQPQQPQQQP QQQTQQPQTW NTSPPQTQQQ
PIQTFTPHIS PPQTQQQQPQ QTTPFQPMQP TQPSYSQPQQ TQPLPLPPMQ PSYNQQPYTQ
QPYTQQPYTQ QPGQQSQYQQ PQQQTPQQQA AVEQPVPTLE NLCPKPFMRL SMNAIPNHPS
ILNKVHIPLG LNIHPLAHDP QGPVPVVYSS IIRCRRCRTY INPFVTWLNG GGRWRCNMCE
NINDTPQDYF SPIDFTTGKR SDILNRPELQ KGCVEFLASS DYLVRPPQPP TYFFIVDVCY
ESIVSGMLNT AINAIKTTLG DLIEKSNGRA RFGIMTFDDS LHFYNLKSNP SNRPQMFVVT
DMDQVYVPPF EDFLVNLKDG LEVVENTLNI IQSMPRTQQK VESCLGSALK AAFSICERVG
GKLIVLQSYI PRGPLGKLSI RDYQPLLGTK KESTLLQPSN DGEFYKELAL SCTSQQLSVD
LFLFSNDYTD TASLGTLCQI TGGSMYYYPS FVASRDGQVF AANLIHSLTR DTAWEAVMRV
RTSRGLTINS YHGNYFLKTS DLLGLPTIDS DKTITLQMGI SDSIGQKYAS LQSALLYTHS
CGERRVRVFT ISIPVVSNYQ DLFRYADISV VTSLISKMAI DKALSSSLND ARDAIANKCV
EILQAFKAAS TSNPQANPAV TLSQNAPKLL LPETLKHLPL YVVSMVKSII FSSRTTHPDL
RAFHMQRMKT LDLNSCLNFF YPYFYSLLAP PNYQPPTTPN TPFVPHSFKL SSDELQRNGL
FAIVNGYTLY LFIGEQLPQP VFTDIFGVPD VSQLDINTFQ DLPILDNDHS RYARKVIELV
RNSYPEYLKM FVVKSTDRQR RPEFQSLLIE DRTPEGCSYY EFIIQLQSRI TQN
