SEC24_SCHPO
ID SEC24_SCHPO Reviewed; 926 AA.
AC Q9UUI5; P78800;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein transport protein sec24;
GN Name=sec24; ORFNames=SPAC22F8.08;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 586-926.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi
CC apparatus membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB52718.1; -; Genomic_DNA.
DR EMBL; D89149; BAA13811.1; -; mRNA.
DR PIR; T38198; T38198.
DR PIR; T42425; T42425.
DR RefSeq; NP_594731.1; NM_001020159.2.
DR AlphaFoldDB; Q9UUI5; -.
DR SMR; Q9UUI5; -.
DR BioGRID; 278098; 5.
DR IntAct; Q9UUI5; 1.
DR STRING; 4896.SPAC22F8.08.1; -.
DR iPTMnet; Q9UUI5; -.
DR MaxQB; Q9UUI5; -.
DR PaxDb; Q9UUI5; -.
DR PRIDE; Q9UUI5; -.
DR EnsemblFungi; SPAC22F8.08.1; SPAC22F8.08.1:pep; SPAC22F8.08.
DR GeneID; 2541601; -.
DR KEGG; spo:SPAC22F8.08; -.
DR PomBase; SPAC22F8.08; sec24.
DR VEuPathDB; FungiDB:SPAC22F8.08; -.
DR eggNOG; KOG1985; Eukaryota.
DR HOGENOM; CLU_004589_2_1_1; -.
DR InParanoid; Q9UUI5; -.
DR OMA; TFPRDQS; -.
DR PhylomeDB; Q9UUI5; -.
DR Reactome; R-SPO-204005; COPII-mediated vesicle transport.
DR Reactome; R-SPO-5694530; Cargo concentration in the ER.
DR Reactome; R-SPO-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR PRO; PR:Q9UUI5; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0030127; C:COPII vesicle coat; ISO:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IDA:PomBase.
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; ISO:PomBase.
DR GO; GO:0006886; P:intracellular protein transport; IC:PomBase.
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 2: Evidence at transcript level;
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..926
FT /note="Protein transport protein sec24"
FT /id="PRO_0000205162"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..281
FT /note="Zinc finger-like"
FT COMPBIAS 73..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 278
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 714
FT /note="G -> C (in Ref. 2; BAA13811)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 926 AA; 101904 MW; 318401DD61BB4D73 CRC64;
MSQEDAFYGK GSYGASSGNS NIPPQGFQPV YPVAGQLDNT APYVGAVAEG TAEGIVSNGE
YAVGAMGAAP TNIIGSVDQQ PPVSHTSHKS RRQYPAEVFE LTNTLAASPA PPSLSEPSYV
MARTPSSSPY PHDRAEVGTK SLSAQFGGMS LGADGAAAMP TNELVSVDLY NQTPEISDLT
SPPPPINLPL SYSATGAATS NCPPKYVRST INCVPTTNSL LKKSKIPFAL VIRPYTSLVE
EDDPVPVVTD TIISRCRRCR MYINPFSIFI DNGHRYRCNS CGIVNEVPQS YDWDSFRNVQ
RDRWQRPELN YAVVDFIAPQ EYMVRAPQPL VYVFLIDISF VSISSGMVGT ASRAILESLD
RIPNKEGRAK VAFIGVDSAL HFFSVSPGAE EATQLVVSDL EEPFLPRNQD LLLNLRECRQ
GIENLLERFQ SMFATTRDSS NALGPGLKAA HRLIENIGGK ICCLISSLPN VGVGKLELRE
DPKLLGTNRE SSLLHPNDSF YKSFAVECST SQVSVDMFLF SSQYQDVATL SCLPRYTSGK
TQFYHRWNAS RSEDALKFAS ELTNYLSMEI ELEAVMRVRG SNGLRMSSFY GNFFNRSSDL
CAFPSFPRDQ SYVVEVVIED TITKPFVSFQ TAMLHTTCNG ERRIRVLTIS LPTTNSMTDL
YASADQVAIA QYLTVRASEK ALSSTLNEAR DSIISKLVEI LEVYKKNLAG QNTGAAIPLQ
ISTNLRLLPL LCLALTKHTG FRRSSHISSD LRSIALCYLS TLPTPLLMRY IYPTLYSLHD
MPIEAGTVTE QGVVLPSALN LTSALLQSFG LYLVDTHIHQ FLYIGKDAVP QLLIDAFGVN
SLADLKAGRF TMPVIDNPLN VRINAILGKL RSLDKGSTIM PSLYLVRGDG DPQLRSWFFS
HFVEDRSENS PSYLQFLQTL KEKVRD
