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SEC23_DICDI
ID   SEC23_DICDI             Reviewed;         750 AA.
AC   Q54T59;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Protein transport protein SEC23;
GN   Name=sec23; ORFNames=DDB_G0281985;
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. SEC23 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000044; EAL66414.2; -; Genomic_DNA.
DR   RefSeq; XP_640392.2; XM_635300.2.
DR   AlphaFoldDB; Q54T59; -.
DR   SMR; Q54T59; -.
DR   STRING; 44689.DDB0235163; -.
DR   PaxDb; Q54T59; -.
DR   EnsemblProtists; EAL66414; EAL66414; DDB_G0281985.
DR   GeneID; 8623347; -.
DR   KEGG; ddi:DDB_G0281985; -.
DR   dictyBase; DDB_G0281985; sec23.
DR   eggNOG; KOG1986; Eukaryota.
DR   HOGENOM; CLU_008658_3_0_1; -.
DR   InParanoid; Q54T59; -.
DR   OMA; FPPHYAE; -.
DR   PhylomeDB; Q54T59; -.
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:Q54T59; -.
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:0005096; F:GTPase activator activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0090110; P:COPII-coated vesicle cargo loading; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   CDD; cd11287; Sec23_C; 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; IPR037364; Sec23.
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; IPR037550; Sec23_C.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   InterPro; IPR006895; Znf_Sec23_Sec24.
DR   InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR   PANTHER; PTHR11141; PTHR11141; 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; 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..750
FT                   /note="Protein transport protein SEC23"
FT                   /id="PRO_0000328077"
SQ   SEQUENCE   750 AA;  84701 MW;  5043203EA5C2B509 CRC64;
     MNFDQSEDRD GVRFSWNVWP TSRVEATKNL LVPLGCLYTP LHQSPEITQV PYPPLRCKGI
     CNAILNPYCT IAPPYKTWVC PFCLQHNQFP PHYAGISDLN RPAELLPHVT TIEYQLPTAE
     TPLPIYLFVV DVCVPDDELQ SLTDSLTMSL SLIPENSYVG LITFGSMVQL YELGFTSCPK
     SYVFRGDPPT NTFKIANLMQ KVGSPETMNL QSKRFLVPVS ECEFHLTSIL EEIQKDPCRV
     ASDKRPLRAT GMAFSVANAL LSTVASNMGG RIMAFIGGPA TTGPGLVVSE DLREPIRSHH
     EVIKGKTKYT SKAYQFYKSI GERSVASGHA IDIFSCSLDQ VGLYEMREMV KLTGGYMVLA
     DSFDHPMFTQ SFQKIFTRED NAFKMGYNAE VQVCTSMSLK VCGAIGHMSS RNNKTSCVGE
     NEIGIGGTSS WKVCALDQNS TFAFYFEIAN TQQNAPEQLG LVQFITSYQN SLGKQILRVS
     TIRREWVQHT MEQQQNITML ANGFDQETSA VLMARLAVFK AETEELPDIT RWLDKMLIKL
     VSKYADYRRD DPTSFKLVSN FSIYPHFMFH LRRSSFLQVF NSSPDESSFY RFMLNRENVS
     NSLIMIQPTL EKYSFSGPPH PEVLSASSIS IDSILLLDTF FHVLIFHGET IAQWRKAGYD
     KDPQHQNFRD LLQAPRDDAA HILKERFPYP RYIVCDQHSG EARFLLATID PNITHTSNTP
     QDPSKGEIVF TDDVNLHVFL EHLKKFAVQS
 
 
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