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Database: UniProt
Entry: B0DAP0_LACBS
LinkDB: B0DAP0_LACBS
Original site: B0DAP0_LACBS 
ID   B0DAP0_LACBS            Unreviewed;       767 AA.
AC   B0DAP0;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   08-NOV-2023, entry version 65.
DE   RecName: Full=Protein transport protein SEC23 {ECO:0000256|RuleBase:RU365030};
GN   ORFNames=LACBIDRAFT_294379 {ECO:0000313|EMBL:EDR08060.1};
OS   Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS   (Laccaria laccata var. bicolor).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX   NCBI_TaxID=486041 {ECO:0000313|Proteomes:UP000001194};
RN   [1] {ECO:0000313|EMBL:EDR08060.1, ECO:0000313|Proteomes:UP000001194}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 / ATCC MYA-4686 {ECO:0000313|Proteomes:UP000001194};
RX   PubMed=18322534; DOI=10.1038/nature06556;
RA   Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA   Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA   Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA   Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA   DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA   Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA   Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA   Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA   Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA   Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA   Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA   Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA   Tuskan G., Grigoriev I.V.;
RT   "The genome of Laccaria bicolor provides insights into mycorrhizal
RT   symbiosis.";
RL   Nature 452:88-92(2008).
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|RuleBase:RU365030}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU365030}.
CC       Cytoplasmic vesicle, COPII-coated vesicle membrane
CC       {ECO:0000256|ARBA:ARBA00004299, ECO:0000256|RuleBase:RU365030};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004299,
CC       ECO:0000256|RuleBase:RU365030}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004299, ECO:0000256|RuleBase:RU365030}.
CC       Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004397,
CC       ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004397, ECO:0000256|RuleBase:RU365030};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004397,
CC       ECO:0000256|RuleBase:RU365030}. Golgi apparatus membrane
CC       {ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein
CC       {ECO:0000256|RuleBase:RU365030}; Cytoplasmic side
CC       {ECO:0000256|RuleBase:RU365030}. 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. SEC23 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009210, ECO:0000256|RuleBase:RU365030}.
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DR   EMBL; DS547102; EDR08060.1; -; Genomic_DNA.
DR   RefSeq; XP_001881130.1; XM_001881095.1.
DR   AlphaFoldDB; B0DAP0; -.
DR   STRING; 486041.B0DAP0; -.
DR   GeneID; 6076668; -.
DR   KEGG; lbc:LACBIDRAFT_294379; -.
DR   HOGENOM; CLU_008658_3_0_1; -.
DR   InParanoid; B0DAP0; -.
DR   OrthoDB; 5474700at2759; -.
DR   Proteomes; UP000001194; 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:0090114; P:COPII-coated vesicle budding; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   CDD; cd01478; Sec23-like; 1.
DR   CDD; cd11287; Sec23_C; 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; 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; PROTEIN TRANSPORT PROTEIN SEC23; 1.
DR   PANTHER; PTHR11141:SF0; PROTEIN TRANSPORT PROTEIN SEC23; 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|RuleBase:RU365030};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW   ECO:0000256|RuleBase:RU365030};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU365030};
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW   ECO:0000256|RuleBase:RU365030};
KW   Golgi apparatus {ECO:0000256|RuleBase:RU365030};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365030};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU365030};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|RuleBase:RU365030};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001194};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365030};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365030}.
FT   DOMAIN          54..93
FT                   /note="Zinc finger Sec23/Sec24-type"
FT                   /evidence="ECO:0000259|Pfam:PF04810"
FT   DOMAIN          122..389
FT                   /note="Sec23/Sec24 trunk"
FT                   /evidence="ECO:0000259|Pfam:PF04811"
FT   DOMAIN          400..502
FT                   /note="Sec23/Sec24 beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF08033"
FT   DOMAIN          515..613
FT                   /note="Sec23/Sec24 helical"
FT                   /evidence="ECO:0000259|Pfam:PF04815"
FT   DOMAIN          627..715
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
SQ   SEQUENCE   767 AA;  85648 MW;  BF49DBBB094B8F38 CRC64;
     MLNFEDVEER DGVRLSWNVW PSSRIEATRT VVPISALYTP LKIREDLPPV LYEPVACKPP
     CRAILNPYCQ IDIRGKLWIC PFCLSRNAFP PHYKDISNTN LPAELLPKYT TIEYTLARPV
     QVPPIFLFVV DTCLDEEDLK ALRDAIVVSL SLIPPYALVG LITFGTMTQV HEIGYAECSK
     SYVFRGGKEY QPKQIQDMLG LTSQNRAAPR PGQPMPQQSF GAARFLMPVQ QCEFQLTGIL
     ESLTRDPWPV ANDKRALRCT GVAVSVAVGL LETTYPNTGA RIVVFAGGPA TEGPGMVVSN
     ELKEPIRSHH DIDRDSVKHY KRAIKLLIFY EALAKRASNN GHAIDLFAGC LDQVGLLEMK
     SLPNSTNGVI VLSDSFATSI FKQSFLRMFN KDDQGHLHMG FNATFDVQTT KELKVSGMIG
     HGISAGKKSA CVGETEIGIG QTSAWKINAV NPHTATAVYF EVVTPAGQPL QQGSRGLIQF
     VTHYQHSSGQ QRLRVTTIAR NFAEAGSPSI AASFDQEAAA VLMSRIAVFK AEIDDSPDVL
     RWLDRMLIRL CQKFADYRKE DPTSFRLTDN FSIYPQFMFH LRRSQFLQVF NNSPDETAFY
     RHILNEEDVN NSLIMIQPTL MSYTFDTPPQ PVLLDSVSIK HDVVLLLDTF FHILIFHGEL
     VAQWRKQGYQ DQEGYENFKE LLELPVADAQ DLLVDRFPIP RYIVCDQGGS QARFLLSKLN
     PSTTHMSATM YGSTPGPGAG QAIFTDDVSL QVFMEHLKRL AVGAQTN
//
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