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Database: UniProt
Entry: A0A197JH36_9FUNG
LinkDB: A0A197JH36_9FUNG
Original site: A0A197JH36_9FUNG 
ID   A0A197JH36_9FUNG        Unreviewed;       763 AA.
AC   A0A197JH36;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   22-FEB-2023, entry version 22.
DE   RecName: Full=Protein transport protein SEC23 {ECO:0000256|RuleBase:RU365030};
GN   ORFNames=K457DRAFT_24126 {ECO:0000313|EMBL:OAQ24455.1};
OS   Linnemannia elongata AG-77.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC   Mortierellomycetes; Mortierellales; Mortierellaceae; Linnemannia.
OX   NCBI_TaxID=1314771 {ECO:0000313|EMBL:OAQ24455.1, ECO:0000313|Proteomes:UP000078512};
RN   [1] {ECO:0000313|EMBL:OAQ24455.1, ECO:0000313|Proteomes:UP000078512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AG-77 {ECO:0000313|EMBL:OAQ24455.1,
RC   ECO:0000313|Proteomes:UP000078512};
RG   DOE Joint Genome Institute;
RA   Uehling J., Gryganskyi A., Hameed K., Tschaplinski T., Misztal P., Wu S.,
RA   Desiro A., Vande Pol N., Du Z.-Y., Zienkiewicz A., Zienkiewicz K.,
RA   Morin E., Tisserant E., Splivallo R., Hainaut M., Henrissat B., Ohm R.,
RA   Kuo A., Yan J., Lipzen A., Nolan M., Labutti K., Barry K., Goldstein A.,
RA   Labbe J., Schadt C., Tuskan G., Grigoriev I., Martin F., Vilgalys R.,
RA   Bonito G.;
RT   "Genome sequencing reveals origins of a unique bacterial endosymbiosis in
RT   the earliest lineages of terrestrial Fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KV442094; OAQ24455.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A197JH36; -.
DR   STRING; 1314771.A0A197JH36; -.
DR   OrthoDB; 5474700at2759; -.
DR   Proteomes; UP000078512; 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:UP000078512};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365030};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365030}.
FT   DOMAIN          53..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..503
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          628..715
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
SQ   SEQUENCE   763 AA;  85247 MW;  587A34BE082CC1A1 CRC64;
     MNFEEIEDQD GIRFSFNAWP ASRIEATRTV VPIAALYTPL KEREDLPLIY YEPVTCKQHT
     CGAILNPYCQ IDPRGKLWIC PFCLHRNQFP AHYRDISNTN LPAELLAKHT TIEYTLARSA
     QVPPIFLYVV DTCVDEDDLK ALKDSLVVSL SLLPPHALVG LITYGTMTQV HELGYSECPK
     SYVFRGNKDY TSKQIQDMLG LSAQAARPQQ PVRPGQPAPF VPSGNSRFLL PIQQCEYTLS
     SILEQLQRDP WPVATDKRPQ RCTGVAMSVA VGLLEATYQN NGGRVMLFVG GAATEGPGMV
     VGTDLKEPLR SHHDIEKENV KHYKKASKFY EGLAKRASTN GHVIDIFAGC LDQVGLLEMK
     SMVNSTGGFM ILSDSFTTLI FKQSFQKMFE KDAEGNLKMG FNATLAVQTT KELKICGLIG
     HAVSANKKTA SVGETEIGIG NTSAWKMCSV TPKTTNGIYF EVVNQQGQSL QPGSRGLIQF
     VTHYQHSSGH FKLRVTTVAR SWAEGNSPII GQSFDQETAA VLMARIAVFK AEIDDGPDVL
     RWLDRMLIRL CQKFADYRKD EPQSFRLTEN FSIYPQFMFH LRRSQFLQVF NNSPDETAYN
     RHILNREDVN NSLIMIQPTL MSYGFEGEPQ PVLLDSVSVK PDSILLLDTF FYILIFHGET
     IAAWRKAGYQ DQAGYENFKE LLEAPVVSSQ ELLTERFPIP RYIVCDQNGS QARFLLSKLN
     PSTTHVSGGQ YGGPPAGQAI FTDDVSLQVF MEYLKKLVVA GTS
//
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