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Database: UniProt
Entry: A0A2T3B1F3_AMORE
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Original site: A0A2T3B1F3_AMORE 
ID   A0A2T3B1F3_AMORE        Unreviewed;       772 AA.
AC   A0A2T3B1F3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Protein transport protein SEC23 {ECO:0000256|ARBA:ARBA00021212, ECO:0000256|RuleBase:RU365030};
GN   ORFNames=M430DRAFT_139551 {ECO:0000313|EMBL:PSS18390.1};
OS   Amorphotheca resinae ATCC 22711.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Amorphothecaceae; Amorphotheca.
OX   NCBI_TaxID=857342 {ECO:0000313|EMBL:PSS18390.1, ECO:0000313|Proteomes:UP000241818};
RN   [1] {ECO:0000313|EMBL:PSS18390.1, ECO:0000313|Proteomes:UP000241818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22711 {ECO:0000313|EMBL:PSS18390.1,
RC   ECO:0000313|Proteomes:UP000241818};
RX   PubMed=29315638; DOI=10.1111/nph.14974;
RA   Martino E., Morin E., Grelet G.A., Kuo A., Kohler A., Daghino S.,
RA   Barry K.W., Cichocki N., Clum A., Dockter R.B., Hainaut M., Kuo R.C.,
RA   LaButti K., Lindahl B.D., Lindquist E.A., Lipzen A., Khouja H.R.,
RA   Magnuson J., Murat C., Ohm R.A., Singer S.W., Spatafora J.W., Wang M.,
RA   Veneault-Fourrey C., Henrissat B., Grigoriev I.V., Martin F.M., Perotto S.;
RT   "Comparative genomics and transcriptomics depict ericoid mycorrhizal fungi
RT   as versatile saprotrophs and plant mutualists.";
RL   New Phytol. 217:1213-1229(2018).
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|ARBA:ARBA00025471,
CC       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; KZ679011; PSS18390.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T3B1F3; -.
DR   STRING; 857342.A0A2T3B1F3; -.
DR   InParanoid; A0A2T3B1F3; -.
DR   OrthoDB; 5474700at2759; -.
DR   Proteomes; UP000241818; 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|ARBA:ARBA00023034,
KW   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:UP000241818};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365030};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365030}.
FT   DOMAIN          60..99
FT                   /note="Zinc finger Sec23/Sec24-type"
FT                   /evidence="ECO:0000259|Pfam:PF04810"
FT   DOMAIN          127..393
FT                   /note="Sec23/Sec24 trunk"
FT                   /evidence="ECO:0000259|Pfam:PF04811"
FT   DOMAIN          404..508
FT                   /note="Sec23/Sec24 beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF08033"
FT   DOMAIN          522..620
FT                   /note="Sec23/Sec24 helical"
FT                   /evidence="ECO:0000259|Pfam:PF04815"
FT   DOMAIN          637..723
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
SQ   SEQUENCE   772 AA;  85957 MW;  182C5E2ABFC1FFAB CRC64;
     MDIDALKEQW SEVEDRDGLR LSWNVFPSSR MEASRLVVPI GALYTPLKEK PDSPLLQFEP
     VVCKAPCRSV LNPFCQVDVR ARLWICPFCL SRNPLPPHYK DITANAIPPE LHPSNTTIEY
     RLSRPAPSAP IFLYVVDTCQ EEDSLNALKE SLVMSLSLLP ENALVGLVTF GTMAQVHEIG
     YTECPKSYVF RGSKDYSAKQ VQEMLGLTNP GLRPGMQQPG RPMAPMGPAA RFLLPVQQCE
     FQLTKALEQL QKDPWPVASD RRNLRCTGVA LSVAVGLLET SFQNAGGRIM LFAGGPATEG
     PGLVVGPELR EPIRSHHDID RDNIKYYKKA LKFYDNLAKR TAHNGHIIDI FAGCLDQVGL
     LEMKGLSNST GGHMVLTDSF TSSMFKQSFI RVFEKDADDN LLMGFNASLE VLTTKELKVT
     GLIGHAVSMN KKSTSVGETE CGIGNTCSWK MCGIDPSASY GIYFEIASQG GPAQHQQTPQ
     KGMMQFLTYY QHSSGQFHLR VTTVSRNLSG PAGDPAVAQS FDQEAAAVLM SRIAVFKAEV
     DDGPDVLRWV DRMLIRLCSR FADYRKDDPS SFRLEKNFTL YPQFMFHLRR SQFLQVFNNS
     PDETAFYRHV LNHEDVSNSL IMIQPTLDSY TFEQDGSQPV LLDSTSIQPT HILLLDTFFH
     ILIFHGETIA EWRKAGYQDQ EGYENFASLL EQPKEDARDL ITDRFPLPRF IVCDAGGSQA
     RFLLSKLNPS TTHTTGAYGG VGAQSAQTIF TDDVSLQTFM DHLMKLAVSG TN
//
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