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Database: UniProt
Entry: A0A059LIF8_9CHLO
LinkDB: A0A059LIF8_9CHLO
Original site: A0A059LIF8_9CHLO 
ID   A0A059LIF8_9CHLO        Unreviewed;       441 AA.
AC   A0A059LIF8;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=Protein transport protein SEC23 {ECO:0000256|RuleBase:RU365030};
DE   Flags: Fragment;
GN   ORFNames=H632_c1547p0 {ECO:0000313|EMBL:KDD74127.1};
OS   Helicosporidium sp. ATCC 50920.
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC   Chlorellales; Chlorellaceae; Helicosporidium.
OX   NCBI_TaxID=1291522 {ECO:0000313|EMBL:KDD74127.1, ECO:0000313|Proteomes:UP000026042};
RN   [1] {ECO:0000313|EMBL:KDD74127.1, ECO:0000313|Proteomes:UP000026042}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 50920 {ECO:0000313|EMBL:KDD74127.1,
RC   ECO:0000313|Proteomes:UP000026042};
RX   PubMed=24809511;
RA   Pombert J.F., Blouin N.A., Lane C., Boucias D., Keeling P.J.;
RT   "A lack of parasitic reduction in the obligate parasitic green alga
RT   helicosporidium.";
RL   PLoS Genet. 10:E1004355-E1004355(2014).
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: Cytoplasmic vesicle, COPII-coated vesicle
CC       membrane {ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein
CC       {ECO:0000256|RuleBase:RU365030}; Cytoplasmic side
CC       {ECO:0000256|RuleBase:RU365030}. Endoplasmic reticulum membrane
CC       {ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein
CC       {ECO:0000256|RuleBase:RU365030}; Cytoplasmic side
CC       {ECO:0000256|RuleBase:RU365030}.
CC   -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily.
CC       {ECO:0000256|RuleBase:RU365030}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDD74127.1}.
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DR   EMBL; AYPS01001547; KDD74127.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059LIF8; -.
DR   STRING; 1291522.A0A059LIF8; -.
DR   OrthoDB; 5474700at2759; -.
DR   Proteomes; UP000026042; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
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   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; IPR036465; vWFA_dom_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   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.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU365030};
KW   Cytoplasmic vesicle {ECO:0000256|RuleBase:RU365030};
KW   Endoplasmic reticulum {ECO:0000256|RuleBase:RU365030};
KW   ER-Golgi transport {ECO:0000256|RuleBase:RU365030};
KW   Membrane {ECO:0000256|RuleBase:RU365030};
KW   Metal-binding {ECO:0000256|RuleBase:RU365030};
KW   Protein transport {ECO:0000256|RuleBase:RU365030};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026042};
KW   Transport {ECO:0000256|RuleBase:RU365030};
KW   Zinc {ECO:0000256|RuleBase:RU365030}.
FT   DOMAIN          2..67
FT                   /note="Sec23/Sec24 trunk"
FT                   /evidence="ECO:0000259|Pfam:PF04811"
FT   DOMAIN          81..186
FT                   /note="Sec23/Sec24 beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF08033"
FT   DOMAIN          199..297
FT                   /note="Sec23/Sec24 helical"
FT                   /evidence="ECO:0000259|Pfam:PF04815"
FT   DOMAIN          311..399
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KDD74127.1"
SQ   SEQUENCE   441 AA;  48446 MW;  983C50EAE916B690 CRC64;
     HWAAARRYYD GLGRALVASG QALDVYACSL DQVGLAEMRN AVELSGGLSV QCDSFSNPQF
     RDSLRRAVTP AGEDGGLGLA AHATLEVRCS KDIRVCGLLG PAAALPLDRK SPLVSDTPVG
     QAGTTRWRLN SLGPQTTVAS VFEITTPGGG GPSAAPQQLY LQFTTRYEHE GGGQRLRVTT
     LSRRWASGEA QADLIQGFDQ EAAAVLVARL AAHKMESEDD FDVTRWLDRS LIRLCARFGD
     YRRDDPDSFQ LRPQLAYFPQ FMFNFRRSQF CQVFGASPDE TAFARMLLNR ETVSEAVTML
     QPLLYAYAMG VQPEPVLLDV SSISPDRVLL LDAYFYVVVF HGATVAQWRK ANYQEQPEYA
     AFKQLLESPL AEAKGIVDRR FPVPRLTVCD QNGSQARFLL AKLNPSSTYQ STAALSSEVI
     MTDDVSLSVF TDHLKKLAVA S
//
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