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Database: UniProt
Entry: S3D9B7_GLAL2
LinkDB: S3D9B7_GLAL2
Original site: S3D9B7_GLAL2 
ID   S3D9B7_GLAL2            Unreviewed;      1018 AA.
AC   S3D9B7;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=VWA-like protein {ECO:0000313|EMBL:EPE34290.1};
GN   ORFNames=GLAREA_09984 {ECO:0000313|EMBL:EPE34290.1};
OS   Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE34290.1, ECO:0000313|Proteomes:UP000016922};
RN   [1] {ECO:0000313|EMBL:EPE34290.1, ECO:0000313|Proteomes:UP000016922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX   PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA   Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA   Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT   "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT   the fungus Glarea lozoyensis.";
RL   BMC Genomics 14:339-339(2013).
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   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC       membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004397}. Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004255}.
CC   -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008334}.
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DR   EMBL; KE145356; EPE34290.1; -; Genomic_DNA.
DR   RefSeq; XP_008078225.1; XM_008080034.1.
DR   AlphaFoldDB; S3D9B7; -.
DR   STRING; 1116229.S3D9B7; -.
DR   GeneID; 19469031; -.
DR   KEGG; glz:GLAREA_09984; -.
DR   eggNOG; KOG1984; Eukaryota.
DR   HOGENOM; CLU_004589_1_0_1; -.
DR   OMA; INPFMTF; -.
DR   OrthoDB; 977017at2759; -.
DR   Proteomes; UP000016922; 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: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   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; 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   InterPro; IPR006895; Znf_Sec23_Sec24.
DR   InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR   PANTHER; PTHR13803; SEC24-RELATED PROTEIN; 1.
DR   PANTHER; PTHR13803:SF4; SECRETORY 24CD, ISOFORM C; 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   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016922};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          311..349
FT                   /note="Zinc finger Sec23/Sec24-type"
FT                   /evidence="ECO:0000259|Pfam:PF04810"
FT   DOMAIN          389..628
FT                   /note="Sec23/Sec24 trunk"
FT                   /evidence="ECO:0000259|Pfam:PF04811"
FT   DOMAIN          635..719
FT                   /note="Sec23/Sec24 beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF08033"
FT   DOMAIN          731..830
FT                   /note="Sec23/Sec24 helical"
FT                   /evidence="ECO:0000259|Pfam:PF04815"
FT   DOMAIN          859..904
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
FT   REGION          1..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1018 AA;  111395 MW;  3524A8A5144D5218 CRC64;
     MSDYQQYHSL AQGDPNDPRN QNRNAQQTPN QFQPPVAPSP YGQPGATYGQ GQVPQQPYGV
     PQASPYGAPQ DPGYFPNQGQ QPQDGGLAAQ MGGMSLGGGE VATYGRKKKK DRHAYHNVEA
     PSGSSAAFNG IPASGVPPSA YLNADPSTMP VGPNSQFMNQ PITPQMSQFP APVGAPFNPA
     VPVSPAEFAS RNGAAPDGFA TNIQASAQGA VDPDQVPSVP RSRDSLAPYY LKNQYPTFEH
     HIPPPASVSF IAFDQGNASP KFTRLTFNNI PSNAEALATT SLPLGLLLQP LAPLSAGEVA
     IPVLDFGDTG PPRCHRCRAY INPFMVFRSG GNKFVCNMCN YANDCPPEYF AATNPQGARV
     DREMRPELMR GTVEFLVPKE YWNKEPVGLR WLFLIDVGQE ALNKGFLESF CEGIMVALYG
     NDHNSEERKI PEGAKVGFVT FDKDIHFYNM NPVLEQAQMI CMPDIDDPFL PLSEGLFVDP
     YEAKSNITSL LTQLPALFSQ VKNPEPALLP TLTAALAALE KTGGKIVCSL SALPTWGPGR
     LFLRDDGKQH GDAEKKLFAT EHPGWKKMAE KMVAAGVGVD FFLAAPGGGY LDIATIGHVS
     ASTGGETFYY PNFVSPRDSA KLSQEIMHTV QRETGFQALM KVRCSNGLQV SSYHGNFVQH
     NFGADVEFGV IDADKAMGVM FSYDGKLDAK LDAHFQSALL YTTANGERRV RCSNVIASVS
     DSVMDCMKFV DQDAVYCLMA KEAASKMTTS TMKEIRGALT EKTVDIVAGY RKIRSGSHPP
     SELVLPENLK ELGMYILGLI KSRSFKGGQE PTDRRVHDMR MLKGMGALEL SLYLYPRMIP
     IHNLQPEDGF PDPETGHLRM PPSVRCSFSR VEEGGVYLID NGQNCYLWMH AQTSPNLIID
     LFGEDKDSLK ALDPYSSSLP VLPTHISAQV RNILEFLKTM RGSKALTIQL ARQGLDGAEY
     EFARLLVEDR NNEAQSYVDW LVHIHRHVQL ELTGQRKKDD GGDNSVISNF AGLRPPYW
//
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