ID T0KMI0_COLGC Unreviewed; 1015 AA.
AC T0KMI0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
GN ORFNames=CGLO_06323 {ECO:0000313|EMBL:EQB53903.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB53903.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC -!- FUNCTION: Involved in the initiation of assembly of the COPII coat
CC required for the formation of transport vesicles from the endoplasmic
CC reticulum (ER) and the selection of cargo molecules. Also involved in
CC autophagy. {ECO:0000256|ARBA:ARBA00024687,
CC ECO:0000256|RuleBase:RU364101}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004397}.
CC -!- SIMILARITY: Belongs to the SEC16 family.
CC {ECO:0000256|ARBA:ARBA00005927, ECO:0000256|RuleBase:RU364101}.
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:EQB53903.1}.
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DR EMBL; AMYD01001281; EQB53903.1; -; Genomic_DNA.
DR AlphaFoldDB; T0KMI0; -.
DR STRING; 1237896.T0KMI0; -.
DR eggNOG; KOG1913; Eukaryota.
DR HOGENOM; CLU_012237_0_0_1; -.
DR OMA; HRYCEAI; -.
DR OrthoDB; 1361743at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IEA:UniProt.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0048208; P:COPII vesicle coating; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd09233; ACE1-Sec16-like; 1.
DR Gene3D; 1.25.40.1030; -; 1.
DR InterPro; IPR024298; ACE1_Sec16_Sec31.
DR InterPro; IPR024880; Sec16.
DR InterPro; IPR024340; Sec16_CCD.
DR PANTHER; PTHR13402; RGPR-RELATED; 1.
DR PANTHER; PTHR13402:SF6; SECRETORY 16, ISOFORM I; 1.
DR Pfam; PF12932; Sec16; 1.
DR Pfam; PF12931; Sec16_C; 1.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|RuleBase:RU364101};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU364101};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW ECO:0000256|RuleBase:RU364101}; Membrane {ECO:0000256|RuleBase:RU364101};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU364101};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530};
KW Transport {ECO:0000256|RuleBase:RU364101}.
FT DOMAIN 1..108
FT /note="Sec16 central conserved"
FT /evidence="ECO:0000259|Pfam:PF12932"
FT DOMAIN 169..472
FT /note="Ancestral coatomer element 1 Sec16/Sec31"
FT /evidence="ECO:0000259|Pfam:PF12931"
FT REGION 476..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 881..1015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..681
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..749
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..829
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..933
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1015 AA; 108023 MW; 93F18105B9243F07 CRC64;
MVTSFPKNVP RYGIGQTAPM IIRSPGEVHV KHIKDIQPLE ERLAKFPGPL KGKSKKKETV
AWLTAGIESL ERELPDISFQ TQLSHEHKRA VERVLLWKIL RVFVEFDGTL EATPAVDKAV
RDVLAPGLTV EEGEPTPGYG AVVSAEALQE SSVTQMKADA VDSSTMDHIR KHLLVGEREK
AVWAAVDKRL WGHAMLISNT VSPDLYKQVA QEFVRKEVNY PGHNNESVAA LYKVLSGNFD
DCVDELVPVH ARAGFQLMNT TSATGPAKDA TEGLDKWRET LGLVLSNRST DDVRALNALG
NLLSSYGRAE AAHICFLFGR KATIFGGLDD GTSNFVLVGA DHKTQGDQFA KETEALLLSE
VYEFGLSLSG TSPLSAGVPH LAAYKLQHAM TLAEYGLRDK ALQYCEAIAG SITAQTKRSP
YYHPILETAV ENLRARLKQA PKEESSSWIS KPSMNKVSDT VWSRFNKFVA GDENENAAAG
GSAEGAESGP FARIAGGTPT ISRSPSVSNF EPLYQGATPG FQVGSPPSAV PIPATRAASR
YAPTSGTPAL SSSYEPGSGY SPAPASVGRS SNELSRSPYE PNAGYMPAPA SIGRSSNEFS
RSPYEGGSYM PAPAPAGRTS NELSRSPYEP RNSMDSQHGN ANGGYMPQSL SGPSLGYTPP
TSAPAQPGAA PVSPLQPPAN SPYEPYGVSQ PSTIPSVEVE TQTGTQESND LSGSGYQPPS
YGYEPPSLVP SDEPQSQGQD STGSDGYQPP SFQPYGYEPP SYNPEPEADE EAEEPKRKPK
SFIDDDDDDI PGLKALRSTS EEKSKAEKDK ENEEMFKKAA EEDAKRAAAA QQQKKGWGFS
SWFGGKKEAI PDAAQPNKPI KAKLGEANNF VYDPELKRWV NKAAGADQAQ AKTATPPPPK
AGPRSMTGTP PPRIMTPPMG RASAPPGGPP VPDLAKTPSI ESLGGGPPGP RPPAMMRSVS
NTSAAGGPLS GPPSRPATSM SNASSIDDLL SAAGPRKPGA KKAKKGGRYV DVMAK
//
