ID A0A2C9WAM6_MANES Unreviewed; 1417 AA.
AC A0A2C9WAM6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
GN ORFNames=MANES_02G039800 {ECO:0000313|EMBL:OAY56720.1};
OS Manihot esculenta (Cassava) (Jatropha manihot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983 {ECO:0000313|EMBL:OAY56720.1, ECO:0000313|Proteomes:UP000091857};
RN [1] {ECO:0000313|EMBL:OAY56720.1, ECO:0000313|Proteomes:UP000091857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AM560-2 {ECO:0000313|Proteomes:UP000091857};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY56720.1};
RA Bredeson J.V., Prochnik S.E., Lyons J.B., Schmutz J., Grimwood J.,
RA Vrebalov J., Bart R.S., Amuge T., Ferguson M.E., Green R., Putnam N.,
RA Stites J., Rounsley S., Rokhsar D.S.;
RT "WGS assembly of Manihot esculenta.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU364101}.
CC -!- SIMILARITY: Belongs to the SEC16 family.
CC {ECO:0000256|ARBA:ARBA00005927, ECO:0000256|RuleBase:RU364101}.
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DR EMBL; CM004388; OAY56720.1; -; Genomic_DNA.
DR STRING; 3983.A0A2C9WAM6; -.
DR EnsemblPlants; OAY56720; OAY56720; MANES_02G039800.
DR Gramene; OAY56720; OAY56720; MANES_02G039800.
DR Proteomes; UP000091857; Chromosome lg2.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IEA:InterPro.
DR GO; GO:0048208; P:COPII vesicle coating; IEA:InterPro.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IBA:GO_Central.
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 Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU364101};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW ECO:0000256|RuleBase:RU364101};
KW Golgi apparatus {ECO:0000256|RuleBase:RU364101};
KW Membrane {ECO:0000256|RuleBase:RU364101};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU364101};
KW Reference proteome {ECO:0000313|Proteomes:UP000091857};
KW Transport {ECO:0000256|RuleBase:RU364101}.
FT DOMAIN 548..673
FT /note="Sec16 central conserved"
FT /evidence="ECO:0000259|Pfam:PF12932"
FT DOMAIN 735..1000
FT /note="Ancestral coatomer element 1 Sec16/Sec31"
FT /evidence="ECO:0000259|Pfam:PF12931"
FT REGION 53..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1169..1235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1307..1334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1352..1397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1182..1219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1417 AA; 154034 MW; F8C666A8E4C8C918 CRC64;
MASNPPFHVM EDQTDEDFFD KLVDDDFGPT NSNLVPKLTE GSDSDEAKAF ANLSIEDATG
EGRDEGKDES DLVHASAGLS SVLAEESDTL DSSLALVSNT KVDSNNDWIE SEVVSDPLIG
ETSGSTKSGV KEVGWGSFYA DSVPNGNHEF GAYSDFFNDL GNTAGDFPEQ AGEAANLEKK
DGDRLHSSVS SYGEYQEGTQ GYGGSIEESV NEQDLNSSQY WENMYPGWKF DANTGQWYQV
DNFDVTASVQ GSSNVNTGNE WAAVSDGKIQ MNYLQQTSHS VLGTVAEASS SESVSTWNQV
SQGINNGYPE HMFFDPQYPG WYYDTIVQEW RSLESYTSSV QSATVQNHDH QATVQNHHQQ
KQNEFACADL GSQNTNSIYA GYEQVDKHDS QGHNSQDKHR SWGESYGDYN QQGLNMWQPD
AVAKTDTVSD FGRNQQLLNS YDSNVSMNNH VEQHKPFNSL GSVLSYDNLS QGRVDSNGFI
GSQNFMPSES FGQQFNQGTV EQSKPMNISN DHYSSQKPIN FSQKSFHNLQ QLSYAPNAGM
SSAGRPPHAL VTFGFGGKLI VMKDSSSSSL TNASFASQEP VGGSIYVLNL MEVILGNDNN
ALNIRGSTCN YFHALCQQSF PGPLLGGNVG SKELNKWIDD RIANCESPDM DYRNGKVLKL
LLSLLKIACQ HYGKFRSPFG TDVSLKESEA PESAVAKLFA SAKRNGTEFS DYGALSRCLQ
SLPSEGQIQA TASEVQNLLV SGRKKEALQC AQIGQLWGPA LVLASQLGDQ FYVDTVKQMA
LRQLVAGSPL RTLCLLIAGQ PADVFSSDAT TGSGLPGAIS QQPIQFEANG MLDDWEENLA
VITANRTKDD ELVIIHLGDC LLKERSEITG AHICYLVAEA NFESYSDSAR LCLIAADHWK
HPRTYASPEA IQRTELYEYS KVLGNSQFIL LPFQPYKLIY AYMLAEVGKI SDSLKYCQAI
LKSLKVGRAP EVETWKQLIL SLEERIRTHQ QGGYTANLAP AKLVGKLLNF FDSTAHRVVG
GLPPPVPSTS PGSMQGTDRH HQPTVPRVSA SQSTMAMSSL MPSASMEPIS EWAADGNRMT
MHNRSASEPD IGRTPRQVES PKGTSSNAQG KTSGSGTASR FGRFGFGSQL LQRTVGLVLR
PRSDRQAKLG ETNKFYYDEK LKRWVEEGAE PPAEEAALPP PPTTSAFQNG VSDYNLKSAL
KSDGSPTNGS PTSKTPNPVE HASGIPPIPT SSNQFSARGR MGVRARYVDT FNQGGRSSAK
LFQSPSVPSV KPAVSANAKF FVPTPLPSSG NSTENVAENV QESAGFAEYP STSIDDSLQS
SSLSSKMNMQ RAPSMDNIPR RERTINDNIP MSSHARRTAS WSGSFSDSFS PPKMVENKPL
GEAAGMPPSS FIPGDPSITH MPMNGGGIGD DLHEVAL
//