ID A0A2G5B4L2_COERN Unreviewed; 1359 AA.
AC A0A2G5B4L2;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
GN ORFNames=COEREDRAFT_103766 {ECO:0000313|EMBL:PIA13983.1};
OS Coemansia reversa (strain ATCC 12441 / NRRL 1564).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Kickxellomycetes; Kickxellales; Kickxellaceae; Coemansia.
OX NCBI_TaxID=763665 {ECO:0000313|EMBL:PIA13983.1, ECO:0000313|Proteomes:UP000242474};
RN [1] {ECO:0000313|EMBL:PIA13983.1, ECO:0000313|Proteomes:UP000242474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1564 {ECO:0000313|EMBL:PIA13983.1,
RC ECO:0000313|Proteomes:UP000242474};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
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|RuleBase:RU364101}.
CC -!- SIMILARITY: Belongs to the SEC16 family.
CC {ECO:0000256|ARBA:ARBA00005927, ECO:0000256|RuleBase:RU364101}.
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DR EMBL; KZ303523; PIA13983.1; -; Genomic_DNA.
DR STRING; 763665.A0A2G5B4L2; -.
DR OrthoDB; 1361743at2759; -.
DR Proteomes; UP000242474; 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 Gene3D; 1.25.40.1030; -; 1.
DR InterPro; IPR024298; ACE1_Sec16_Sec31.
DR InterPro; IPR041591; OCRE.
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; PF17780; OCRE; 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:UP000242474};
KW Transport {ECO:0000256|RuleBase:RU364101}.
FT DOMAIN 241..269
FT /note="OCRE"
FT /evidence="ECO:0000259|Pfam:PF17780"
FT DOMAIN 626..706
FT /note="Sec16 central conserved"
FT /evidence="ECO:0000259|Pfam:PF12932"
FT DOMAIN 778..1048
FT /note="Ancestral coatomer element 1 Sec16/Sec31"
FT /evidence="ECO:0000259|Pfam:PF12931"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1260..1282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1327..1359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1359 AA; 141335 MW; 4F2B31B472B586A1 CRC64;
MPQTPKAEFA ASPTRRGTPS TSEPIPYFSG NSNGATDTDF FSLIGTTSAA ETNYTTHQSV
ATDPQILQQS DLAPVSMQYG HVSSEQQVDF GVPPRCATGP AVEFPYQSAA NQHEGPYVAA
ANIEAYRSAS VIYGGAHHGA QRMYQTAGTG IGSDYWVPNE ASRVSGVGID GSTRDAIGNT
EQQMGYSTAS TYAYSGHANH SQTTEDITPG TLAYTEINGD ATLGSEAALA GHTAAETANN
GVMFDETIGR YYDTNSGQYY DDVSGSWYYP QQVQGHLNQE QQVANETKAS TYEMPQQATQ
DVQGIGSSEW TNEPDGAAFF ENLSGAAAGP QHQQNVNDRV QASSAVETGQ KIESHGEDGT
VPQTSSWGTS LLVTDDPYKE ASHAAYVDKG NVVLQPEQSG QSQAIFYSKP TAPALSPATT
VQLTDEWAQH SKENQALTKC TAAPVGSRED GLDIMDASME VLAGRDNPPL QQNTEAGFVP
YEAAKIGSSF VSPENETNLS PSTVQGTRDV RPGDVHADTA AGGVYADVAL TDPIQPDGSE
HAAFQSWSAG AKSAPSGATY NGVELSIGSD ATDIVDHGIE YSGRQSLATE RHFGNSVCTA
DGYSTPDSMA GKQAAATALR RDGARIPVVA FGVGGRMVTM HPRMVTRFGA DGSETQRVVP
GLLQVRTLVG VLAEKDAALP GLPILTGDTA RAEVLQQRDA AVDWASALAE APAVRALGAE
EQALARVVVA VLRMAGERDA QGRALNKAVD ALRPLFAEMP RVDALDTCVE PGGLHELEEL
LLAGRRDDAV SAASARGQWG HALAIASGAG REAFAAVVAA FAAALHDGHA ALGAQYGLFS
GRGAAAVTAG FGDWARTLAL ALANRTPGDA AAMVRLGDGL HTTPPAAAHA CYVPALQRGV
FEGAAPRVVL LGAPRTSRCQ LAVVLTELHE LSLALHAVAA GDTPHCLPHL LPYKLLRAWW
LADCGHVTPA FLYCEAALRL IAALPPATAS PYIMVLAREL RALRERLAVA EPSARPPAAS
WLARAVTRPS LASLMTAVDS SIDRFIAGAD AVPETAPDVS PGLFEIGPDV ARVFSAQGPQ
AATPAVCDHA ASGTLAAIPA ALDPPAWGDP GVAGQLFVSA SQGDLLVPAA APGPAITSAW
GYASAADSSH SLNSVAAPPH PPPPAAEEEE EDMFGFAKRP APTSRSARPS ANTAHSAPVS
TRPSSDVPPA GAASKDPPID KEPAGVFGML KGLWASRKNQ ANLGEESQFV YDPALQRWVD
KSAPAESQDA APPPPPPMAM RFQSYNAVPS APRPASALPA GFSGANGMPL LPPAAMSASA
NISRTVTPMT SAAPDSAAPP FASKRRGARS RYVDVLNQS
//
