ID A0A218Z1D6_9HELO Unreviewed; 2027 AA.
AC A0A218Z1D6;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
GN ORFNames=B2J93_4717 {ECO:0000313|EMBL:OWP01867.1};
OS Marssonina coronariae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Dermateaceae; Marssonina.
OX NCBI_TaxID=503106 {ECO:0000313|EMBL:OWP01867.1, ECO:0000313|Proteomes:UP000242519};
RN [1] {ECO:0000313|EMBL:OWP01867.1, ECO:0000313|Proteomes:UP000242519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NL1 {ECO:0000313|EMBL:OWP01867.1,
RC ECO:0000313|Proteomes:UP000242519};
RA Cheng Q.;
RT "Draft genome sequence of Marssonina coronaria NL1: causal agent of apple
RT blotch.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:OWP01867.1}.
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DR EMBL; MZNU01000257; OWP01867.1; -; Genomic_DNA.
DR STRING; 503106.A0A218Z1D6; -.
DR InParanoid; A0A218Z1D6; -.
DR OrthoDB; 1361743at2759; -.
DR Proteomes; UP000242519; 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 InterPro; IPR024468; Sec16_N.
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.
DR Pfam; PF12935; Sec16_N; 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:UP000242519};
KW Transport {ECO:0000256|RuleBase:RU364101}.
FT DOMAIN 274..435
FT /note="Sec16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12935"
FT DOMAIN 1026..1143
FT /note="Sec16 central conserved"
FT /evidence="ECO:0000259|Pfam:PF12932"
FT DOMAIN 1203..1506
FT /note="Ancestral coatomer element 1 Sec16/Sec31"
FT /evidence="ECO:0000259|Pfam:PF12931"
FT REGION 30..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1513..1534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1568..1864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1878..2027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..566
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..715
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..1004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1568..1596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1597..1611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1613..1685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1686..1703
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1765..1781
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1796..1826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1889..1924
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1930..1952
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1963..1991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2027 AA; 217979 MW; 20DCD178BDBA510D CRC64;
MQPGPAEASW HPAFMPNSAL RVTAAKAPEL VALGQPTPEP AFEDQQEQVS PASRPDGPEY
LEKELKTQDQ MRTGNDAHLE LKKLHDAAPT SLASPGGIEL AENSWHNGYE NTAAAENYTA
EISSEGPHNE NRHLSTMSFA RTVSEEVNWG EDDEVDSPWN IQRTDTDPFK LMAKSDRTNS
FPEVPSAHSP GLNPHDQSLP LSQAEEIMAD VEQEVSENLF GDEKADLGDE FSTRNTRKSG
DHLEFSHGNR LDDDELRLPD YGQKYGIDLR RDQDEEMETR FVEGLPLVQH KDEQGQPQPH
AQASNMDDLF ATDDADEENF FTQVHSVGHE LREPVQAPPL ERKSTMQVID AINYQPHEQI
HENILEEDQE KSSQKSSERS TGGEIAASSS TIVSAVLDDP EIAIQTQSEG SDEDLAAKWK
AALAGDELLT DEDDAFLPDD DWPTENSGFD PAALFGSDDE GFLEDNERDV GDLVTQQTSP
HVTASVAGLN SHALGFGTIT GAAQPTRATI SSNKYLPAGA STAPAPISSN SYAPSAPLLT
DLSATTTPAS VPSPYMSPPV SNLQPLPARP EMPKAQSFAD KSKGGYASPY DLPMEVVKPR
KRVSMQQMNR PAQPTADIAP PRSSSMYNPA TRGPTSSMSP PPSSHGPSGQ MNPETAPQPT
KTSRNSQSGF FEELPMSRPR PAARQSSSLA SPGLSPYGPS TPGAVPPPLA GPARTPYAPP
SIQQNVVQHP TQSSHQIQGL VAPERVSPYA SLPSANVPVP AVASRYSPAP PAPQQSHTAL
PPAVQSRYSP APPSQRTGPY APSQLNTQSP QTAPVLAHLP RTSSPLAHFE RNKELRSRGS
FSEAGSLDRR TSHSGYEPCV RSQQLPPTRE VEENGRFSPT STLDCGDLQS QYSQQAQPRM
ARNTSTPPPQ SLASRLANSP QKRATSNYLP QQSSNGSAEP LLPPKRSQTQ SPGNGFSGPR
LDMSSSVPYQ RPASVEVPAS PRNSNVYKSM SVSSGSGRPR GFSQSLSFVA PTDGRENDPL
QRWRGAPVFA WGVGGTVMTS FPQDIPRYGM NSQAMIIRTP GTVKIRSIKD LDPLHGRFSS
FPGPLKGKSK KKEVLTWLTS GIELLQQNAS YLRSVSMLSH EDKRIEERIL LWKILRVFIE
HDGTLEGSPA VDKAVRSVLS PGLDEQGTSD PLCGTGADLS GISQSLNIAP RADPVDPAAV
DQLRKHLLRG DREKAVWDAV DKRLWAHAML ISNTVSKDLY KKVAQEFIQK EVKIIGDNVE
PLAALYEIFA GNFEESIDEL VPLSARAGFQ MVSTSNAVGP SKDAMDGLDR WRETLGLVLS
NRSSEDSQAL NALGKLLSGY GRAEAAHICF LFARSLSIFG GVDDPQASIV LVGSDQLRQP
HDFDRELEPV LLSEVFEYGT SLSSTSTIAI SSPHLAVYKL QHAKILAEYG FRDKALQYCE
AVGTSITSQT RRSPYHHALL VSELEDLSKR LKRSPKDETA SWISKPSIDK AKGSVWATFN
KFVVGDEADA AANDSNGAGA PDTGPFSRIA GGKTPTISRS ASVADIYAAY NGVPNGTVPV
PITKASSRYA PSASSYGNHE PHSSTSYGSQ PRNSLEERSS SEFRRYEPQR RPSDYGPNSQ
PSNQSNSYTP QSASGFPPLS SYTPFGNSGS YEPSSAHAPQ TPLTEQPSPQ PLNYFDGQPP
SSYTPSEPSY GLPPAPSFEP PAVNKNQPPS SNGYEPAVSN DYGPPVSSGY EAPQYEPQAS
GYEPPSNGYA PPSYEPIAMN DEPDSAIDTR PKKKSFMDDD DDDLQAPTNA QAAPENREKT
KAEKDKEADE AFRKAAEADA QKGKDAAPSK KGWGLGGWFG GSKKESPDTG PAPNKPIKAK
LGEASSFFYD PELKRWVNKK AGAEDTPAKS ATPPPPRAPG PPRTASAPLH PPAAMTPPRP
IPTRSGGPQM LAQRAVSDST HMGFNPSPQS DDGSVGGLAA PPAMNRSQSN GSLRSAPPSR
PGTSMSNASS IDDLLGPPVP RKAGLAAKKG AKKKGRGYVD VMGDKAG
//
