ID A0A3M9Y7Z8_9PEZI Unreviewed; 2005 AA.
AC A0A3M9Y7Z8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
GN Name=SEC16 {ECO:0000313|EMBL:RNJ56617.1};
GN ORFNames=D7B24_007106 {ECO:0000313|EMBL:RNJ56617.1};
OS Verticillium nonalfalfae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=1051616 {ECO:0000313|EMBL:RNJ56617.1, ECO:0000313|Proteomes:UP000267145};
RN [1] {ECO:0000313|EMBL:RNJ56617.1, ECO:0000313|Proteomes:UP000267145}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VnAa140 {ECO:0000313|EMBL:RNJ56617.1,
RC ECO:0000313|Proteomes:UP000267145};
RA Stajich J.E., Kasson M.T.;
RT "Genome sequence of Verticillium nonalfalfae VnAa140.";
RL Submitted (OCT-2018) 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:RNJ56617.1}.
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DR EMBL; RBVV01000054; RNJ56617.1; -; Genomic_DNA.
DR STRING; 1051616.A0A3M9Y7Z8; -.
DR OrthoDB; 1361743at2759; -.
DR Proteomes; UP000267145; 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}; Transport {ECO:0000256|RuleBase:RU364101}.
FT DOMAIN 1022..1140
FT /note="Sec16 central conserved"
FT /evidence="ECO:0000259|Pfam:PF12932"
FT DOMAIN 1200..1502
FT /note="Ancestral coatomer element 1 Sec16/Sec31"
FT /evidence="ECO:0000259|Pfam:PF12931"
FT REGION 1..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1503..1541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1568..2005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..98
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..223
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..501
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..627
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 678..698
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..805
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..845
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1573..1629
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1681..1711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1750..1801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1810..1824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1888..1924
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2005 AA; 211053 MW; A9CAF148F9157331 CRC64;
MSSDEHVSSW HPALMPNSSA SATVDGHPSA PAHTQPPPVQ DSLEASEPYA HDTTTSSTDS
SAQPEATADL DASLINEPTE PTPTSEATMP PVPDPIPQDE SANRPWFAEE PVAQADAEGD
WPVFDHPTSA PAEPEASPAD AEAAAPAESS PPAPEVQAAG PVLGHSSTVS FARTVSHDIN
FHDDEDADWN LSRTDTDPFK FMPPSDRTNS FPVVPPASPP GASAGTQPLP ATEAQHVIQA
TEQHQDDLDA PLSERAISPA QPHFADDPSD TPHINGYSEQ AQYVGRDMTD ADEDDVGSRF
EEGLPLIPRA PEHTETAASA SFFDHEASAD DDFFSHVQDA GHDDTPPTLE RKSTMQVLGA
FGTNPLSRAD TLEGMAEEDE HQATPSQALA TEDDSSKPAP EDLAAKWQEA FAGDDDDEFL
LDDNAGDSKP VDPAAFFGSD DEGFLDDDDD ETAASAPAVQ PPSLPAAQQQ SLQGRYTPQS
PSFPFPKAAA TPSPYVPVAA APPQTPTSAY APSPAVTSFP APTSYAAQSQ PSPIQAAYGM
PPPPRPEASK AQSFADKNKG GYTSPYDLPM DVKPRKRASM QQLPRAQVQA PPVQLPPRSS
SMYAPSPTSS APPSAGLPPP SPALALPSPG TAGPAAGLKP RAVTPSKENF FEDLPMTSRP
RPASRQSSRL PSPALGGPAS LPQGPPPGPP PGPPAAQYAP LPSSQSMELP KQEAPPALPR
AESSGLTGLV APPRVSPYAA LQSNSPGTSS IPNNSRYSPA PPLAPAVNGT ARPGSANRYS
PAPPASRPPS ATYSAAPPPA AVLPHLPRTS SPLAHFEVSH DRAQSAPVTN GEHGQHGQHG
QQDRRISAQF EPRVNRVSSL PPTQEVEEDE GAKAEQSPQP IDAYAPLGAT PASPPLARHT
PPPSAHGYGP SMLSPPKRAA ANYTPQPQSN PLSPEQRFAP PMRSQTQSPG SLQSRYQPSE
AAARPASSHG AAAPQAAQPA SAQHSYAAAP RTGRHRAPSQ SLNMVAPTDG RENDPLKRWK
GAPVFSWGIG GTIITSFPKE IPRYGMGQTA PMIVRTPGEV RVKQVKDIEP LEDRLAKFPG
PLKGKSKKKE TISWLTAGIE SLEANLPGQT YSSQITHEDK RTTERVLLWK ILRTFIEFDG
ALEGGAEVEA AVRDILSPEA KDEAAEAAPL YADGAAGVAF PATSTQMQAD GVDSQTVVSI
RKHLLAGDRE QAVWAAVDKR LWGHAMLISN TVSPDLYKQV AQEFVRKEVN YPGHNNESIA
ALYKVLSGNF DECVDELVPS HARAGRQLMT TAATAEPAKD ALDGLDKWRE TLGLVLSNRS
PDDTKALSAL GDLLSTYGRA EAAHICFLFA RKTIVFGGLD DQTASFVLLG ADHKTQAEQF
GKETEALLLS EVFEYGLSLA SGANSAGVPH LAAYKLQHAA TLAEHGFRDK ALQYCDVIAN
SITAQTKRSP YHHALLEAAV DDLSKRLKQA PKGESSSWIS KPSMNKVSDS MWNRFNKFVA
GDEADGSGTA TPGEPGAETG PFGRIAGGTP TISPSPSVSN FDVYGNNNPG YPVTAPAALA
QGTRAASRYA PMGAQPSTPT TSYEPTSGYT PAAQSTQPSN DYGRASFDAP TRTSIDSQSG
VTAGSYTPQA YNPAPYGAPL DGHAPQPDPA PSAYGPYGGL QEAPVITHQG SPAPPADDPT
QFTPQGDQGY QPPSYGYEPS SFVTNAGPDS QQAEPEDAAA SGGYEAPSYQ PYSYEPPTYD
PGVEPSNDDN DDDDKPKPKK KSFMDDDEDD IPALRPQGKS KSEKDKENDE MFRKAAEEDG
KIQSGHAPFL YHNEANSSTA KRAGEQSAGK KGWGFGSWWG GKKDAMPDSN QGNKPIRAKL
GESSSFVYDP DQKRWVNKKA GAEQTPAKTA TPPPPKSTGT PPPPSSSAPP MGPPGGPPRP
PMPIGAGSLS KAPSRESLDI PAGPPAMARS VSNSSTGPPS GPPSRPTTSM SNASSIDDLI
GAAGPRRPGA KKARKSGRYV DIMAK
//
