ID A0A395RHP9_9HYPO Unreviewed; 1927 AA.
AC A0A395RHP9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
GN ORFNames=FLONG3_11146 {ECO:0000313|EMBL:RGP59630.1};
OS Fusarium longipes.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=694270 {ECO:0000313|EMBL:RGP59630.1, ECO:0000313|Proteomes:UP000266234};
RN [1] {ECO:0000313|EMBL:RGP59630.1, ECO:0000313|Proteomes:UP000266234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 20695 {ECO:0000313|EMBL:RGP59630.1,
RC ECO:0000313|Proteomes:UP000266234};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP59630.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PXOG01000371; RGP59630.1; -; Genomic_DNA.
DR STRING; 694270.A0A395RHP9; -.
DR Proteomes; UP000266234; 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:UP000266234};
KW Transport {ECO:0000256|RuleBase:RU364101}.
FT DOMAIN 267..477
FT /note="Sec16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12935"
FT DOMAIN 974..1092
FT /note="Sec16 central conserved"
FT /evidence="ECO:0000259|Pfam:PF12932"
FT DOMAIN 1152..1455
FT /note="Ancestral coatomer element 1 Sec16/Sec31"
FT /evidence="ECO:0000259|Pfam:PF12931"
FT REGION 1..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1454..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1517..1579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1598..1927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..383
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..524
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..678
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1475..1491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1517..1550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1559..1573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1598..1628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1681..1737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1804..1840
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1855..1901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1906..1927
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1927 AA; 205193 MW; 698C2C88B0FD81F2 CRC64;
MASESPRATD LATMPNDSDV SSSSTESPVP ATSSATDTLV QSDKSTTQDM PSQHDQESPE
GVGAANAWLS QEDGDDGGNN WLASDDAVPE QTQQEETPSE AIPEQADTEQ TATEQATTRQ
ADTEKSDVEQ VDAEAVSQPK GPVSQHSSSR SFARTVSHEI SFGDDDEGEW TLSRTDTDPF
RFMPPSDRTN SFPPVPPAHS TSEVDEQQPL PSNQAMDVLE ETEREADAEE ELYQQEEASH
GLGAPRRGHS SSISIGGDLK SPEGQDSDER YEEGIPLIPQ PAEEASQVPV AQDAKTAGNL
FEEEEEEEGD EGADFFSQVQ GSEVAPEEQH APALERKSTM QVLDSMNAGS IQKKPTLEET
PEEEEEEEDL GSNDNEDEDP EGKAAPDELT PATSDPAPVK QEDLASKWEQ AFADDEDDDD
FLLDDNTGEE KQVDPAAFFG SDDEGFLEDE EPAADPVPAP APFPASRQVS GSNPYMPQAP
AIHPAPSPYA PVSQMPGVAV PPAPAYNSPA APQYGQPPPP RPDMSKAQSF ADKSKGGYHS
PYDLPTDLVT NLVKPRKRAS MQQLSQTEQL HAPVQAPPRS ASVGMPAPPT KLTPPSSSHG
LPAQQTGPPK ATTSGAQHKE NFFEELPMTS RPRPSSRTSQ RAASPARNAP PMARASHVPS
PLAPSFPNQV PPPSVPATAP ASNEHYTEPP TQAPVVPGAG LVAPERVSPY AALTTSANHM
PPPPSTTASR YSPAPGTSHT APPAVSSRYS PAPPATKTHG SYGAVTNSGP GPMLPHQPRT
SSPLTHSETA HFEPRLSRVS SLPPTREVDE EDDQQTQTRS VSATLSPPPQ ESRYNPVSPP
KLSRQTPPPP SYAGQLTLSP PKQSGPYAPL AASTAHSGIV PPPRAQTQSP SASFGHKQAQ
GSSDSTRRPS SAHSHSYPSP VAAKPAPSPY APVAPAAPAA GVSTVRTRGQ SITMNMIAPT
DGRENDELQR WKGVPIISWG VGGTVVTSFP KSVPRYGMNQ AVPMIVRTPG EVKVQSVKDI
EPLHEHVAKF PGPLRGKSKK KETISWLNAG IELLEKDLPD VSFHSQLSLE AKRAVERLLL
WKIMRIFVEN DGILEGNPTV DAAVRDVLSP GEAAAAASDD ALFPAASNFA AGIASVTSMQ
ADGVDVSTMD QVRHHLLRGD RDQAVWALVD KRLWGHAMLI SHTVEGDLYK RVAQEFVRKE
VNYPGHANES MAALYKILSG NFEDCVDELV PVHARAGLQL VSTDAGSGPS KDTLDGLDKW
RETLSLVLSN RSTDDIQGLN ALGNLLSSYG RAEAAHICFI FGRHSSVFGG LDDPNANFVL
IGADHRQQSD QFAKETEALQ LSEVYEYGLS LAGGALAAAG TPHLAAYKLE HAMTLAEYGH
RDKAMQYCDA ILTAMSSQTK RSPYHHHVLE TAVEDFMSRL KSAPKEESGS WISKPSMNKV
SDSMWNRFNK FVAGDDNEDN AGGAGEAGPF TRPSGEFSRS PSVSNFDIYG QQSPGFGMTP
AQTLAGAAQS KYAPASMTPA ASLNPYSPTS QYTPGRSSME QTTTNYGHNP YEPTYPGAAS
ANQADSYTPS VPKFESNDAG LGSSGLAPAA QITQGYSPAG YQPYGMPNPT SMSGDDKPSD
SSAQGFQPLS YGYEPPPMSS THPEQAGEED NNENGSGGYE PPSFQPYGYE PPSYEPQSTA
EDDDEAPKPK KKSIMDDDDD DGFPSMKPAE KSKSDKDREN EEMFRKAAEE DAKRAAAQQS
SKKGWGFGGW FGGNKKAALE PSSSGESSPG KPIRAKLGEA SSFVYDPDLK RWVNKKPGAE
NTPAKTATPP PPKAGPRSVS GTPPPPAGTP PPPLVTSNSA PPPLMVPKLR AGTPELTKQA
STESLGLAPP VMTRSVSNTS NASAPPSRPT TSMSNASSID DLLSAAPRKA GDKKKPRKGR
YVDVMAK
//
