SEC16_ASPNC
ID SEC16_ASPNC Reviewed; 1914 AA.
AC A2R4T4;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=COPII coat assembly protein sec16;
DE AltName: Full=Protein transport protein sec16;
GN Name=sec16; ORFNames=An15g01520;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SEC16 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAL00966.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; AM270336; CAL00966.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A2R4T4; -.
DR PaxDb; A2R4T4; -.
DR PRIDE; A2R4T4; -.
DR EnsemblFungi; CAL00966; CAL00966; An15g01520.
DR Proteomes; UP000006706; Chromosome 3R.
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 InterPro; IPR024298; ACE1_Sec16_Sec31.
DR InterPro; IPR024880; Sec16.
DR InterPro; IPR024340; Sec16_CCD.
DR InterPro; IPR024468; Sec16_N.
DR PANTHER; PTHR13402; PTHR13402; 1.
DR Pfam; PF12932; Sec16; 1.
DR Pfam; PF12931; Sec16_C; 1.
DR Pfam; PF12935; Sec16_N; 2.
PE 3: Inferred from homology;
KW Autophagy; Endoplasmic reticulum; ER-Golgi transport; Membrane;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..1914
FT /note="COPII coat assembly protein sec16"
FT /id="PRO_0000295530"
FT REPEAT 315..341
FT /note="1"
FT REPEAT 342..368
FT /note="2"
FT REPEAT 369..395
FT /note="3"
FT REPEAT 396..422
FT /note="4"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..422
FT /note="4 X 27 AA approximate tandem repeats"
FT REGION 352..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1506..1568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1600..1763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1776..1914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..623
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..684
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..707
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..768
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1673..1725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1812..1847
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1848..1864
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1914 AA; 202729 MW; 6488E20D7922FF2A CRC64;
MAQSDVAAVW NPALRSDDNA TPVPTGPASL EIDTSIEATT IPLGSPMETP HEYSISDIAF
PDSDTAAPPQ EAASPDMIDT EPLPNPDQIP ARDEVLEAPS ADVEATPEIS YDHETPNLDA
PQTEHAHDNE AMPLDDPEDQ VTEAQPAQPQ AEDSISTEAT AAQDMDVEEQ SSTPHAGDQD
GTEPADTNGE AHSSHDIWGS PAKENSAEDD FFNQLKTQTK PIYVPPENES RFEEGVPLLD
DSAESPVEPT ATQEGQIDNL FTDDNDEDDG FFKAVQSSPP PDKSQPASHI TRKSTFQVMD
SLGFSLDSPM SDADPAAQEF DNALAAATTN NSVGISAFEE DPAAQEFDNV LAAAATDNSA
DKPSSEEDPA AQELDNVLAA ATTNNSVGIS AFEEDPAAQE FDNVLAAAAT DNTVRKSSSE
EDLAARWQAE LAEEEAEVAP SEDDLAARWQ MELDDDDDLL LEDDIGGATA EHAPTSQNIN
GATAGAAVPG LSSPFGTPQS SVRPGAPATA YTPHQPSTSD LLQGVPVPGA APPANMAASA
DYFTQPPRPN VTANKAESFA ERAKEGYRSP YDLPEDLTRP RRPVASHKPV VTQPGSTPPP
PRSNSIPIPP PSTSMPPPPL GAQPDGAQST AKVAAPKNFY EELPLPPPRP QSRPASSGRY
TPGANAMPPA SSHPPPPPAN PYASLSTAPP AAAEAYSQPQ VQQPEGLDPY ASLSAPGASS
GPAPPSATSR YSPKPPTLQA GIKPPPSPRY SPAPPPATAP PPRNRYASQP TAPPSQGVAL
PFQPRTSSPL AYHEKVSYRP QEPSEQQPSA MEQPAIIPPI EVQSQPTAPA EYSPIQPPEV
PHVPEAVNMG SSVHQMSQQP MSPPRNQYAP PGYVDEFSKR IAPIANVPPA PVLPADDPTF
VPPRRSMTQS PSQQTLGPRL SVPSVDPLQR PASVHGAGSP TKAVNPYAPA QMSAHNRVAS
QSLEFIPPTD DQQFDPLERW KGAPIVKFGF GGSVLSCFPK HIPRYSAGQA TPKIKSTPGE
VKTHQLSDWI PVPDTIARHP GPLKSKSKKK DLLAWLSSKI AAFENEGIPQ AVYMHADSQK
RSEEKILLWK VVRVLVEHDG VLEGSPEIQK SLRQIIFPHL QDVDSAQPYG NGLPSFSTAQ
SLDAPSRPDA ADPQAVESIR NNLLVGEREK AVWGAVDHRL WGHAMIIAST MDKSVWKQVV
QEFVRREVRS ASGNTESLAA LYEIFAGNVE ESVDELVPPS ARAGLQMVSK VDGHGTSKNA
LDGLDSWRDT LGLVLSNRSS EDYQALLALG RLLQSYGRTE AAHICFIFSR AAVFGGVDDP
QASVVLLGAD HQHLSLAALQ DEDSILLTEA YEYATSVLSA SPKPPLPHLL AFKLVYAWSL
ADQGRKSEAQ QYCDAIAATL KATTKPSPYQ HQHLYFGVDE LSARLRQTTS DGGSSWISRP
SMEKVSGSMW AKFNSFVAGE DNEAGSAGSA KAGDGDIGPF AKIAGTPTVS RSPSVSDIYG
SYSAQPSYSS GPSRYQPNNQ YAPTSSPEQL RGRSSLDSQR SSSYGFGFGQ RRGSQEPSTP
VESNMYQGGM LYNSPPAVGY QSTPPQTSYM PLAPVKEDLA PQAHAEASAG PVEQSYGSGS
PYQPAGYGSF DQPFMNQVPS DGAGYMPPGV SSGYEPPAIE SHPEPVAAPS EEVNEEEPAK
KKSFMDDDDD DDIAARAAAI QKAERARKDR EADEAFRKAA EADAQKPAPA KKSWFGGWFG
GAAGGKKEDL NPNKPIRAKL GEENSFYYDK DLKKWVNKKD PNSATAARAT PPPPRASGPP
SRTASGSSAA PPPPASASPM MPPPSSRPPS TTGMPPPGSP APSSLGVPPP SIQRSVSTGA
AVSTPPSGLA APPRPATSLS NASSIDDLLG APTARKGAAA KGKKKGRYVD VMAK
