SEC16_NEUCR
ID SEC16_NEUCR Reviewed; 2084 AA.
AC Q9HEC9; V5IM51;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=COPII coat assembly protein sec16;
DE AltName: Full=Protein transport protein sec16;
GN Name=sec16; ORFNames=99H12.230, NCU03819;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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}.
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DR EMBL; AL451018; CAC18259.1; -; Genomic_DNA.
DR EMBL; CM002240; ESA42474.1; -; Genomic_DNA.
DR EMBL; CM002240; ESA42475.1; -; Genomic_DNA.
DR EMBL; CM002240; ESA42476.1; -; Genomic_DNA.
DR RefSeq; XP_011394599.1; XM_011396297.1.
DR RefSeq; XP_011394600.1; XM_011396298.1.
DR RefSeq; XP_011394601.1; XM_011396299.1.
DR AlphaFoldDB; Q9HEC9; -.
DR SMR; Q9HEC9; -.
DR STRING; 5141.EFNCRP00000003319; -.
DR EnsemblFungi; ESA42474; ESA42474; NCU03819.
DR EnsemblFungi; ESA42475; ESA42475; NCU03819.
DR EnsemblFungi; ESA42476; ESA42476; NCU03819.
DR GeneID; 3877336; -.
DR KEGG; ncr:NCU03819; -.
DR VEuPathDB; FungiDB:NCU03819; -.
DR HOGENOM; CLU_001147_0_0_1; -.
DR InParanoid; Q9HEC9; -.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0048208; P:COPII vesicle coating; IEA:InterPro.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IBA:GO_Central.
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 PANTHER; PTHR13402; PTHR13402; 1.
DR Pfam; PF12932; Sec16; 1.
DR Pfam; PF12931; Sec16_C; 1.
PE 3: Inferred from homology;
KW Autophagy; Endoplasmic reticulum; ER-Golgi transport; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..2084
FT /note="COPII coat assembly protein sec16"
FT /id="PRO_0000295540"
FT REGION 1..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1532..1573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1588..1852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1885..1904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1917..2084
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..562
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..681
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..736
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 966..980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1040
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1594..1608
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1611..1733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1770..1788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1801..1852
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1990..2016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2030..2052
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2084 AA; 222491 MW; 15EE3001C70158B7 CRC64;
MASWNPAFMP ESAADLPAPL PTDNTVADST DHANGVAQDG SDFWGIDGGE EDVPAQNGAS
DSWFPDYGTG SHTTLPATDA QATSQITSET DTDTPDTATE QTETAHVTTE DAEAVEPAPT
QTDEAPEPIV ENAQATEAVP GDAATVDLVP EHVEPTDATT TEKADTDEPS DVASKHTSTM
SFTRTIPHEP SWSDDGDPEW NLARADTDPF KFLPSSDRTN SFPPVPPLEQ HEQQQEEQQE
NQQVQQVQQQ QQQPQTDPHL EQSAIVQPQV ANFLGDDDEV EVQGDDGFFS QLSEAQNDGF
DQFGAQDANN SQQYMVGDLG AKATEALDAR FEEGVPLIAH DGNSTAERED TKDLFGGEDA
NDEDDFFSQV QQGSVNQADF EAQPLERKST MQVLGAMDMG SVQPSFPPVE EQPEEEAVAT
VETQTHDHPE ITSTDLNTGE GHEEQKPAGE DVEAKWKELF ADDEEDTLSL LDDSTEASNE
IKEKEIDPAA FFGSDDEGFL DDSEEFPTME ETTQPRAPSV AGSNTTTTPT TRYMPQTQTP
SLTGAPNPYA PTAPPLTSAP SNPYFPAAPS AVAQTPSVTP FGAPVSAPPP SGRFGYGAVP
PPQIERKAQS FVDKKGGYQS PYDLPMEVVK VKKRPSTATL NKPVTAPAAP PPSKSATHLP
PPPPPTSVPH SSQPGVKPPP PRGEAKPKEK FFEELPVVTK ARPASRNTLG TASPAQSSPY
GPPPPAGPPS IASQPPVPGM PSAMGSVPNS SFTQHAEVPN LVAPPRVNPY ASIQPSTTSL
APAVPAPASS RYSPAPSSGS QLSTPVPPAA ASRYSPAPPA SRPTSSGYTP TTSVPPVLPP
VLPHQPRTSS PLAHFESRPL VSSHAESGLA EKRSSSSLYD LRLQRVPSLP PTQEVEEEGP
MQGMVSPNQV PASHQTSPTA SRHGAMPHRS RRTPPPQSLT VQPVTSPQRA AYSYQPAASA
PSHEFAPPPR SQTQSPGALY GNRNVKPIEP IPRPSSVTDA TSPRAALYSP ITMQPSSTFP
PISTITSRPR GNTQNFNLVP PTDGREHDPL QRWRGVPLIS WGVGGALVTM FPKNVPRYGM
GQTAPMVIRS PGEVKVKSMK DIEPMEERLA KFPGPLKGKS KKKETIAWLT NGIEMLERTV
PHNLSHQLNP SHDDKRTTER LLLWKILRVF VEHDGVLEGN PTVNQAVREI LYPEASTIGG
QPEFANALNP SGMGNSATTS LQADSVDSSA VEQIRNHLIS GDNEKAVWAA VDKRLWGHAF
LLANALNPDL YKRVAQEFVK NEVNSTGHNN ESLAALYDVL SGNHEESVDE LVPAHARAGL
QLVAKNSSSG PSKDAMGGLD KWRETLSLIL SNRTADDARA INFLGNLLSG YGRAEAAHIC
FLFARSQTIF GGLDNPNSNF VLVGSDHRRQ ADHFAKEIEP LLLSEVYEYG QSLAGGTVPV
SNPHLAAYKL QHAYALAEYG FRDKALQYCE AITAAITAQT KRSPYYHPIL EAYVDDLMKR
LRQAPKEESN SWIPKPSMNK VSDSMWNRFN KFVAGDDNED GSKGSPDAAG ESGPFARIAG
GTPTISRSPS VNNLETFGAT IPSYGMPSAP VTNGPNMFSP PPPTRTASRY APGAPQPSTP
NYNPYETNSP YAPRSSMERA SGEYSRSSVE LPRQSLDSQR GYSHSSYAPN RTSSPAQPYT
PYGTTPQESS YSLHNMQPQQ SLTSPAATTS GYQPFTPQNN VSANDEPSNE PPSAPSTGYQ
PPSYGYEPPS FTPYEAPATN DEEEGASKEN GDSNQGGEGV NTFEPPSFQP YSYEPPSYEP
DTPPSKDDDQ SEEEKPKPKK KGPMYDDDDD DFPAAPKPAG KSKAEIDREN EEMVRRIAEE
EAKRAAEAKA AKKGWGFTSW FAKKEAAAAD ANAAGSSPGK PIRAKLGEAN SFYYDPEQKR
WINKNASPED QAAKKSTPPP PKGGIPRSSA SSPAPPMGMG VGGGSAPNTP GRASAPPTGP
PRPAALMPSA SESNVGSGPP SAVGPLSPSG SNGPPSAGLL SPGMGPAAMQ RPASTSTSGP
PAGTSKPLSA TSSIDDLLGA AVPRKRGEAK KPRKAARYVD VMQK
