ID   SEC16_NEOFI             Reviewed;        1835 AA.
AC   A1DLN3;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=COPII coat assembly protein sec16;
DE   AltName: Full=Protein transport protein sec16;
GN   Name=sec16; ORFNames=NFIA_050490;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027698; EAW15704.1; -; Genomic_DNA.
DR   RefSeq; XP_001257601.1; XM_001257600.1.
DR   AlphaFoldDB; A1DLN3; -.
DR   STRING; 36630.CADNFIAP00004521; -.
DR   PRIDE; A1DLN3; -.
DR   EnsemblFungi; EAW15704; EAW15704; NFIA_050490.
DR   GeneID; 4584116; -.
DR   KEGG; nfi:NFIA_050490; -.
DR   VEuPathDB; FungiDB:NFIA_050490; -.
DR   eggNOG; KOG1913; Eukaryota.
DR   HOGENOM; CLU_001147_0_0_1; -.
DR   OMA; LERWKGA; -.
DR   OrthoDB; 56582at2759; -.
DR   Proteomes; UP000006702; 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   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; 1.
PE   3: Inferred from homology;
KW   Autophagy; Endoplasmic reticulum; ER-Golgi transport; Membrane;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..1835
FT                   /note="COPII coat assembly protein sec16"
FT                   /id="PRO_0000295539"
FT   REGION          33..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          378..866
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1040..1068
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1376..1404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1422..1485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1512..1682
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1695..1835
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..216
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..295
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        425..472
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..497
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..532
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..582
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        650..665
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        683..704
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        740..764
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        805..835
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        844..858
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1040..1058
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1432..1477
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1517..1535
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1551..1566
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1586..1651
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1740..1755
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1756..1770
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1793..1808
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1835 AA;  195066 MW;  785ABC3999EB0869 CRC64;
     MAQPEGVLAW NPAFRPEDND SVATDLARLA LDSKKEVSET TDLDTHASPS AEEVTEENGP
     IEFKAAISAD TGDQGAPDFV DSNMPAADDS SKPDIEEPEE PSCDESISMQ TDEPRAVEDV
     TENVPTENGN VDITSGLRLE EHVAEEPHYG VPENSTGLAS QNDAQDLFEG ADTAWMDEAE
     GEENGATVNG EASDTRPGFW DNLGDNERDN EDDFFNQLKT QTKPIYSPPE TESRFEEGIP
     LLGHGAATQN DHAQKGESQL DDVFGGDEDD ESGFFSEIQK PTSAEGPSHI TRKSTSQVID
     SLNAVSDSPF SEPSPTAVEF NNGLTVPTAD GEIKKAPSEE DLAARWQAEL SDDADETMPT
     EDDLAARWQA ELDDDDDDLL LDYDTTNAQG PPEAANIDHM NDSSILQSPF GTPENPARPK
     MQPVSYTPHQ PSTSGLLSGI PAQNTAAQPT NASMSSYFSA QAPPNPVTTR AESFAERSKE
     GYKSPYDLPE DLARPRRAVA SSRTVVAQPG TVPQPPPRSS SIPAPPLKAS TVPPAPLGTS
     SAAPTAPQKN FFEELPLPPP RPKSRPASSG RYTPNATVCA PSVPQSIPPP ANPYSNVPGA
     PQSNIGPPNP PQLQQPERLD PYSNLLAPNV PSAPAVPSTA SRYSPRPPGL QAGVKPPPSP
     RYSPAPPQST NAAAAAPPRN RYASQPASIS GQGAALQFQP RTSSPLAYHE KIHYQDQGQS
     EERPQLQPTA IPPPLNHSHP SEQPVSSENK GPSSADVLEN MPPVSTRPQS PPKNPYAPSA
     YTSEFAKRAA PVSTGPPIAG MTGVLNPSTE ESPFVPPRRS QTQSPSQTLS PRLSVPSLDP
     FQRPASVHGS TSPTRTVNPY APAPVPTHNR APSQVLEFIP PTDGQQLDSL ERWKGAPIFK
     FGFGGAVISC FPKHIPRYSA GQAAPMIKSC PGEVRVSQLN DWLPAAEGIV QHPGPLKGKS
     KKKDLVAWLS SKIAAFENAD IPDFDRLSPD ATKRREEKTL LWKVIRVLVE NDGVLEGSVE
     AQKSLRNLLF PNLQDSVPNQ SLGDGFTPST TLQPLNAPSQ PDAVDPRSVD SLRDTLVLGE
     REKAVWAAVD KRLWGHAMII ASTMDRSVWQ QVVQEFVRRE VRSATSRTES LAAFYEILAG
     NVEESIDELV PPSARAGLQM ISKVDGHGTA KNSLDGLDSW RETLGLVLSN RSPDDQRALV
     ALGRLLLSYN RTEAAHICFI LSRAAVFGGV DDPLANIVLL GVDHQRLASS AALYDDDSIL
     LTEAYEFATS VLAGSSVSTL PHLLAFKLIH AWSLADRGRK SEAQQYCDAI AAALKATTKP
     SGYHNQHLFF GVDELSARLR ETTSDGGSSW ISRPSMEKVS GSMWAKFNSF VAGDDSDAAS
     TGSGKAEEIG PFARVSGTPT ISRSPSVSDI YGSYPVAAAQ PLPGTGPSRY QPVSHYAPSA
     SPEQLRGRSS MDSQRSSSFG YPLGQRRGSQ EPSTPVDTNM FHGMPMYGSP PVAGYQSTPP
     QSSYMPLAPV AEDSASGAQQ GPFSAYSQVS DSAPSHRPSA YAPEPFGHPF DTQGVSTTSQ
     PDQGGYMPPA STGAYEPPSV ESNTEPADGV RDESTEEDKP KKKSFMDEDD DEDLAARAAA
     IQKAERARRD READEAFRKA AEADAKKPPP ATEKKGWFSG WFGGKKDDNS GGGPIRAKLG
     EENSFYYDTE LKKWVNKKDP GSAAPTRGTP PPPKGSAPPS RSMSGSGGPP PAMATPPPTG
     ASGSRPSSSA GAPPSVSASP APPSLGAPPP AIPRSVSTGA VLPTPPSSSA GAPPRPATSL
     SNASSIDDLL GAPQARKGPA ARGKKKGRYV DVMAK