SEC16_ASPFU
ID SEC16_ASPFU Reviewed; 1832 AA.
AC Q4WD95;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=COPII coat assembly protein sec16;
DE AltName: Full=Protein transport protein sec16;
GN Name=sec16; ORFNames=AFUA_6G03960;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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; AAHF01000012; EAL85643.1; -; Genomic_DNA.
DR RefSeq; XP_747681.1; XM_742588.1.
DR AlphaFoldDB; Q4WD95; -.
DR STRING; 746128.CADAFUBP00009169; -.
DR PRIDE; Q4WD95; -.
DR EnsemblFungi; EAL85643; EAL85643; AFUA_6G03960.
DR GeneID; 3505046; -.
DR KEGG; afm:AFUA_6G03960; -.
DR VEuPathDB; FungiDB:Afu6g03960; -.
DR eggNOG; KOG1913; Eukaryota.
DR HOGENOM; CLU_001147_0_0_1; -.
DR InParanoid; Q4WD95; -.
DR OMA; LERWKGA; -.
DR OrthoDB; 56582at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
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 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..1832
FT /note="COPII coat assembly protein sec16"
FT /id="PRO_0000295529"
FT REGION 1..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1509..1679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1692..1832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..380
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..470
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..663
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1424..1457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1512..1536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1548..1564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1572..1586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1590..1646
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1737..1758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1790..1805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1832 AA; 194987 MW; 4FD33EBF7E665837 CRC64;
MAQPEGVLAW NPAFRPEDND SVATDLARLA LDSGKEVSET TDVDTHVSPP AEEFTDENGS
IESKTAISAD TSDQGAPDLV DSNTPAADNG SKPDTEEPDK PSRDESIFMQ TDKSRAVEDV
TENVPTENGN VDITSGLEEH VAEEPHYEGP EKSTGLAGRN DAQDLFEGND TAWMDEAEGE
VNGATVNGEA SGTRPGFWDS LGDNERDNED DFFNQLKTQT KPIYSPPETE ARFEEGIPLL
GQGAAPQNNH AHKGESQVDD VFGDDEDDES GFFSEIQKRT SAEGPPPITR KSTSQVIDSI
NAVSDSMFSK QLPAAAELNN SLAVPTADGE IKNSPSEEDL AARWQAELSD DADETMPTED
DLAARWQAEL DDDDDDLLLD DDTTNAQRPP EAANIDHMND TSMLQSPFGT PENLARPKVQ
PVSYTPHQPS TSDLLSGIPA QNTAAQPTNA SMSSYFSAQA PPNPVTTRAE SFAERSKEGY
KSPYDIPEDL ARPRRAVANS RTVVAQPGTV PKPPPRSSSI PAPPLKASTV SPAPLGTSST
APTAPQKNFF EELPLPPPRP KSRPASSGRY TPNAPVSAPS LPQSIPPPAN QYSNVPGAPQ
SNIGPPDPPQ LQQPERLDPY SNLLAPNVPS APAVPSTASR YSPRPPGVQA GVKPPPSPRY
SPAPPQSTNA VAAAPRNRYA SQPASISGQG AALQFQPRTS SPLAYHEKIH YEDQGQSEER
PQLQSTASPP PLNHSHPSEQ PVSSENKGPS GVDVLENVPP LSTRPQSPPK NPYAPSAYTN
EFANRVAPVS TGPPIAGMTG VLNSSTEESP FVPPRRSQTQ SPSQTLSPRL SVPSLDPFQR
PASVHGSTSP TRTVNPYAPA PVPTHNRAPS QVLEFIPPTD GQQLDSLERW KGAPIFKFGF
GGAVISCFPK HIPRYSAGQA APMIKSCPGE VRISQLNDWL PAAEGIVQHP GPLKGKSKKK
DLVAWLSSKI AAFENADIPD FDRLSPDASK LREEKTLLWK VIRVLVENDG VLEGSVEAQK
SLRNLLFPNL QDSGPNQSLG DVFTPSATLQ PLNAPSQPDA VDSRSVDLLR DTLVLGEREK
AVWAAVDKRL WGHAMIIASR MDRSVWQQVV QEFVRREVRS ATSRTESLAA FYEILAGNIE
ESIDELVPPS ARAGLQMISK VDGHGPAKNS LDGLDSWRET VGLVLSNRSP DDQRALVALG
RLLLSYNRTE AAHICFILSR VAVFGGLDDP QANIVLLGVD HQRLSSCAAL YNDDSILLTE
AYEFATSVLA GSSVSTLPHL LAFKLIHAWS LAERGRKSEA QQYCDAIAAA LKATTKPSGY
HNQHLFFGVD ELSARLRETT SDGGSSWISR PSMEKVSGSM WAKFNSFVAG DDSDAASTGS
VKAEEIGPFA RVSGTPTISR SPSVSDIYGS YPVAAAQPLP ATGPSRYQPV SQYAPSASPE
QLRGRSSMDS QRSASFGYPL GQRRGSQEPS TPVDTNMFHG MPMYGSPPVA GYQSTPPQSS
YMPLAPVAED SASGAQQESF SAHSQVSDNA PSHRSSTYAP EPFGHPFDTQ AVSTTSQPDQ
GGYMPPTSSG AYEPPSFESN TESADGAQDE STEEDKPKKK SIMDEDDDED LAARAAAIQK
AERARRDREA DEAFRKAAEA DAKKPPPATG KKGWFSGWFG GKKDDNSGGG PIRAKLGEEN
SFYYDTELKK WVNKKDPGSA APTRGTPPPP KGSAPPSRSM SGSGGPPPAM ATPPPTGASG
SRPSSSAGAP TSVSASPAPP SLGAPPPAIP RSVSTGAVLP TPPSSSAGAP PRPATSLSNA
SSIDDLLGAP QARKGPAARG KKKGRYVDVM AK
