SEC16_ASPTN
ID SEC16_ASPTN Reviewed; 1806 AA.
AC Q0CGY7;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=COPII coat assembly protein sec16;
DE AltName: Full=Protein transport protein sec16;
GN Name=sec16; ORFNames=ATEG_07055;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476603; EAU32439.1; -; Genomic_DNA.
DR RefSeq; XP_001209741.1; XM_001209741.1.
DR AlphaFoldDB; Q0CGY7; -.
DR STRING; 341663.Q0CGY7; -.
DR PRIDE; Q0CGY7; -.
DR EnsemblFungi; EAU32439; EAU32439; ATEG_07055.
DR GeneID; 4319158; -.
DR VEuPathDB; FungiDB:ATEG_07055; -.
DR eggNOG; KOG1913; Eukaryota.
DR HOGENOM; CLU_001147_0_0_1; -.
DR OMA; LERWKGA; -.
DR OrthoDB; 56582at2759; -.
DR Proteomes; UP000007963; 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..1806
FT /note="COPII coat assembly protein sec16"
FT /id="PRO_0000295532"
FT REGION 1..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1418..1647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1663..1806
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..554
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..592
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..657
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..749
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 825..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1505..1557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1561..1614
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1699..1736
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1765..1779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1806 AA; 193035 MW; B23A8D1EBD10F83C CRC64;
MAASEQFASW NPALRSEDHS IPTIENTLDQ QPTSPAEQVE SQAKTVTPPP QEDSPLQEVP
EDVVDTVVPP VSGDTQPIAN ALDQDQTQPQ PEETDRDIPP MIVDTPKDTQ ETQESVPRNA
TDEGNVFSLE SNDSAFPTTQ NAPDLSWAED SQPQAVERHD DSVWTLHQQS KETPTSPNGD
FGTTSHDLWG SPTSPGGEHD FFDQLKTQTK PIYVPPESES RYEEGVPLLD EGVSSPTEPT
ANQESRIDQI FDGDEDEEGA FFNEVQESAS TDESRPYGHM TRKSTSQVLD SLDTSMKSPV
SDASPTAREF DNILAAAASG NQVKKSTSEE DLAARWQAEL SDEEPEPAPE DDLAARWQAE
LDDDDDMLLE DETSGELPNQ EMHMNGIASQ AAPPVLSSPF GTPESAARPK AQPTSYTPHQ
PSTSDLLQGI PAQGYAQGNT TTAPNYFAPQ PPKPATSRAE SFAERSKEGY KSPYDLPEDL
ARPRRAAATH RPVVVPGNNM APGPPAASVP PPQRAPSMPT PPMATLPSTT TAPPAPPKNF
YEELPPPPPK PQSRPSSSGR YTPGPASSHP VLPPPSNPYA AVPPPPTVDS SIPPHLHQPE
KTDPYVNLLA PSAPSAPSAP SAASRYSPKP PSLQGGVKPP PSPRYSPAPP PSTAPVPPRN
RYASQPSSGP GQTAVLPFQP RTSSPLAYHE KVSYQPQEGL RKPSFAEQES AAGPQNEIQE
QPVGHHVGQS VPGGTVVDTQ NTGAPMAPQQ TSPPRNPYAP PAYVNDFSKR VAPMTSAPPP
ASAPPATETQ FMPPRRSQTQ SPSQQVLGPR LSVPAVDPLQ RPASVHGSGS PTKSSSPYAP
SAPAHNRVAS QQLEFIPPTD GQELDPLERW RGAPIVKFGF GGAIVSCFPK HIPRYTAGQP
APKIMAAPGE ARIHQLRDWV PIADSIVQHP GPLKNKSKKK DLLAWLSSKI AQFENEGISE
AAQLHPESGM RHDEKILLWK IIRILVEHDG TLEGSEPIKK ALRGVIFPHL AENPDSSESY
GANVPSFGDI KPLDAPSKSD AMDPQAIGNL RNYLLLGDRE KAVWSAVDNR LWGHAMVIAS
TMDKSVWKQV VQEFVRREVR SATGNTESLA ALYEIFAGNV EESIDELVPP SARAGMQMIS
TVDGHGPAKN ALDGLNSWRD TLGLVLNNRS PDDHQALLSL GRLLLSYGRV EAAHICFIFS
RAAVFGGADD PQSCIVLLGA DHQHLPSTIL QDEDAFLLTE AYEYATTILA GAPMATLPHL
LAFKLLHAWS LADRGRKAEA QQYCDAIAAS LKSTTKPSGY HNQHLLFGVD ELSARLRQTT
NDGGSSWISK PSMEKVSGSM WAKFNSFVAG DDSDAASTGS GKAGEGDVGP FARFTGTPTL
SLFLAADPPV TSQITNMPLM HLLNNLADGL RWTPSAHHPM DFPFPQRRGS QEPATPMENT
FYQGGGPYGS PPAVGYQSTP PQTSYMPLAP VEEDSATQSY PAASAPPHEP AMNTSPYLPP
GGPSSQPLNR GSMMDSQTGA SSYMPAETSG SSYTPPTFNT GYEPPTIETT AAPDTQSTDE
PADDVPLKKK KSFMDDDDDD DIAARAAALQ KAEKERKDRE AEENFRRIAE AEAKNAPQQK
KSSWWPGWFG GGKKEENNNS GGPIRAKLGE ENSFYYDKEL KKWVNKKDPN SATVSRGTPP
PPRGAAPPSR TASGSSAPPP AASPKPPGPD SRPTSSAGAP PPQTGSPAPS LLGAPPPFLN
AVPRSVSTGA AAPPTRPGSS SGPPPRPATS LSTASSIDDL LGPPQARKGG TVKGKKKGRY
VDVMAK
