SEC16_ASPCL
ID SEC16_ASPCL Reviewed; 1875 AA.
AC A1CME3;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=COPII coat assembly protein sec16;
DE AltName: Full=Protein transport protein sec16;
GN Name=sec16; ORFNames=ACLA_096630;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
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; DS027058; EAW08730.1; -; Genomic_DNA.
DR RefSeq; XP_001270156.1; XM_001270155.1.
DR AlphaFoldDB; A1CME3; -.
DR STRING; 5057.CADACLAP00009100; -.
DR PRIDE; A1CME3; -.
DR EnsemblFungi; EAW08730; EAW08730; ACLA_096630.
DR GeneID; 4702212; -.
DR KEGG; act:ACLA_096630; -.
DR VEuPathDB; FungiDB:ACLA_096630; -.
DR eggNOG; KOG1913; Eukaryota.
DR HOGENOM; CLU_001147_0_0_1; -.
DR OMA; LERWKGA; -.
DR OrthoDB; 56582at2759; -.
DR Proteomes; UP000006701; 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..1875
FT /note="COPII coat assembly protein sec16"
FT /id="PRO_0000295528"
FT REGION 34..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1413..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1475..1717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1733..1875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..411
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..442
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..559
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..622
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..708
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..763
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..782
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1475..1501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1507..1541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1586..1603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1630..1680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1744..1776
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1875 AA; 200247 MW; D8005D56812AE5DB CRC64;
MTQVEGLSTW NPAFRPEDNE SIITNNLAQL VLDPESRPAE VSPVDVHTSP FGDDADVENE
THVLESPLPS EPQDAPAPVA TDSDPSQNAD PITELKDVLE QPRHIDGNDS SIHPDDTQVA
ENVAEYVSTQ PEDDKEQANG LHLGNTVAEG MSAEHDKDEH TSGLHLGNSV AEASHFSAPE
EFSGVETSGN GLHFRAVKGD TSWIDGDEVE EDKDAMPHGE ISNDRPGFWG NLGNDGRDNE
DDFFDQLKTQ TKPIYVPPET ESRFEEGVPL LDNSPQTPVE QAQRGDNQLD NVFAGDEDDE
GDFFNEIQKS TPEEGPFHIT RKSTTQVLST LDTTPDSPFS ETSPTAQDFN QILADTSAQN
ETKEPSDADL AARWQAELSD DAEETMPPED DLAARWQAEL DDDDDDLLLD EASTANNDQE
AAQLNQDHNA GFAASLQSPF GTPENPARPK AQPISYTPHQ PSTSDLLQGI PAQAPVPQPH
NAPTSNYFTA QAPPNPVTTR AESFAERSKE GYKSPYDLPE DLARPRRPVV SKQVIPQPGN
LPPPPPRSSS IPAPSPQPSK APAGVLGTSP KQPVAAVTPK NFYEELPLPP PRPKSRPASS
GRYTPNPTSA PPPAPLSVPQ SIPAPANPYA SIPLAPKSAG DLQSPPELHQ PEKLDPYSSL
LAPAALGAPV VPGAQSRYSP KPPGLQAGTK PLPSPRYSPA PPASTVVAGA PPPRNRYASQ
PSSISGPGAV LPFQPRTSSP LAHHEKISYH PPGVSEERRR SEPAAGLPPP SHAQPFQPPV
IPESQGPVDA GIHENVQPSV TQPNSPPRNP YAPSAYVNEF AKRVAPVQND LPSIGTQNVA
YAPPVGESPF VPPRRSQTQS PSQQLLSPRL SLPPIDPLQR PASVHGATSP TKTVNPYAPA
QVSLHNRALS QSLDFIPPTD GQQLDPLERW KGAPIVKFGF GGIVTSCFPK HIPRYSAGQA
APMIKSCPGE IKICPLNDRL PPAESIVQYP GPLKNKSKKK DLLAWLSSKI AAFENEGDPS
FDPTQPDITK RHEEKILLWK IVRFLVEHDG ALEGSAEAQK SLRSVMFPHL QQSTTDQVPG
DSFIPAATPQ AIDASARSDA ADSHSIESLR DSLVLGEREK AVWAAVDNRL WGHAMIIAST
MDRSVWKQVV QEFVRREVRS TTSRTESLAA FYEILAGNVE ESIDELVPPS ARAGLQMISK
VDGQGPAKNT LDGLESWRET LGLVLSNRSP DDQRALLALG QLLLSYGRTE AAHICFIVSR
AAVFGGIDDP QANIVLLGVD HHRLASSAPL HNDDSILLTE AYEYATSVLA GSPMNTLPYL
LAFKLIHAWS LADQGRKSEA QQYCDAIAAA LKAATKPSGY HNPHLFYGVD ELSARLRQTA
SDAGSSWITR PSMEKVSGSM WAKFNSFVAG EESDAASTGS GKAEEIGPFA KVSGTPTVSR
SPSVSDIYGS YPMGGAQSAP NTGASRYHPV NQYALSSSPE QLRGRSSLDS QRSSSYGFPP
PQRRGSQEPS TPVEMNIYQG MPTYGSPSAA GYQSTPPQTS YMPLAPVEED SAAYSPPDPQ
PAPSQTLDNV SPYQPAHYAP ESFGQPFETN DASATSQFEQ GGYMPPSSGG GYEPPFVEVN
PASASDDVED ESNEGAKPKK KSFMDEDDDD DMAARAAAIQ KAERARRDRE ADEAFRKAAE
ADAQKPPPTT AKKGWFTGWF GGKKEENNSG GGPIRAKLGE ENSFYYDKEL KKWVNKKDPG
SSTPARGTPP PPRGSAPPSR TASGTGGPPP PAVGTPPLAA LGAGSRPSSS AGVPPRLTSS
PAPSALGAPP PIPRSVSTSA TLPTPPDGSA GAPPRPATSL SYASSIDDLL GAPQARKGPA
ARGKKKGRYV DVMAK
