SEC16_ASPOR
ID SEC16_ASPOR Reviewed; 1843 AA.
AC Q2U968;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=COPII coat assembly protein sec16;
DE AltName: Full=Protein transport protein sec16;
GN Name=sec16; ORFNames=AO090701000149;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(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; AP007164; BAE61897.1; -; Genomic_DNA.
DR RefSeq; XP_001823030.1; XM_001822978.2.
DR AlphaFoldDB; Q2U968; -.
DR SMR; Q2U968; -.
DR STRING; 510516.Q2U968; -.
DR PRIDE; Q2U968; -.
DR EnsemblFungi; BAE61897; BAE61897; AO090701000149.
DR GeneID; 5995087; -.
DR KEGG; aor:AO090701000149; -.
DR VEuPathDB; FungiDB:AO090701000149; -.
DR HOGENOM; CLU_001147_0_0_1; -.
DR OMA; LERWKGA; -.
DR Proteomes; UP000006564; Chromosome 5.
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..1843
FT /note="COPII coat assembly protein sec16"
FT /id="PRO_0000295531"
FT REGION 1..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1385..1691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1706..1843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 480..508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..552
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..609
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..685
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 825..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1431..1490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1568
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1601..1657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1843 AA; 194829 MW; 8E3C7F3A23B6BCF8 CRC64;
MAHNEVSAAW HPALRSEDGV PSNAPVSDDL TQVSKDSMTE SAAELKPSEA VIQENDLHSS
STSPDTDASV NVQSTAVPAV LDSDTPVYAE QVLNQENAQK NTAENSAQED APDHGQELSQ
TISDEPHVIE TSEESAPTLG AAFGSDANGS HDTAAPDYMM DEPSPAEHDT TERREDNDAA
SWFNEQVDSG DRQTTNEFVN DDNQDFWGSP TNGDAGDDFF NQLKTQTKPI YIPPETESRY
EEGVPLLDNT VESPVQPSMK EESQIDKIFE DDGDDEGGAF FNEVQGSVPN EGVPSPPITR
KSTTQVIGSL DASPDSPVSP ASSTAQEFNN ILAAAASENQ VKEDLSDDDL AAKWQAELSD
DQPEKSTEDD LAARWQAALD DDDDLLLEDE IGKGPNNGQE SLPQNPNGSV HETTQATLSS
PFGTPQSSAR PQAQPTSYTP HQPSTSDLLQ GIPGIAPQSS AAPMQDYFAP PAQPRPTTKR
AESFAERSKE GYKSPYDLPD DLTRPRKPVV THKPVVAQPG SMPPPPRSSS IPVPPTNAPG
VPTPPPAPST VPAVTTPKNF YEELPLPPPR PRSRPASSGR YTPTANIVTS PPSHSQPPPP
PPANPYASLS PPPQDSGSVG SQTQLQQPER LDPYANLLGP GAPGAPAAPS AASRYSPKPP
TLQPGTKPPS APRYSPAPPQ SAAPAPPRTR YASQPSSVSS QGAVLPFQPR TSSPLAHHEK
VSYQPPEGLA IRSAPESASS YAPNGMQPRP NQQDVSNSIT APVGAAGSAA VTAVPENVSA
AIQPTSPPRN PYAPPAYINE FSKRVAPMAS PPPAVVPPTG DAQFVPPRRS QTQSPSQQAS
APGLSVPSDS LQRPASVHAP ASPTKSANPY APSQISIHNR VPSQPLEFIP PNDGQELDPL
ERWKGAPIVK FGFGGSITSC FPKHVPRYAA GQAAPKIKST PGEVKIFSAN DWVPITEGIV
QHPGPLKNKS KKKDLVAWLS SKIAAFENEG ISEAAQLHPE SSKRHDEKIL LWKIVRALVE
HDGVLEGSAE VEKSLRYIIF PHLQNSEPES TSGVNLPAFN ALPPLNAPSQ SDATDSQSLE
SIRNSLLVGN REKAVWDAVD NRLWGHAMVI ASTLDRSVWK QVVQEFVRRE VKSTTGNSES
LAALYEIFAG NVDESVDELV PPSARAGFQM VSKVGGQGPS KNALEGLDSW RDTLGLVLSN
RSPEDHKALL ALGRLLLSYG RTEAAHICFM FSRAAVFGGA DDPQTSIVLL GADHQHLPLN
VLQDDDAILL TEAYEYAVSV LAGSPTSTLP HLLAFKLIHA CSLAEHGRKS EALQYVDAIT
AALNATTKPS GYHNQHLLFG VDELSARLRQ TTSDSGSSWI SRPSMEKVSG SMWAKFNSFV
AGEDSDAAST GSGKAGDGDI GPFAKFSGTP TVSRSPSVSD FGPYSLPAAQ SVPGSGPSRY
QPGNQYVPNS SPEQYRGRSS LDSQRSSSFG FPFGQRRGSQ EPSTPVESSM YQGGPLYGSP
SAAGYQSTPP QASYMPLAPV VEDSAPQPYP VEPAPMQGSP VNISPYQPPA NESFGEPLDQ
SSATVPASSM AGYVPPGAGG GYEPPSVEIS AAPALDTTEE PTHQDVLKKK KSFMDDDDDD
DLAARAAAIQ KAEKARKDRE ADEAFRKAAE ADAKRPPAAK KSWFGGWFGG AKKENDNNNN
SGGPIRAKLG EENSFYYDKE LKKWVNKKDP NSASVSRGTP PPPKASAPSR SASGSTAPPA
ASMGLGLDSR PPSSAGAPPS LSSSPAPPSL AAPPPMLGTA RSASTSAAMP TPPIGSSLPP
PPRPATSLSN ASSIDDLLGA PQARKGTSAK GRKKGRYVDV MAK
