SEC16_CHAGB
ID SEC16_CHAGB Reviewed; 1865 AA.
AC Q2GXM1;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=COPII coat assembly protein SEC16;
DE AltName: Full=Protein transport protein SEC16;
GN Name=SEC16; ORFNames=CHGG_07283;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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; CH408033; EAQ86030.1; -; Genomic_DNA.
DR RefSeq; XP_001224939.1; XM_001224938.1.
DR AlphaFoldDB; Q2GXM1; -.
DR STRING; 38033.XP_001224939.1; -.
DR PRIDE; Q2GXM1; -.
DR EnsemblFungi; EAQ86030; EAQ86030; CHGG_07283.
DR GeneID; 4394275; -.
DR eggNOG; KOG1913; Eukaryota.
DR HOGENOM; CLU_001147_0_0_1; -.
DR InParanoid; Q2GXM1; -.
DR OMA; LERWKGA; -.
DR OrthoDB; 56582at2759; -.
DR Proteomes; UP000001056; 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 PANTHER; PTHR13402; PTHR13402; 1.
DR Pfam; PF12932; Sec16; 1.
DR Pfam; PF12931; Sec16_C; 1.
PE 3: Inferred from homology;
KW Autophagy; Endoplasmic reticulum; ER-Golgi transport; Membrane;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..1865
FT /note="COPII coat assembly protein SEC16"
FT /id="PRO_0000295534"
FT REGION 1..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1301..1339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1355..1665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1681..1842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..482
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..643
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 721..737
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1379..1411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1435..1468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1469..1483
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1566..1624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1710..1733
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1739..1756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1865 AA; 196681 MW; 8A09CC40A35DAAD5 CRC64;
MVSDAPNSSW HPAMMPNSIA DLRNRREDTV PPSAPEGSVL EDNTTQSNTA GEESGAWFQD
DGTGDDWLAD TNNAPESEPT PAPASAPDTE TPEQTGPAES VEEAVPEESS TTSKHLSTMS
FTRTVPHEVN WNDDDDAEWS LPRTDTDPFK FIPETNRTNS FPTVSPLEDR AHGAAQEFDH
PISFNPAEDL IREIEEEESR EDGTLPGAAA ESATQNAQDD TTTQQYLTGG PDAVANDALG
ARFEEGLPLV SSADQDATQE GQQEAGGDLF AEETVGEEDD FFSNVRSDEA TQQDDDFQPT
PVQRKSTMDV LNSLDMPSTG TGFVPLEETV EEPEAQESPQ DQPKAQEGEN LDEKWKEMFG
DDDAEEGFLP DESTGPNELD ASAFLGSDDE GLLEDSETEQ QEQSQPLASP GYVSASGPSA
QPVNGQYFPH NQGPAVPTPT NPYLPAVSPV TPAHSYLPAA PVSAAQPPTA APYAPPSTAP
PAPALAQFGY GAPPPTQEKN KAQSFVDKKG GYTSPYDLPM EVVKPKRRAG ALPLQNNTSG
PNSPSTMPPP PRSASMYSQP SPSTGAPTPG TARPASSHSA QAPSSGRKPS HESFFEDLPM
TTKPRPASRP KPKSAAPNLV PAAPPVASSR YSPAPPGAPL TNGPAPAPVS SRYSPAPPAP
RQPSGGHERS RAHAPVGHVE GSLAERRSSS SLHDHRLQRV PSLPSTREVE EEEVPTQAQA
SPGGPAPPHP MSPPVSRYAP SPQGARQTPP HTAPSGQTVL SPPKRVMSSH SPLAPPYDFA
PPPRSQTQSP GALYGNRATK PVEPIPRPSS VHDPTSPREA AYPAAPASFA PVAPATTYGR
PRVPRYGMNQ SIPAVIRSPG EVKIQNIKDI IPFEERLAKF PGPLKGKSKK KETIAWLTAG
IESLEQGLPT SFSLHTPFSH DDKRAVERVL LWKILRVFVE HDGVLEGNPT VDKAVRDLLS
PGLEGADSTT PYVNGGGNFG LADPASAGLQ SDGVSSSTVE QIRRQLLSGD HEKAIWAAAD
QRLWGHALLL SNALAPNLYK QVAQEFIKKE VNSPGRNNES LAALYGVLSG NHEESVDELV
PSHARAGLQL VTTHAASSPS KDAMEGLDKW RETLGLILSN RSTDDGRAIN SLGVLLSGYG
RAEAAHVCFM FARNHTVFGG LDDPASHFVL VGSDHKKQAE QFAKEIEPLL LSEVYEYGQS
LAGGFSVPVT NPHLAAYKLQ HAIALAEYGF RDKALQYCDA IATAITSQTK RSPYHHPILE
NAVEDLMMRL KQAPREDSGS WIPKPTMNKV SDTVWSKFNK FVSGDDDGSG QGPTGEGEPG
PFSRVAGGTP TISRSPSASN LETFGAAVPS YGMSSSLPNG PVPASAPATR AASRYAPGAP
QATGSNSRPS TSAYAPRSSM ERTSSELNRG SFEVPRRSLE MQAGHRGSYS PVRSGSPAAM
YTPQSTDFGS PQQSPYQPVS HAQPTPFQAP TSAPQPVGYP GPPANGVAPG QESEAPGQSP
EASGYQPPSY GYEPPSFTPY EAPTEEKDGT PEETPNGGSY EAPSYQPYSY EPPSYEPDTQ
PSNEDAGSDD ESKPKPKKKG IMYDDDDDFP TPRPAEKSRA EKDRENDEMF RKAAEEDAQR
VEAAKQAKKG WGFTSWFGGG GAKKDAATPD SKGANPNKPI RAKLGEANSF YYDPELKRWV
NKNAGPEDTA KKATPPPPKA GAPRSVSASP ASPPFSPGPG RGASAPPPMG GAGGPPRSAS
RPPTSSGSTD TTGLPGSPGS VAGGALGPPP GPVAMLRSVS NTSTASAPPL GGGGSGVGGG
GGGGPPPSSR PPTSLSNSSS IDDLLGAAGP RKPGAARKAR KGARYVDVMG EVKGWRGGEE
WVRLG
