SEC16_CANGA
ID SEC16_CANGA Reviewed; 2238 AA.
AC Q6FRV6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=COPII coat assembly protein SEC16;
DE AltName: Full=Protein transport protein SEC16;
GN Name=SEC16; OrderedLocusNames=CAGL0H05577g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380954; CAG59971.1; -; Genomic_DNA.
DR RefSeq; XP_447038.1; XM_447038.1.
DR AlphaFoldDB; Q6FRV6; -.
DR SMR; Q6FRV6; -.
DR STRING; 5478.XP_447038.1; -.
DR PRIDE; Q6FRV6; -.
DR EnsemblFungi; CAG59971; CAG59971; CAGL0H05577g.
DR GeneID; 2888609; -.
DR KEGG; cgr:CAGL0H05577g; -.
DR CGD; CAL0131878; CAGL0H05577g.
DR VEuPathDB; FungiDB:CAGL0H05577g; -.
DR eggNOG; KOG1913; Eukaryota.
DR HOGENOM; CLU_000768_0_0_1; -.
DR InParanoid; Q6FRV6; -.
DR OMA; VPNAGPY; -.
DR Proteomes; UP000002428; Chromosome H.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
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 PANTHER; PTHR13402; PTHR13402; 2.
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..2238
FT /note="COPII coat assembly protein SEC16"
FT /id="PRO_0000295533"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 757..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1547..1577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1600..1704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1732..1766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1809..1901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1928..2102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2133..2238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..345
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 394..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..518
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..549
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1547..1573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1601..1674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1676..1694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1732..1747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1821..1851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1939..1954
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1994..2027
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2035..2052
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2053..2070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2071..2091
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2238 AA; 247422 MW; 8BF0BA3E2602FD0C CRC64;
MTPEAKRKKN QKKKLRQKQK KAAEKATDLP ATDQSVNISG AEDALTSNSN VSTPDYTSNF
EISVTSTQEV NVDSQLSQNQ NSDNFINEQK ENDPQSETVF DSHEDIESEM KDNYHNDIKN
TTEAITFDTA QNIIGGSIDS SNTVKSEDKI NESSSKISDP DCQEDILKLE LEGQPLESSC
NDDKESVVEG NNENDNNDDL VNDHPTAEDG SDFFDNLASN NTEVELSSTQ NSNLLTENRL
ESEEFGKPEK LDYPKELSYS EEVDLVEEVD HVEEVDHVEE VDHSEEEDLV EEVDHVEEVD
HSEEVDHSEE VDHVEEVDHS EELLTSSVST QTGMAENTIR HVDESNLGQQ KMEERNINSD
THKDATARVS DFHANDEFET GPAAQINSLI EMNDDEQSVN DLQDESSLLQ EETTFSQIPK
NEVNTENQEN IGSESVSKIN VANENSMESA IEDLFPSMHN TNEQNPWELP QQGENVVENE
VSHEENQRIT ETTKDDSDNI DRILCDREDK KEDSFDDLFG NNEVGDDVPW LQESMKSEEG
EKHHQSSTAK EESPANVRTS DNTASQDNDT LPSESVKSNQ QQNVESSSDR QQTSADTVKK
FSFLEEDDDL LDDDDSFLES EEEIEELESN ETVQINELTQ EMSTSAESKK LNHNPYRPSS
HSSINTQMDP KYNNYQTVPN SSTAPTGIVR PQQITTFLPT NNAQTNTPGT ILSPIQTTNE
KVKKLTEEKK KSDAYDFPIN LVSSTVKKGH AKPVGVFTNQ FSRNGSTPTT PKINPHSRNS
SVNPAQIIPK NPYASIQQPN PVIAPTTNMI NNPINMMPTA RMRGNSAVST TSGKSVGTSV
ATKQNPYSPQ ITKSPRASIS QPAGIPNNSK YGPISPSTSQ FNSLGQVLDS GLVHSSTTPM
GSTLSPISTK LNANNQPSPQ SKQYPGNSSY LPSQNDSRSK YAPAFSTGQY AGYSSHSKPA
VNQPALPFPR KQSESAGDAN PPINTVLPPG IRKTNVLLES QQNLRQNANY PTYAEHSHEQ
TNSYNVHGAS NKKIVNNNAL LVKQFPIFNW GSNNKVIYGI PLGQNDSVMM PTNSPLQNLR
MIGAEILIKP TQLIKSFPGP LCGSKVKKSD VEQWLLTASK DADVDEEAAL LLSLLKLKLS
TTSTFKDMAT LLYDTATLHE YLAQPLTSLN QAPNAFSLDP ESQFRVLSFL QVGAHDDALR
FSLEKKDYSI SLLIGSLLGK DKWCEVVQRY LSEQFTAIAN NSNLWAHLLP LIFQVFVGSS
KTAVSRFYKN QEEANWAAEN WRGIVAAVLI NITDHSQPKQ TASIQTPPAV VTEFLIEFGI
FLKKLGMNLP ASILFVIANV PLSNVPILPD SDVHFRSIGS TNNVLGAILS ETYEYTISQD
LKFKGYPATL PLKLFHAYCL QEEGLTSLAY KYVDYLSSAT KSMTKKDAES LNLSHHLSIL
TNRLAGSSSS WLGKPKLSSV WGQIDKSFNK YIGGDDDLPK PATEKKVFDS YTPSSSTNSS
MIDLSHSVSN FMPAQINQLS RNNLNSENKM STVPDLTAFG EKNAFEPPTN TWTGMSLQGS
PQRAVSNMKP PLSNRPNLRR IKTELPSGED ELLSMTVKQG KKSYAPDNLN RASNSSNETL
KSSQSANNSV PYHQSTPNLI GMQSVEQKKS YYPSNQRAMR KSAMPTQPEN LEISRNARSY
EPHTKTKKVY KPNQTLEEEP PIQSYNDDVV SQNQFEEAPN LQNDQEKILQ PTASPEGLSQ
TRISNYSPER PPLPVYSEDS KNMDPKNISD LVKEQQITDK SLEHELEQLP TENDADYKIS
NANEDNAINE EEREIGNGEV ELNVDQSQSH LSASIPQTQN DRESTTVSIS PGLGLEMDVD
KEDSNAPAPK LFSEKPNPSP YAPPTVGKKG TKKTSYMPKG KTESFIAEPE ISSYESSPLD
MYAYSGYRPQ EKEKSTSSIV EESSQISNED APDKSSIAAR QAVELKQDEV SKKPITTKLS
TPKSLPIPPS PFANPLANNN TTGVLPTENF EPVIKVSRNT TARAFTPVPP ASDQYDDVVE
EDSDDSDDSE DDSPMQSNNS NNGNSERNEN KQNDNYSDDE MPTKKKSHDN NDAGSGWFGW
LKKDTNEKKA VKAKLGNQNS FYYDEQLKRW VNKNASEEDK QQLATPAPPP PIVKRKDTEP
KTKPRSISGV TPHLDTGIGS SIPPISGNAP PKPKSGPSLA AKTNGLDDLL NLTAAAPATS
TRRKKKGGRG YVNVMENL
