SEC16_PICGU
ID SEC16_PICGU Reviewed; 1825 AA.
AC A5DH19;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=COPII coat assembly protein SEC16;
DE AltName: Full=Protein transport protein SEC16;
GN Name=SEC16; ORFNames=PGUG_02570;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH408157; EDK38472.2; -; Genomic_DNA.
DR RefSeq; XP_001484841.1; XM_001484791.1.
DR AlphaFoldDB; A5DH19; -.
DR SMR; A5DH19; -.
DR STRING; 4929.XP_001484841.1; -.
DR PRIDE; A5DH19; -.
DR EnsemblFungi; EDK38472; EDK38472; PGUG_02570.
DR GeneID; 5127136; -.
DR KEGG; pgu:PGUG_02570; -.
DR VEuPathDB; FungiDB:PGUG_02570; -.
DR eggNOG; KOG1913; Eukaryota.
DR HOGENOM; CLU_232483_0_0_1; -.
DR InParanoid; A5DH19; -.
DR OMA; ESHENGY; -.
DR OrthoDB; 555132at2759; -.
DR Proteomes; UP000001997; 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..1825
FT /note="COPII coat assembly protein SEC16"
FT /id="PRO_0000295542"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1206..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1322..1353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1387..1696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1712..1825
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1206..1245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1387..1401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1486
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1529..1543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1544..1579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1610..1631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1652..1671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1735..1759
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1760..1783
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1825 AA; 195632 MW; 168AFDF9424886DC CRC64;
MESDAGAQQP PEASENSNMY GGYQTETESD PLVYKSDNNH NPGSTNLDGP NSIVAQTEPN
AVSERRTSVL QQADDVLPRH SSIDDAIASV ARQSAGFSED FLRRDSRVSA SHSSHNEAGH
HADSEQLETR LPVPENVQEH NNVSNTENHE STGAPADDSF FSELASRPET SEQFFSTHAQ
EEITPLVDPL QEVDERRESF PWEESKEGAD FFSSLGNSEH NQTPASGTEE HEQSHVSTSF
NEEETAITHG NEESIPWPSY DENSHEAHAQ HTSEGAQETD SVAPSAHTVH ESDSTPTPKP
DSTNELDELF AGDDDDFLQE IVKDQEPVTS NGNQDTKTPS SQEPEPAEES QVKKKDSFAF
LELDDDLLLD DDLLPDEEDE GEINSNATVV QPQTTTTSRY SRPSQPTSTS SSFSKPVAAQ
EFNKKLEEAK KKHDAYDFPS NLLHSSIKPA PRTNNKYAAP SGSAGSPNSA SASAPPPSST
TSLPLHPQAA PGVAQENRPP LQSHSSAPNQ APSKSPAKKS FFEELPIPTP RAAVRPARSG
PSKPSPVTAK PAVGQAQKKP TQPPVNPYAM QNLKTPSAAS SPASAVPQVT LPNAPVGPVP
PVAPIGGVVA PGPFSDMASV APLPQSAPQN SLSATPNTTS QPRKLSNAGS SPYVPKVGPY
GPSGHTRHHS RASSLVGAKG KEVNPYAPAL SPVNASGGQM SPQNQASSLS AVAPPTAHSS
ATASRLRRIS NPRSIYGNAV AQQLKPVDPN IRFQKQFPIF NWGLNNNVSM IPKNMQRNIN
IKQLTGGAFT EILKSFPGPL SKKSKAKDVE KWLKTKVTHL DSSTPNVATN EAKLSDEVGE
ILAALVASNG DVRSQEFIST ACSVLNPHHY SQVEAMATPQ GSNHSATAYK LDNSGSNQLL
TYCQAGQTDR ALELCVAAGD WALALIISHS MGPQAFGKTA SDFARTSYPF QKSQSKLNHL
MPIILKVFSG NVKSIIEDFQ NVATELEWVL LHWRDVVTSI AANAIQNGKV NEFLNEFGQL
LASHGNFIGR DVCFILTGAP LSPSFSVVGG DSQMGLFYTE IYEYALSQRS AATANTLLPT
LSVKLHHAQL LADYGLNVDS QRYCDQIGAS LKTTKQQVPP AIIHEFQRLL VRVSDTGAND
QSWYGGIGKI NKMWGQLDKL ISGDENTEKK GETGLFSKFS PSVSRNASTT DIHALDRPEF
HSMVSSMSAP ITPGEQYGRT PSSVAPVTSL SGVSSSQTSN PLTSVPRYAP PAKNSRPQQS
PQQPTRSHDM APHSGSRYAP SNASSSNLGN PEEAIQSRKP PSKYSRPAQV GAAFSYNNPV
AEASSSSIGS YGSHAVPNPP PATQGHTKQP SFNSIVSNDY SVIRDHNRSP SVQSDISLDY
PVDFRERIAE SKQESEENAD IKQLNEIPTN GNGNENTQAQ SSKDQSSPLP YANQSGTTMD
STEVASQQSQ QPPPPPPKLT QTPTQSPSRG PPPAVSRSPS QPPKANPYAP GARTNKPRGR
NRYGPPSALG SNAPSVPEVN GNRASEEPKN VNPKVHEEKT SNIDDSFTSS YQEDTQMSSP
SLMLNHNQGA INQTERPNSK FGLGDEFPIP GSPEVTTRAN SVYGGHGGFF SSRLSQSQQS
TMYQQYEVTD DTVQDYVPVV EEEDEEEDAP KSQSSQPAQN GSKSAANAKG QTGLFSIFGM
RKNDGKPKPI RAKMGEPMKL VYDEEMKAWI DPSIPRDQQL KKAAPPPPPK MKTSAKPSNV
PSVGEAPSQQ HTPQTGPVLP PGNSSGPTPK PIGSGPKPPA PRAGTKPQLA NANLDDLLSL
SSQPGAAGRK PKRGARRGYV NVMEQ
