SEC16_DEBHA
ID SEC16_DEBHA Reviewed; 2130 AA.
AC Q6BXI1;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=COPII coat assembly protein SEC16;
DE AltName: Full=Protein transport protein SEC16;
GN Name=SEC16; OrderedLocusNames=DEHA2B02838g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382134; CAG85079.2; -; Genomic_DNA.
DR RefSeq; XP_457088.2; XM_457088.2.
DR AlphaFoldDB; Q6BXI1; -.
DR SMR; Q6BXI1; -.
DR STRING; 4959.XP_457088.2; -.
DR PRIDE; Q6BXI1; -.
DR EnsemblFungi; CAG85079; CAG85079; DEHA2B02838g.
DR GeneID; 2913023; -.
DR KEGG; dha:DEHA2B02838g; -.
DR VEuPathDB; FungiDB:DEHA2B02838g; -.
DR eggNOG; KOG1913; Eukaryota.
DR HOGENOM; CLU_231080_0_0_1; -.
DR InParanoid; Q6BXI1; -.
DR OMA; VPNAGPY; -.
DR OrthoDB; 555132at2759; -.
DR Proteomes; UP000000599; Chromosome B.
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; 2.
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..2130
FT /note="COPII coat assembly protein SEC16"
FT /id="PRO_0000295536"
FT REGION 27..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1347..1366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1374..1519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1558..1731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1751..1997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2014..2130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..647
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..842
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1400..1519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1558..1591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1611..1638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1639..1661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1703..1731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1751..1777
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1788..1807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1818..1844
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1895..1912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1936..1964
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1981..1997
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2035..2080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2130 AA; 232928 MW; 5F28BD3DE4653355 CRC64;
MSASFTDDKI LRKSSVVEGG EISEELKILE KEPEHEPSEV VIGNDDDVKD DVKDDVKDDV
KDDVKDDVKD DLKDDVEDDT IAPNQFEEAI KKNKLDPQDQ TAAGDSGRSQ PDLSPRTTTG
VVKPSSFETK DTDGHDSAEV VSGSATQDDD NRNMDHDPIT LVGDKRKSEL QEYIPQTEAD
KEETKDFDPA QEDLTSADKA GKDQTPKVSD ASEAKIDSLP WGPETSTDAK LPWETEDTNS
DNKTADPIPW EQGSSDEASK NDDNLPWESN KNDAPSSQAD NDKLPWESDI NDAPSSQAGD
DNLPWDSNTN DAPSSQAGDG NLPWDSNTND APSSQAEDDK LPWESDINND VPASQEDPEN
KESNDSTNVD DLFGGSHNID FLKEIQKQEE SKDTDEVLLD SSENTPSAQP SSQDQDTSQD
MRNYSTTQTD ISHSEENKLA LQSKNVPKGE NEKTTENSDI HRPQDTDHFD DLFQNDDHDF
LQEVGSSDNK SDPFKFPPDN SAPENKDSDK FETQNKSLDF LEMDDDLLDD EFLEDDTTSQ
TQTLKSKSNK QTYLPSTTNP STTPVVPTQE KPKGSAMNKK KNDAYDFPDS LIAHKFKPAA
RSTNKYAPGS SNHNSPPVAS MPPKLHSPSM NAVGSVPVPN EKQATMSQPL SAAVSTQGLQ
KKSFFEDLPI PVQKQPVKPA RAALPRSQMS QSISPTVNPA QPQLQKPVVN PYAKPAMNTV
VSPPMNYAQP PGMPQVTNNR GGSHLPAGMV APPPPSQITG NNNVLPHAQP QPFPNMQNQN
LGQNTNSYAP SRKISNPSPN LINTALPKVQ GAQSATSPYV PNAGPYAPSS HKRTSSRASS
LIGAKSKEVN PYAPASINVP NAQQGISHGI MMPNTASPTA PPAVMNNSIH GRRRGVSNVK
SNFYHKEQTA PKVENPNALL QRQFPIFNWS SSKNIAYLIP SAVTNTYNRT SESVNVTDIK
YVLKDSHYLS TFPGPFNKLK TKKKDVEKWL ESYNEFLIQN NTGMKQDEVL VSQILLALVR
FNGDCKSDDF TKAACAVLNP SVDYANDNTH MDMNPISTLA NAYRLDNTGI NIIWSLLQIG
NTEKALEFCL SKGDWALGLM IARFEGPEKF GKVASDYART TFPFQKSQSK VHHLMPIMLK
LFAGNFKSAI DDITNVQAEG EWFIQNWREL VSLVVINKPQ HGHEFLCEFS KLLALSGQII
ASQICLILAG LPLSSIPSQA NGILFSVIGF GSHSFAYSET YEYAMQLSTT NIPPTGFAHL
LPLKLKHAQV LADYGLFTES QKYCDAISSI IKATGRSSFF NPVAFQEFQN LLMRISQSGA
SDSGWFGSKK LTLDKMWDQL DKFIGGDESK AKSGENGTFS KFSPAVSRAP SSLDITSLNN
HYPQTSPQVR PDHIRDPLVT TNSAPGTSSE NSVLKSNGMS HSRPPPSLYS NNSTTSIQKY
APSSSQVTPK PTLTRNDQSF SSQQQVGNPV YESLQQSRMA PNNSSSQYLP MNQGQSENIK
APSKYSANPQ KVYSNNNGSL PYMNPSAQFS SSSIASHQSL HMGISGVNAN PLTSVKRPSI
SNSFSESHVN SNPISGHKHT SSLQSDISLD YPSEFKSMPK PASDNPIAPD THSSLKRDTE
NVPETITESR ESEKSSELRD SSNSLTMPSE EGHSTVEDST LPQAPPPKGH SKPNIASSSV
APKKARARAN PYAPGAVASR SGGNNKYGPQ SSDKYTSKKE NTSMLVDTPS DISYNDIFNY
GGYKVPKKTE INDTETLHDR NEVKEAPNQE SIDTKEEASK TNSYIYPEPP KVASTSQSRN
INVDESFDGE NINDHDFETS SLHTPNANVP ASNLNNSFRT NEKESMFHPY QEGENKSRRT
SNFGVDSSFG DFPIPGSPDL TTRANSVIGG PGGLFSSRLS QSQQSALYQQ YEVQDDTVKE
YIPVVDEEED EDSEDESSKK EKRKKEEQER QARIEADRAK QRQDAVASQR NQTWWPGFLA
RKNDDKPKAI RAKLGEKNKF VYDEKLKRWI DKSIPLEEQL KSSAPPPPPA AKKKPTEGSS
SSISKPSSSS TPLGPAKQDM APPASNSSNS APSLGPSQSR PSQSGPPPPA GPSLANAGLD
DLLSLGGGPS SGRKTKKGPR RGYVNLLDQK
