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Protein

COPII coat assembly protein SEC16

Gene

SEC16

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in the initiation of assembly of the COPII coat required for the formation of transport vesicles from the endoplasmic reticulum (ER) and the selection of cargo molecules. Also involved in autophagy.9 Publications

Miscellaneous

Present with 358 molecules/cell in log phase SD medium.1 Publication

GO - Molecular functioni

  • protein membrane anchor Source: SGD

GO - Biological processi

  • COPII vesicle coating Source: SGD
  • macroautophagy Source: SGD
  • protein localization to endoplasmic reticulum exit site Source: SGD
  • protein transport Source: UniProtKB-KW

Keywordsi

Biological processAutophagy, ER-Golgi transport, Protein transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-33991-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
COPII coat assembly protein SEC16
Alternative name(s):
Protein transport protein SEC16
Gene namesi
Name:SEC16
Ordered Locus Names:YPL085W
ORF Names:LPF1W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL085W
SGDiS000006006 SEC16

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1059L → S in SEC16-4; ts accumulation of ER membranes. 1 Publication1
Mutagenesisi1084L → P in SEC16-3; ts accumulation of ER membranes. 1 Publication1
Mutagenesisi1089L → P in SEC16-2; ts accumulation of ER membranes. 1 Publication1
Mutagenesisi1231W → R in SEC16-1; ts accumulation of ER membranes. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000976581 – 2195COPII coat assembly protein SEC16Add BLAST2195

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei28PhosphoserineCombined sources1
Modified residuei73PhosphoserineCombined sources1
Modified residuei144PhosphoserineCombined sources1
Modified residuei313PhosphoserineCombined sources1
Modified residuei472PhosphoserineCombined sources1
Modified residuei483PhosphoserineCombined sources1
Modified residuei595PhosphothreonineCombined sources1
Modified residuei607PhosphoserineCombined sources1
Modified residuei660PhosphoserineCombined sources1
Modified residuei663PhosphoserineCombined sources1
Modified residuei665PhosphoserineCombined sources1
Modified residuei674PhosphoserineCombined sources1
Modified residuei678PhosphoserineCombined sources1
Modified residuei681PhosphoserineCombined sources1
Modified residuei701PhosphoserineCombined sources1
Modified residuei704PhosphoserineCombined sources1
Modified residuei706PhosphoserineCombined sources1
Modified residuei759PhosphoserineCombined sources1
Modified residuei762PhosphoserineCombined sources1
Modified residuei765PhosphoserineCombined sources1
Modified residuei768PhosphoserineCombined sources1
Modified residuei843PhosphoserineCombined sources1
Modified residuei1511PhosphoserineCombined sources1
Modified residuei1515PhosphoserineCombined sources1
Modified residuei1578PhosphoserineCombined sources1
Modified residuei1602PhosphoserineCombined sources1
Modified residuei1603PhosphoserineCombined sources1
Modified residuei1611PhosphoserineCombined sources1
Modified residuei1617PhosphoserineCombined sources1
Modified residuei1778PhosphoserineCombined sources1
Modified residuei1875PhosphoserineCombined sources1
Modified residuei1973PhosphoserineCombined sources1
Modified residuei1986PhosphoserineCombined sources1
Modified residuei1992PhosphoserineCombined sources1
Modified residuei2049PhosphothreonineCombined sources1
Modified residuei2130PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP48415
PaxDbiP48415
PRIDEiP48415

PTM databases

iPTMnetiP48415

Interactioni

Subunit structurei

Interacts with SEC23, SEC31 and SED4.3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein membrane anchor Source: SGD

Protein-protein interaction databases

BioGridi36096, 283 interactors
DIPiDIP-5815N
IntActiP48415, 52 interactors
MINTiP48415
STRINGi4932.YPL085W

Structurei

Secondary structure

12195
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi995 – 998Combined sources4
Beta strandi1002 – 1007Combined sources6
Beta strandi1027 – 1031Combined sources5
Helixi1032 – 1034Combined sources3
Helixi1040 – 1044Combined sources5
Helixi1056 – 1073Combined sources18
Helixi1080 – 1090Combined sources11
Helixi1095 – 1102Combined sources8
Helixi1106 – 1113Combined sources8
Helixi1130 – 1141Combined sources12
Helixi1145 – 1154Combined sources10
Helixi1158 – 1166Combined sources9
Helixi1170 – 1182Combined sources13
Helixi1193 – 1205Combined sources13
Turni1206 – 1208Combined sources3
Helixi1210 – 1219Combined sources10
Helixi1221 – 1229Combined sources9
Helixi1231 – 1240Combined sources10
Helixi1254 – 1269Combined sources16
Helixi1273 – 1282Combined sources10
Beta strandi1288 – 1293Combined sources6
Helixi1309 – 1323Combined sources15
Helixi1332 – 1334Combined sources3
Helixi1335 – 1347Combined sources13
Helixi1351 – 1366Combined sources16
Helixi1373 – 1388Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3MZKX-ray2.69B/C984-1420[»]
ProteinModelPortaliP48415
SMRiP48415
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP48415

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1997 – 2094Lys-richAdd BLAST98
Compositional biasi2078 – 2145Pro-richAdd BLAST68

Sequence similaritiesi

Belongs to the SEC16 family.Curated

Phylogenomic databases

InParanoidiP48415
KOiK20353
OMAiVPNAGPY
OrthoDBiEOG092C01W6

Family and domain databases

CDDicd09233 ACE1-Sec16-like, 1 hit
InterProiView protein in InterPro
IPR024298 ACE1_Sec16_Sec31
IPR024880 Sec16
IPR024340 Sec16_CCD
IPR024468 Sec16_N
PfamiView protein in Pfam
PF12932 Sec16, 1 hit
PF12931 Sec16_C, 1 hit
PF12935 Sec16_N, 1 hit

Sequencei

Sequence statusi: Complete.

P48415-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTPEAKKRKN QKKKLKQKQK KAAEKAASHS EEPLELPEST INSSFNDDSV
60 70 80 90 100
NRTESDIASK SDVPPVSSST NISPANETQL EIPDTQELHH KLLNDSDQHD
110 120 130 140 150
ITADSNDLPD NSIVEHDSVI TQTKPAMSQE YEETAAHLSS RNPSLDVVAG
160 170 180 190 200
ELHNNNEHTQ KIAVSAVEED SFNEEEGENH DSIIISSLND ATPSQYNHFL
210 220 230 240 250
PSDGNLLSPE LSSGDTPTHN VPLGTKDNEI NDDEYCNDKE ISLNANNVLP
260 270 280 290 300
DELSKEEDER LKLETHVSTE EKKQDIADQE TAENLFTSST EPSENKIRNS
310 320 330 340 350
GDDTSMLFQD DESDQKVPWE EDVKKDFHNE NTNNTQESAP NTDDRDKGYE
360 370 380 390 400
GNEALKKSES CTAADERSYS EETSEDIFHG HDKQVVEGQN DFTGKNIENE
410 420 430 440 450
SQKLMGEGNH KLPLSAEADI IEPGKDIQDQ AEDLFTQSSG DLGEVLPWES
460 470 480 490 500
TDKNADVTSK SQEKHEDLFA ASGNDEKLPW EVSDGEVSSG KTENSMQTST
510 520 530 540 550
EKIAEQKFSF LENDDDLLDD DDSFLASSEE EDTVPNTDNT TNLTSKPVEE
560 570 580 590 600
KKASRYKPII EEEAGMRQEQ VHFTNTTGIV TPQQFHGLTK TGLGTPNQQV
610 620 630 640 650
SVPNIVSPKP PVVKDNRSNF KINEEKKKSD AYDFPLEIIS ESSKKGHAKP
660 670 680 690 700
VAVPTQRFGS GNSFSSLDKP IPQSRKGSNN SNRPPVIPLG TQEPRSSRTN
710 720 730 740 750
SAISQSPVNY AFPNPYKIQQ LQQAPIQSGM PLPNTNIPPP ALKVETTVSA
760 770 780 790 800
PPIRARGVSN ASVGSSASFG ARHATQYGLN NGVPPVSPYG QATINLPTAN
810 820 830 840 850
KYAPVSPTVQ QKQYPSVVQN LGASAVNTPN FVKTHRGHTS SISSYTPNQN
860 870 880 890 900
EHASRYAPNY QQSYQVPYTS QPVGPVAGNS SYQSQTRSSY AVPMMPQAQT
910 920 930 940 950
SASIQPHANI QPPTGILPLA PLRPLDPLQA ATNLQPRASN ITAANSLPLA
960 970 980 990 1000
NLPLAENILP EIITHRATSS VAPPRQENNP IKIDNEALLR RQFPIFHWSA
1010 1020 1030 1040 1050
ANKVVYAVPP IPDQSQYMIS SSIVQEIKVT PIDQIIKPND MLKSFPGPLG
1060 1070 1080 1090 1100
SAKLKKKDLT KWMETTIKSI SENESSTDMT IWQLLEMKLN DKVNWKNISK
1110 1120 1130 1140 1150
LLYNSDELLM YLSQPFPNGD MIPNAYRLDI NCQMRVLAFL QTGNHDEALR
1160 1170 1180 1190 1200
LALSKRDYAI ALLVGSLMGK DRWSEVIQKY LYEGFTAGPN DQKELAHFLL
1210 1220 1230 1240 1250
LIFQVFVGNS KMAIKSFYTN NETSQWASEN WKSIVAAVLI NIPENNEDPL
1260 1270 1280 1290 1300
LIPPVVLEFL IEFGIFLTKK GLTAAASTLF IIGNVPLSNE PVMADSDVIF
1310 1320 1330 1340 1350
ESIGNMNTFE SILWDEIYEY IFSYDPKFKG FSSILPQKIY HASLLQEQGL
1360 1370 1380 1390 1400
NSLGTKYTDY LSSSVRKLPK KDILTINLTR ELSEVASRLS ESNTGWLAKP
1410 1420 1430 1440 1450
KLSSVWGQLD KSFNKYIGGD DIDALNKKND KKKVFDGFTP GSSANSSTVD
1460 1470 1480 1490 1500
LTQTFTPFQA QVTSQSYVDT TALLHNAHNV PSHSVLHSKP SNVSKGLVEA
1510 1520 1530 1540 1550
NLPYTHRIGD SLQGSPQRIH NTQFAAAEPQ MASLRRVRTD QHTNEKALKS
1560 1570 1580 1590 1600
QQILEKKSTA YTPQFGQNHS VPMEKSNSNV PSLFADFPAP PKLGTVPSNY
1610 1620 1630 1640 1650
VSSPDLVRRE SIISTGSEFL PPPKIGVPTK ANSSQGSLMY SPSVEALPID
1660 1670 1680 1690 1700
PVVPQVHETG YNDFGNKHSQ KSMPEDESHT SHDNSNADQN TLKDSADVTD
1710 1720 1730 1740 1750
ETMDIEGPGF NDVKNLLPME PNHQPTSTVN PIQTISDDIQ PILQTNVEVR
1760 1770 1780 1790 1800
GTDASKMENS LPSIENERSS EEQPENISKS ASSAYLPSTG GLSLENRPLT
1810 1820 1830 1840 1850
QDENSISETV QSTYLPAGSI SMEAKPISQV QDVPRNVNNK ASKLVEQHMA
1860 1870 1880 1890 1900
PPKPKSTDAT KMNYSPYVPQ STAASADGDE STILKTSPAI YARTHQAHAS
1910 1920 1930 1940 1950
NPSQYFPLVN QANETASFEL SESTSQAQSN GNVASENRFS PIKKAEVVEK
1960 1970 1980 1990 2000
DTFQPTIRKA STNQYRAFKP LESDADKYND VIEDESDDDN MSTDEAKNRK
2010 2020 2030 2040 2050
EEKKNVNMKK ETKPSNKDID DKSNGWFGWL KKDTGDKKVY KAKLGHKNTL
2060 2070 2080 2090 2100
YYDEKLKRWV NKDATEEEKQ KIIESSAPPP PPIVKRKDGG PKTKPRSGPI
2110 2120 2130 2140 2150
NNSLPPVHAT SVIPNNPITG EPLPIKTSPS PTGPNPNNSP SPSSPISRIS
2160 2170 2180 2190
GVNLTSKKAN GLDDLLSLAG GPKPASTRRK KKTARGYVNV MDNIQ
Length:2,195
Mass (Da):241,696
Last modified:May 15, 2002 - v2
Checksum:i757B7A7231BEE6F0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti522Missing in AAC49088 (PubMed:7593161).Curated1
Sequence conflicti560I → F in AAC49088 (PubMed:7593161).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U23819 Genomic DNA Translation: AAC49088.1
U41849 Genomic DNA Translation: AAB68254.1
BK006949 Genomic DNA Translation: DAA11348.1
PIRiS61103
RefSeqiNP_015240.1, NM_001183899.1

Genome annotation databases

EnsemblFungiiYPL085W; YPL085W; YPL085W
GeneIDi856020
KEGGisce:YPL085W

Similar proteinsi

Entry informationi

Entry nameiSEC16_YEAST
AccessioniPrimary (citable) accession number: P48415
Secondary accession number(s): D6W3T2, Q02822
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: May 15, 2002
Last modified: March 28, 2018
This is version 149 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health