ID A0A1G4JV85_9SACH Unreviewed; 2361 AA.
AC A0A1G4JV85;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
GN ORFNames=LANO_0E08416G {ECO:0000313|EMBL:SCU94855.1};
OS Lachancea nothofagi CBS 11611.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=1266666 {ECO:0000313|EMBL:SCU94855.1};
RN [1] {ECO:0000313|EMBL:SCU94855.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 11611 {ECO:0000313|EMBL:SCU94855.1};
RA Devillers H.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00024687,
CC ECO:0000256|RuleBase:RU364101}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004397}.
CC -!- SIMILARITY: Belongs to the SEC16 family.
CC {ECO:0000256|ARBA:ARBA00005927, ECO:0000256|RuleBase:RU364101}.
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DR EMBL; LT598451; SCU94855.1; -; Genomic_DNA.
DR OrthoDB; 1361743at2759; -.
DR Proteomes; UP000189911; Chromosome e.
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 CDD; cd09233; ACE1-Sec16-like; 1.
DR Gene3D; 1.20.58.940; -; 1.
DR Gene3D; 6.20.50.30; -; 1.
DR InterPro; IPR024298; ACE1_Sec16_Sec31.
DR InterPro; IPR024880; Sec16.
DR InterPro; IPR024340; Sec16_CCD.
DR PANTHER; PTHR13402; RGPR-RELATED; 1.
DR PANTHER; PTHR13402:SF6; SECRETORY 16, ISOFORM I; 1.
DR Pfam; PF12932; Sec16; 1.
DR Pfam; PF12931; Sec16_C; 1.
PE 3: Inferred from homology;
KW Autophagy {ECO:0000256|RuleBase:RU364101};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU364101};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW ECO:0000256|RuleBase:RU364101}; Membrane {ECO:0000256|RuleBase:RU364101};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU364101}; Transport {ECO:0000256|RuleBase:RU364101}.
FT DOMAIN 1130..1212
FT /note="Sec16 central conserved"
FT /evidence="ECO:0000259|Pfam:PF12932"
FT DOMAIN 1273..1562
FT /note="Ancestral coatomer element 1 Sec16/Sec31"
FT /evidence="ECO:0000259|Pfam:PF12931"
FT REGION 1..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 811..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1561..1673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1700..1721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1770..1816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1881..1917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1959..2013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2155..2222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2237..2361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 744..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1572..1612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1620..1673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1700..1717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1771..1809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1884..1917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1960..2013
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2162..2197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2302..2322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2361 AA; 256595 MW; 97B3E341468DD49E CRC64;
MGPEAKKKKN QKKKQKQKQK KDSLKDVESH EATEKHAVNA DAPIESISEG RDDSEQFQEG
SQNDNELTVT HKVQGELGVT ESSVGPGAAK APNPPSASEE GLGLGEKPVS NSANQSAANN
TIADSPEFAA LQDGEMEAET AAERNTLETA SQANNEQDLN ATANSEMRPK SPISSIREPP
LDPDSQVNLA NSDSSATGLK TDIDVFGQGE VFAPSVSLEL KQNSEKHKDE GFSTQLDLSM
APPINGGFSS SGAIELENVQ SEDVVGLKEP PSPREDQVIN FEVSSDDWSR NDYKVSTHDK
EPLPKHDTQV ISGTNIPISS RQSLSSPGRE ESFDNQGVSS ADKHESSRPG NSHLAEDNVH
TVHEHEGDAE SSVVSQSQVL NPTLETEAVK SSDLGNLRVF SESTVSTPEP EQNWERAPVP
HLNSELKSSK STHEDTQQNV LASENFVDLT ASTESINADF EYNKNHVAME MHTAQPKELP
VEQSTEPSQE QELLFTQEPD REPLPWEEQN EVSTKATEET PDISNLQESL LSADRSRVLE
TPGDITFPAQ TDASIGNMFP DDSEVVDEEL PWQSNQRSPS LAKTEDLISS PDLFTKEPKH
GECNYSPERL SSDRDSQNGL LPWEGVENED GDSSVIQHSI NAAEEPKKFS FLENDDDLLD
DDDSFLDSDE DLAEGLAVQV TTEAPHEASD PKIAPLGSSL QQRDLSKSYV PTSTPAVPPK
NAYVQPIARI ISGAERQPSP DKKISKYEPS TQNQSTTSNV SPISSFATVN PSLRTGFAAN
VKPIESIHKQ LDEEKKRSDA YDIPLEIAPR KPKKVNQAKP FGASSSTLSS SNSVAALPPN
QHGTPLPSKI KTTHGGPPIS VNQSAVNPPY RAHAECHGAK INPTLPNAPT SIEQVGYPHV
NTHAPPYLTT AASLPQKQQN SYEPTVNLRT TSVAKDAPAS NRYAPSSTNP EPPKNVNAMY
QYPSQSARIR AFSNVSNGSI GSFGSSNSQS NVPPTSRPYV QVSYADKGLQ QDPYARIEHQ
APLVPALKTA GLSTIGQAAL SPNTQRRSHA RSNSSVYAPA YSSKYAPTVQ PQFQLPSHDG
MNTNYYASAH SGPSAASNSF KPKTNQANLI ADVINEQPVD PHIAFHKQFP IFHWGKSSKV
VYALPSKAES DDYLSSTNLG QKIHVSGYDA IVEPSILLKN FPGPLMKNKN KNKEIQKWIE
DTCAYLSKQQ PLRDLTLHKV LSLKLSPQTA LRSISQTLYN SDELLPFLSQ PSMRKKGSFN
SHKLIENDQL KVLAALQTGN HSQALELALS EGDFALALIL SSLVGKEKWS EVVDIYLREE
FHSINDNSND FSANLLALIF QVSVGNSKHV VKEISTNASK ENWAMNNWKI IISAVLNNVK
HQSSDSSNNS HEVPPLALEF LVEFGIFLHQ RGMIIEGITS FVIADVPLSD HEMVPGSGLK
FKSLGSENSS EGIILSEIYE FYCGTKDPKY TGFDYLLLQK LAHSSALIEC GMNADGTRYA
DYVALALRSL PRNSSLACTV DLRLNFVSSK LIGTNASWLG KPKLSQVWGQ LDKSFNKFIG
GDNEENNADE SGKIFENFTP NGSRNSSKID LSQPSSSFNP AASLNNCNPP NFVPNLGRPP
LHTNVSSSGA LSKGRNPNGS AAHESKYEPS QSQKQWGSTP NHKPSMDATS SFDSPIQTIY
QNSPMRSKDQ LITAMTPPPL FSTSSKKYTN RKGHNTGETN PFEMKVAATD NLLTSQPHSG
LKRSIKGETP ANAALLADLQ VAPPPIFGSS SIYKSRRNSA QSRSSAQSQY SNLSSPKHVP
ISLASSGPSY SPDLARAESY QAQQLSVRDN TSTGGYLSSE GLSQEKCLDV ENSATNTLQT
LKGDLDGEAS QGHIRDLYDE SEATNEEGTN GFQPLQNNSS APESVSEVRE TDIVTSQISD
AETVNEKLGV ARKLSVGTEP VSNAHASYFD IEISKNERRE MQAVSSAPKQ SNLGSNNGNN
PYAPAQSGRT TKSSHNPYAP TKSQSDLDNH GTLKLMDDTN QEASQEELNM FSYGGYNVQE
TFAPEAQADK FDDGKAAKHF NQYNVEGTSN LEHSICPVQD LTPIEEKIPT PALEPRFQPV
SSKKLSLSIS SEEGDKLFSS ISAPVIRPSS NPSFKPFTPA APAAEEYYDD IVENESDEDE
EATEAAKVKK AEEAKKAEAK AKKREERDKD ERDKSQHGPS WFGWLRKETN EKKPVKAKLG
HQNTFYYDDK LQRWINKNAT EEEKQQVSTP PPPPPIIKKK AEGSPKVKPR TGSIAGGAAA
RTAAFVPPTN PLSKDPISAA GLEKDTSNSG SPSVSPSVSL SGKKANGLED LMSLVGNAGS
QTGTRRKKKG TRGYVNVMNN M
//
