ID A0A091CUW9_FUKDA Unreviewed; 2000 AA.
AC A0A091CUW9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
GN ORFNames=H920_17126 {ECO:0000313|EMBL:KFO21485.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO21485.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO21485.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO21485.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in the organization of the endoplasmic reticulum
CC exit sites (ERES), also known as transitional endoplasmic reticulum
CC (tER). Required for secretory cargo traffic from the endoplasmic
CC reticulum to the Golgi apparatus. {ECO:0000256|RuleBase:RU364101}.
CC -!- SUBUNIT: SEC16A and SEC16B are each present in multiple copies in a
CC heteromeric complex. {ECO:0000256|RuleBase:RU364101}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004406}. Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU364101}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the SEC16 family.
CC {ECO:0000256|ARBA:ARBA00005927, ECO:0000256|RuleBase:RU364101}.
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DR EMBL; KN124375; KFO21485.1; -; Genomic_DNA.
DR STRING; 885580.ENSFDAP00000012818; -.
DR eggNOG; KOG1913; Eukaryota.
DR Proteomes; UP000028990; 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:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006914; P:autophagy; IEA:InterPro.
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; 1.25.40.1030; -; 1.
DR InterPro; IPR024298; ACE1_Sec16_Sec31.
DR InterPro; IPR024880; Sec16.
DR InterPro; IPR024340; Sec16_CCD.
DR PANTHER; PTHR13402:SF13; PROTEIN TRANSPORT PROTEIN SEC16A; 1.
DR PANTHER; PTHR13402; RGPR-RELATED; 1.
DR Pfam; PF12932; Sec16; 1.
DR Pfam; PF12931; Sec16_C; 1.
PE 3: Inferred from homology;
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};
KW Golgi apparatus {ECO:0000256|RuleBase:RU364101};
KW Membrane {ECO:0000256|RuleBase:RU364101};
KW Protein transport {ECO:0000256|RuleBase:RU364101};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Transport {ECO:0000256|RuleBase:RU364101}.
FT DOMAIN 1188..1285
FT /note="Sec16 central conserved"
FT /evidence="ECO:0000259|Pfam:PF12932"
FT DOMAIN 1358..1592
FT /note="Ancestral coatomer element 1 Sec16/Sec31"
FT /evidence="ECO:0000259|Pfam:PF12931"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 36..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 534..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1630..1652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1679..2000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..797
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1099
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1688..1718
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1831..1892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1893..1915
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1960..1988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2000 AA; 215106 MW; 61FD0CC0705A7291 CRC64;
MQPPPQTVPS GMAGPPPAGT PRSMFWGSSS YRRLASSSAL TAPPCPQQPV TDPFAFSRQM
LQNSALGSPS RSSLPAGHDS ALPVFSQWSG LPMPHASAED GTRGPQESPP GPLSQPGADP
FPAASVPASL PGHEMCRTAE ISSTSGSEVL TPLHPPHHIP GGGPDLSHGG HQHGGGTGPE
QALSGHTLSD GGVAPAIAAA ASPYLPQPRP QMPAQWGPVQ GSPQPSQQHP LPCPEGPVQS
VGPQATSTPH FPAPSSLHHS PACEPHTQLG SLAPLASGRG SEVTPLQSGN HSADNFHSEN
SFGHNSRIGN MWENQELRQN PGVNKAHLRD PAPGNPLTLG NSPENHTHYP PGAGTGQAPL
ETASGTLSMF FQGEETENEE NLSSEKTGSV GRLDFDGFSP SPGLGHLHRP AHVTGSVQQA
FLQGSHGETT QQEGDTQPYF SQSVSIQNDR QATDSAASDT WGDTASAGAY GTGSSQYENV
ENLEFIQNQE VLPSEPLSLD ASSPSDQFRY GPLPMPPVTR HGTVGLTRGG VLHLEAPDTP
VHPVRSDSLS SSYSSQSHRS LPGSARSQEL VGTFIQQEVG KPEDESTGSF FKQIDCSPVG
GEIEEVGGSQ NYYSTLSQPS TPSPPKPTGI FQTSANSSFE PVKSHSVGVK PVEADRANVV
GEVRGTHECV KKPRSVATPP NTSLGNLEQP PDNMETLFAP QACPQPLPPT GEAGHMAPPL
DTVRPTPEKR PSARAQGTVK CESPATTLWA QNELADFGGN VLLAPAAPAL YVPAKPQPPA
VVQPPEEGLP GQPSRKPGPV HPLQSRAHPG ASENLENPPK VPQAASNIES PPTEGQSQNS
AQTPTSSAMA NADQKLPPQP PRSSSVSAVS TDSSQAAMRP EQPWLQPPPS SAFGPPPQDL
ASYYYYRPLY DAYQAQYPAP YPSDPGTASL CYQDIYGLYE PRYRPYDSSA SAYTENYRYP
EPERPSSRAS QCSDRPPARQ GYPEGYYSSK GGWSSQSDYY ANFYSGQYDY GDPGRWDRYY
GSRFRDPRTW DRRYWYDSEY EPHRKESYSY GSRPEKGDDH WRYDPRFTGS FDDDAEPHRD
PYGEEVDRRS VHSEHSARSL PSRRSSLSSH SHQSQIYRSH NVTAGPFEAP PAPGSFHGDF
AYGTYGSNFG GAHGFADYGY PVDSWPAAEQ VPSRPTSPEK FSVPHLCARF GPGGQLIKVI
PNLPSEGQPA LVEVHSMETL LQHTAEQEEL RAFPGPLGKD DTHKVDVINF AQNKAAKCLQ
NENLLDKESA SLLWNFIILL CRQNGTVVGT DIAELLLRDH RTVWLPGKSP NEANLIDFTN
EAVEQVEEEE SGEAQLSFLM DSQVTATSAL EKETERFREL LLYGRKKDAL ESAMKNGLWG
HALLLASKMD SRTHARVMTR FANSLPINDP LQTVYQLMSG RMPAASTCCG DEKWGDWRPH
LAMVLSNLSN NVDVESRTMA TMGDTLASKG LLDAAHFCYL MAQVGFGVYT KKTTKLVLIG
SNHSLPFLKF ATNEAIQRTE AYEYAQSLGS HTCSLPNFQV FKFIYSCRLA EMGLATQAFH
YCEVVAKSIL ARPSLYSPVL LSQLVQVASQ LRLFDPQLKE KPEEESFLEP AWLVQLQLVH
RQVQEGTVPC GQDAAEPQRC PSTPGSEVEQ LDGPGLSRLV GLGTEPSLLP GPECLSPVGQ
LPPSALQSLP AGQPPHPARV PMYPVPLPLD PQEPGPGYGP PGSALSFPES PRPEPVALYP
GPGLPLGTPS LQDSGPLLQA WSPDPGMAPQ ESPVRNPLPE PSEEDFGGNF ANLGSPRTAQ
DLETPPAWDG AGSGSPQPAP PPTPAPEAKK AAPAARKETR EPKKSESWFS RWLPGKKRTE
AYLPDDKNKS IVWDEKKNQW VNLNEPEEEK KVPPPPPTAF PRAPQGAPPG PSGPPAASVN
VFSRKADAEE PQLAGGAGSG GQVPTGAQAD LEPVEDPKLS RWSSGSSLSW EVGQHFQQAS
TTSGSLRPGR IGQRRYPTLN
//
