ID A0A0D9RTG0_CHLSB Unreviewed; 2365 AA.
AC A0A0D9RTG0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Protein transport protein sec16 {ECO:0000256|RuleBase:RU364101};
GN Name=SEC16A {ECO:0000313|Ensembl:ENSCSAP00000011899.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000011899.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000011899.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000011899.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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}.
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; AQIB01148133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01148134; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 60711.ENSCSAP00000011899; -.
DR Ensembl; ENSCSAT00000013915.1; ENSCSAP00000011899.1; ENSCSAG00000015852.1.
DR eggNOG; KOG1913; Eukaryota.
DR GeneTree; ENSGT00940000159324; -.
DR OMA; YKSPYDL; -.
DR Proteomes; UP000029965; Chromosome 12.
DR Bgee; ENSCSAG00000015852; Expressed in pituitary gland and 7 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IEA:Ensembl.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0006914; P:autophagy; IEA:InterPro.
DR GO; GO:0048208; P:COPII vesicle coating; IEA:InterPro.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IEA:Ensembl.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IEA:Ensembl.
DR GO; GO:0032527; P:protein exit from endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl.
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:UP000029965};
KW Transport {ECO:0000256|RuleBase:RU364101}.
FT DOMAIN 1450..1549
FT /note="Sec16 central conserved"
FT /evidence="ECO:0000259|Pfam:PF12932"
FT DOMAIN 1622..1856
FT /note="Ancestral coatomer element 1 Sec16/Sec31"
FT /evidence="ECO:0000259|Pfam:PF12931"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 435..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1214..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1303..1379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2028..2187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2228..2336
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 62..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..302
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1303..1356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2099..2160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2231..2245
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2276..2315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2365 AA; 252349 MW; 8D2AC1D0E3B7E64E CRC64;
MQPPPQAVPS GVAGPPPAGN PRSVFWASSP YRRRANGNAA VAPITCPLQP VTDPFAFSRQ
ALQSTPVGSS SKSSLPVLQV PAPSGFSQHP GLLVPHTHAR DSSQGPCEPL PGPLTQPRAD
ASPFSGVLTP SAPPGPEMNR STEVGPSSEP EVQTPPYLPH YIPGVDPEPS HGGHSHGNMP
GLDRPLSRQN PHDGVVTPAA SPSFPQPRLL MAGQWGPVQG SPQPLGQHRS PCPEGPVPSG
VPCATSVPHF PIPSVLHQGP GHEQHSPLVA PPAALPSDGR DEVGHLQTGS HLANNFDPEN
TFRQNPRIVN HWASPELRQN PGVKKEHQPA SALVNPLAQG DSPEHRTHHP LGAGAGPGCA
PLEADSGASG ALAMFFQGGE TENEENLSSE KAGSSGQADF DDFCSSPGLG HLPAPAHMGA
GSLCQALLPG PGNEATGDVW GDAAGTGLPD ASGSQYENVE NLEFVQNQEV LPSEPLNLDP
SSLSDQFRYG PLPGPAVPRH GAVCHTGAPD TTLHTVHPDS ASSSYNSRSH GRLSGSARPQ
ELVGTFIQQE VGKPEDEASG SFFKQIDSSP VGGETDETTV SQNYRGSVSQ PSTPSPPKPT
GIFQTSANSS FEPVKSHLVG VKPFEADRAN VVGEVRETCA RQKQCRPAAA LPDASPGNLE
QPPDNMETLC APQVCPLPLN STTEAGHVLP HAGAPPLDTV YPAPEKRPSA RAQGPVKCES
PATTLWAQSE LPDFGGNVLL APAAPALYVS AKPQPPEVVQ PPEEAMSGQQ SRKPSSAAPV
QSRDGIGASE NLENPPKMGE EEALQSQASS GYASLLSSPP TESLQNPPVL IAQPDHSYNL
AQPINFPMSL SNSNEKNQSW REALVGDRPA VGSWALGGDS GENSSLSGIP TGSVLSLSLP
SSVAQSNFPQ GSGASEMVSN QPANLLVQPP SQPVPENLVP ESQKDRKAGN ALPGFANSPA
GSTSVVLVPP AHGTLVPDGN KANHSSHQED TYGALDFSLS RTLENPVSMY SPSHSDSLAS
QQTVASHPRQ SGPGAPNLDR FYQQVTKDAQ GQSGLERAQQ ELVPPQQQAS PQVPKATLSE
LSNPESLPAQ GQAQNSAQPP ASLAPADAGQ QLPPRPPQSS SASLVSTGSG QAAVPSEQPW
PQPMPALAPG PPPQDLAAYY YYRPLYDAYQ PQYPSPYPLE PGAASLYYQD VYGLYETRYR
PYDSAASAYA ENYRYPEPER PSSRASHSSE RPPPRQGYPE GYYSSKSGWS SQSDYYASYY
SSQYDYGDPG HWDRYHYSAR VRDPRTYDRR YWCDAEYDTY RREHSTYGDR PEKRDNNWRY
DPRFTGSFDD DPDPHRDPYG EEVDRRSVHS EHSARSLHSA HSLASRRSSL SSHSHQSQIY
RSHNVAASSY EAPLPPGSFH GDFAYGTYRS NFNSGPGFPE YGYPADTVWP AMEQVSSRPT
SPEKFSVPHV CARFGPGGQL IKVIPNLPSE GQPALVEVHS MEALLQHTSE QEEMRAFPGP
LAKDDTHKVD VINFAQNKAI KCLQNENLID KESASLLWNF IVLLCRQNGT VVGTDIAELL
LRDHRTVWLP GKSPNEANLI DFTNEAVEQV EEEESGEAQL SFLTGGPTAA ASSLERETER
FRELLLYGRK KDALESAMKN GLWGHALLLA SKMDSRTHAR VMTRFANSLP INDPLQTVYQ
LMSGRMPAAS TCCGDEKWGD WRPHLAMVLS NLNNNMDVES RTMATMGDTL ASKGLLDAAH
FCYLMAQVGF GVYTKKTTKL VLIGSNHSLP FLKFATNEAI QRTEAYEYAQ SLGAQTCPLP
SFQVFKFIYS CRLAEMGLAT QAFHYCEAIA KSILTQPHLY SPVLISQLVQ MASQLRLFDP
QLKEKPEEES LAAPTWLVHL QQVEQQIKEG AGVWHQDGAF PQQCPSTPSS EVEQDGAGLS
QPAALGIANP LLAVPVPSPE HSSPSVRLLP SALQTLPDGP LASPARVPMF PVPLPPGPLE
PGPGCVTPGS ALGFPEPSRP DPATLCPGPG LPPGVPPLQE RRHLLQEARS PDPGIVPPEA
PVGNSLSELS EENFGGKFAT LAPSRTAPDS EAPPGWDRAD SGPTQPPLSL PPAPETKRAG
QAAKKETKEP KKGESWFSRW LPGKKKTEAY LPDDKNKSIV WDEKKNQWVN LNEPEEEKKA
PPPPPTSLPK AVQAAPPGLA GPAGAPVNMF SRRAAGSRAR YVDVLNPSGT QRNEPALAPA
DFVAPLAPLP IPSNLFVPSP DAEEPQPPDG TGREGPAPAR GLANLEPAPE PTVLSSAASL
PGSELPSSKP EGSQGGELSR CSSMSSLSRE VSQHFNQAPG DLPAAGGPPS GAVPFYNPAQ
LAQACATSGS SRLGRIDQRK HLVQN
//
