SC16B_RAT
ID SC16B_RAT Reviewed; 1057 AA.
AC Q75N33; Q925T1;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Protein transport protein Sec16B;
DE AltName: Full=Leucine zipper transcription regulator 2;
DE AltName: Full=Regucalcin gene promoter region-related protein p117;
DE Short=RGPR-p117;
DE AltName: Full=SEC16 homolog B;
GN Name=Sec16b; Synonyms=Lztr2, Rgpr;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11605020; DOI=10.3892/ijmm.8.5.513;
RA Misawa H., Yamaguchi M.;
RT "Molecular cloning and sequencing of the cDNA coding for a novel regucalcin
RT gene promoter region-related protein in rat, mouse and human liver.";
RL Int. J. Mol. Med. 8:513-520(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Yamaguchi M., Sawada N., Murata T.;
RT "Rat regucalcin gene promoter region-related protein.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=12244571; DOI=10.1002/jcb.10289;
RA Misawa H., Yamaguchi M.;
RT "Gene expression for a novel protein RGPR-p117 in various species: the
RT stimulation by intracellular signaling factors.";
RL J. Cell. Biochem. 87:188-193(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-866; SER-869 AND
RP SER-872, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Involved in peroxisome biogenesis.
CC Regulates the transport of peroxisomal biogenesis factors PEX3 and
CC PEX16 from the ER to peroxisomes. {ECO:0000250|UniProtKB:Q96JE7}.
CC -!- SUBUNIT: SEC16A and SEC16B are each present in multiple copies in a
CC heteromeric complex. Interacts with TFG. Interacts with SEC13.
CC {ECO:0000250|UniProtKB:Q96JE7}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q96JE7}; Peripheral membrane protein
CC {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}. Note=Localizes to endoplasmic reticulum
CC exit sites (ERES), also known as transitional endoplasmic reticulum
CC (tER). {ECO:0000250|UniProtKB:Q96JE7}.
CC -!- TISSUE SPECIFICITY: Liver, kidney, heart, spleen and brain.
CC {ECO:0000269|PubMed:11605020, ECO:0000269|PubMed:12244571}.
CC -!- INDUCTION: Stimulated by intracellular signaling factors.
CC {ECO:0000269|PubMed:12244571}.
CC -!- SIMILARITY: Belongs to the SEC16 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB43905.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB060653; BAB43905.1; ALT_FRAME; mRNA.
DR EMBL; AB178524; BAD18068.1; -; Genomic_DNA.
DR RefSeq; NP_446023.1; NM_053571.1.
DR RefSeq; XP_008767904.1; XM_008769682.2.
DR RefSeq; XP_008767907.1; XM_008769685.2.
DR RefSeq; XP_017454437.1; XM_017598948.1.
DR RefSeq; XP_017454438.1; XM_017598949.1.
DR RefSeq; XP_017454439.1; XM_017598950.1.
DR RefSeq; XP_017454440.1; XM_017598951.1.
DR AlphaFoldDB; Q75N33; -.
DR SMR; Q75N33; -.
DR STRING; 10116.ENSRNOP00000046286; -.
DR iPTMnet; Q75N33; -.
DR PhosphoSitePlus; Q75N33; -.
DR PaxDb; Q75N33; -.
DR Ensembl; ENSRNOT00000044008; ENSRNOP00000046286; ENSRNOG00000005229.
DR GeneID; 89868; -.
DR KEGG; rno:89868; -.
DR UCSC; RGD:621658; rat.
DR CTD; 89866; -.
DR RGD; 621658; Sec16b.
DR eggNOG; KOG1913; Eukaryota.
DR GeneTree; ENSGT00940000160138; -.
DR HOGENOM; CLU_010575_0_0_1; -.
DR InParanoid; Q75N33; -.
DR OMA; HPRDEGH; -.
DR OrthoDB; 235062at2759; -.
DR PhylomeDB; Q75N33; -.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR PRO; PR:Q75N33; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000005229; Expressed in liver and 19 other tissues.
DR Genevisible; Q75N33; RN.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IBA:GO_Central.
DR GO; GO:0016559; P:peroxisome fission; ISO:RGD.
DR GO; GO:0007031; P:peroxisome organization; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; ISO:RGD.
DR GO; GO:0070973; P:protein localization to endoplasmic reticulum exit site; IBA:GO_Central.
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; 1.
DR Pfam; PF12932; Sec16; 1.
DR Pfam; PF12931; Sec16_C; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW Peroxisome biogenesis; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..1057
FT /note="Protein transport protein Sec16B"
FT /id="PRO_0000341977"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..708
FT /note="Central conserved domain (CCD); required for
FT localization to endoplasmic reticulum exit sites"
FT /evidence="ECO:0000250|UniProtKB:Q96JE7"
FT REGION 704..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 849..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..903
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..930
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..989
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XT4"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JE7"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XT4"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JE7"
FT MOD_RES 856
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96JE7"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 872
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XT4"
FT CONFLICT 15
FT /note="P -> L (in Ref. 1; BAB43905)"
FT /evidence="ECO:0000305"
FT CONFLICT 47
FT /note="T -> A (in Ref. 1; BAB43905)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="Q -> R (in Ref. 1; BAB43905)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="L -> P (in Ref. 1; BAB43905)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="N -> K (in Ref. 1; BAB43905)"
FT /evidence="ECO:0000305"
FT CONFLICT 726
FT /note="G -> R (in Ref. 1; BAB43905)"
FT /evidence="ECO:0000305"
FT CONFLICT 880
FT /note="T -> S (in Ref. 1; BAB43905)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1057 AA; 116897 MW; 30D505492331872E CRC64;
MELWVPQTQG RTTGPSRDAN RRLQSGHYRP RPHPQYSGDN YHQWQDTHKN SKPQQDPRDD
HQQPHYVPRS GEWSQPVSGA DYLKGSYPSH PYSRSGYEDP YQSYHTPTPR DEYAYGNYYY
HGHPQLPQGE RVARQGSPYI WHEDHRDQRH FSEHHWEKHN STFEANSDTQ FQFTSKNPYN
DNPASAFGLE QPGEFFPESG AQKQKPSLTS KSNLLQQHES GLSSSSYELS QYMTEAPEQY
EPMVSATWRP IQADDTSATV PKAPMRFYVP HVSVSFGPGG QLICVSPNSP ADGQTALVEV
HSMEVILNDF EDQEEMRAFP GPLIREDIHK VDIMTFCQKK AAQCLKSETP GSRDSALLWQ
LLVLLCRQNG SMVGSDIAEL LMQDCKKLEK YKRQPPVANL INLTDEDWPV LSSGTRNLLT
GEIPLNVDTP AQIVEKFTNL LYYGRKKEAL EWAMKNHLWG HALFLASKMD PRTYNWVMSG
FTTTLALNDP LQTLFQLMSG RIPQAATCCG DKQWGDWRPH LAVILSNQAG DAELYQRAIV
SMGDTLAGKG LVEASHFCYL MAHVPFGHYT VKTDHLALVG SNHSQEFLKF ATIEAIQRTE
IFEYCQMLGR PKSFIPSFQV YKLLYASRLA DYGLASQALH YCEAIGAAVL SEGGSSHPVL
LAELIKLAEK LKLSDPLVLE SRRGDRVLEP DWLVQLRRKH KELEQTRTGD LRDPDLTPSD
IYGARGTTDT PYRDLYGQQN YSEDSEYSSA LWPTSEQTSL TNPTPQQPFP LQRDTYSERD
GPVHMGTPVP LYSVPATHLT VISGSSSGSG VAVTGAPGGR VGEEMLQKHP ALGENTVPQE
AVQDPDGLAV ISSPQTPLAP RDRSFSEDSA ISAKEDEEGT SDGADKPPHP DASQKEKLRD
GKNTKSSGFG WFSWFRSKPA SSVSTSGDED SVDSSDSEES PRASPPHHAS LGLSPTPPLS
SPSLPGASTF PRGTGGNSLQ GSSNSSGMAE GVGIGGFSGP QGVSSEFYSQ PGALPPPPTL
QGAVPLYNPS QVPQLPTASS LNRPNRLAQR RYPSQPC
