SC16B_MOUSE
ID SC16B_MOUSE Reviewed; 1051 AA.
AC Q91XT4; E9QL61; Q69Z64; Q6PCR8;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 113.
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=Kiaa1928, Lztr2, Rgpr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
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 [LARGE SCALE MRNA].
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP TISSUE SPECIFICITY.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-182; SER-863;
RP SER-866; SER-874 AND SER-875, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-185, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. {ECO:0000269|PubMed:12244571}.
CC -!- SIMILARITY: Belongs to the SEC16 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32580.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB063356; BAB61034.1; -; mRNA.
DR EMBL; AK173302; BAD32580.1; ALT_INIT; mRNA.
DR EMBL; AC161108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC059194; AAH59194.1; -; mRNA.
DR CCDS; CCDS15400.1; -.
DR RefSeq; NP_001153458.1; NM_001159986.1.
DR RefSeq; NP_203505.3; NM_033354.3.
DR RefSeq; XP_017168472.1; XM_017312983.1.
DR RefSeq; XP_017168473.1; XM_017312984.1.
DR AlphaFoldDB; Q91XT4; -.
DR SMR; Q91XT4; -.
DR STRING; 10090.ENSMUSP00000083300; -.
DR iPTMnet; Q91XT4; -.
DR PhosphoSitePlus; Q91XT4; -.
DR jPOST; Q91XT4; -.
DR MaxQB; Q91XT4; -.
DR PaxDb; Q91XT4; -.
DR PeptideAtlas; Q91XT4; -.
DR PRIDE; Q91XT4; -.
DR ProteomicsDB; 255464; -.
DR Antibodypedia; 35113; 126 antibodies from 28 providers.
DR DNASU; 89867; -.
DR Ensembl; ENSMUST00000027881; ENSMUSP00000027881; ENSMUSG00000026589.
DR Ensembl; ENSMUST00000086130; ENSMUSP00000083300; ENSMUSG00000026589.
DR Ensembl; ENSMUST00000111700; ENSMUSP00000107329; ENSMUSG00000026589.
DR GeneID; 89867; -.
DR KEGG; mmu:89867; -.
DR UCSC; uc007ddl.2; mouse.
DR CTD; 89866; -.
DR MGI; MGI:2148802; Sec16b.
DR VEuPathDB; HostDB:ENSMUSG00000026589; -.
DR eggNOG; KOG1913; Eukaryota.
DR GeneTree; ENSGT00940000160138; -.
DR HOGENOM; CLU_010575_0_0_1; -.
DR InParanoid; Q91XT4; -.
DR OMA; HPRDEGH; -.
DR OrthoDB; 235062at2759; -.
DR PhylomeDB; Q91XT4; -.
DR TreeFam; TF316276; -.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR BioGRID-ORCS; 89867; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q91XT4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q91XT4; protein.
DR Bgee; ENSMUSG00000026589; Expressed in mesenchyme of lower jaw and 138 other tissues.
DR ExpressionAtlas; Q91XT4; baseline and differential.
DR Genevisible; Q91XT4; MM.
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:MGI.
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: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; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IEA:Ensembl.
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..1051
FT /note="Protein transport protein Sec16B"
FT /id="PRO_0000341975"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..203
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 703..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 850..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..892
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..983
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1051
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 70
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q75N33"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JE7"
FT MOD_RES 850
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96JE7"
FT MOD_RES 860
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q75N33"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 874
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 875
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT CONFLICT 7
FT /note="Q -> H (in Ref. 4; AAH59194)"
FT /evidence="ECO:0000305"
FT CONFLICT 32
FT /note="L -> P (in Ref. 1; BAB61034 and 4; AAH59194)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="D -> G (in Ref. 1; BAB61034)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="S -> R (in Ref. 1; BAB61034)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="P -> S (in Ref. 1; BAB61034)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="P -> A (in Ref. 1; BAB61034)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="H -> P (in Ref. 1; BAB61034)"
FT /evidence="ECO:0000305"
FT CONFLICT 711
FT /note="P -> L (in Ref. 1; BAB61034 and 4; AAH59194)"
FT /evidence="ECO:0000305"
FT CONFLICT 939
FT /note="S -> P (in Ref. 1; BAB61034 and 4; AAH59194)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1051 AA; 115513 MW; CA802D45E2E39748 CRC64;
MEPWVPQTQG RTTGPSRDTN RGLQSGHYRP RLHSQYSGDK YHQWQDAHKN SKSQQDLRDD
HQQSHSVSRS GEWSQPVSGA DYLKGSYPSH LYSRSGYGDP YQRYHTPTPR DEYAYGNYYY
HGHPQLLPEE RVARQGSPYI WHEDHGDQRY FGEHHREKHN GTFGANSDTQ FQFTSKNPYR
DSPASVSGQE QPGEFFPESE AQKQKPLLTS KSSLLQQHES GLSSSSYELS QYMTAAPEEY
EPMVSAAWRP IQADDTSATV PKAPMRFYVP HVSVSFGPGG QLVCVPPNSP ADGQTALVEV
HSMEVLLNDF EDQEEMRAFP GPLIREDIHK VDIMTFCQQK ATQCLKSETP GSRDSALLWQ
LLVLLCRQNG SMVGSDIAEL LMQDCKKLEK YKRQPPVANL INLTDEDWPV LSSGTRDLLT
GEIPPNVDTP AQIVEKFTKL LYYGRKKEAL EWAMKNHLWG HALFLASKMD PRTYNWVMSG
FTSTLALNDP LQTLFQLMSG RIPQAATVCG DKQWGDWRPH LAVILSNQAG DTELYQRAIV
SMGDTLAGKG LVEASHFCYL MAHVPFGHYT VKTDHLALVG SSHSQEFMKF ATIEAIQRTE
IFEYCQMLGR PKSFIPSFQV YKLLYASRLA DYGLASQALH YCEAIGAAVL SQEGSSHPVL
LAELIKLAEK LKLSDPLVLE RRRGDRDLEP DWLVQLRRKH KDLEQNRTGA PRDPDSTPSD
IYGAGGTTDT PYPDLSGHQN YSEDSEYSST LWSTAEQTSL TNPLAQQSFP LQRDTYSGHM
GTPVPLYSVP ATHLAVTSGA SGSSVAVTGT PGGRVGEDML RTHPAFGENT MTQEPLEDPD
GLEVISSLQT PAAPRVPSFS EDSAASAKED EEGSSDGADK PSHPDASQKG KLGDGKNTKS
SGFGWFSWFR SKPASSVSTS GDEDSSDSSD SEESPRASSP HHASPGLSPT PPLTSPSLPG
ASTFSRGTGG SILQGSSNSS GIAEGMGIGG FSGTQGVSSE FYSQPGALPP PPTLQGAVPL
YNPSQVPQLP TASSLNRPNR LAQRRYPTQP C
