SC16B_RABIT
ID SC16B_RABIT Reviewed; 1045 AA.
AC Q6BCB4;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Protein transport protein Sec16B;
DE AltName: Full=Regucalcin gene promoter region-related protein p117;
DE Short=RGPR-p117;
DE AltName: Full=SEC16 homolog B;
GN Name=SEC16B; Synonyms=RGPR;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15583834;
RA Sawada N., Yamaguchi M.;
RT "A novel regucalcin gene promoter region-related protein: comparison of
RT nucleotide and amino acid sequences in vertebrate species.";
RL Int. J. Mol. Med. 15:97-104(2005).
RN [2]
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).
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}.
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DR EMBL; AB185244; BAD30088.1; -; mRNA.
DR RefSeq; NP_001075483.1; NM_001082014.1.
DR AlphaFoldDB; Q6BCB4; -.
DR SMR; Q6BCB4; -.
DR STRING; 9986.ENSOCUP00000004518; -.
DR PRIDE; Q6BCB4; -.
DR GeneID; 100008637; -.
DR KEGG; ocu:100008637; -.
DR CTD; 89866; -.
DR eggNOG; KOG1913; Eukaryota.
DR InParanoid; Q6BCB4; -.
DR OrthoDB; 235062at2759; -.
DR Proteomes; UP000001811; Unplaced.
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: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:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0007031; P:peroxisome organization; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; ER-Golgi transport; Golgi apparatus; Membrane;
KW Peroxisome biogenesis; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..1045
FT /note="Protein transport protein Sec16B"
FT /id="PRO_0000341976"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..711
FT /note="Central conserved domain (CCD); required for
FT localization to endoplasmic reticulum exit sites"
FT /evidence="ECO:0000250|UniProtKB:Q96JE7"
FT REGION 707..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 752..779
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 858..876
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96JE7"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q75N33"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XT4"
FT MOD_RES 852
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q75N33"
FT MOD_RES 858
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XT4"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XT4"
FT MOD_RES 867
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91XT4"
SQ SEQUENCE 1045 AA; 114360 MW; 6148D35BA06D94A1 CRC64;
MEPWVPQWPP PSRGRPRSPV PDSERGLQRD GYHRPAPHSW HNGERLPQWQ DVQGSPQPQQ
DPRAGPQRPQ HVPRLGAWQQ HAPAVDYYEG GHRGQLYSRP SYESLYPALT EDYAYGSHYY
HGHPQWQQEG RVPRQGSPYV WHDSYRDQRH LSEHRPENQS RTFRRDSETQ FQRSNRRNPH
KDGPASSSGQ ERPGELFAEG RLSWGLTSQP SLGSKSNLLQ QREVGLSSSS YELSQYMVDA
PELYDPAAAA GWRPVPAEDI PVAGPKAPKK FYIPHVSVGF GPRGQLVCVS PSSPMDGQTA
LVEVHSMEVI LNDLEEQEEM RSFPGPLIRE DVHKVDVMTF CQQKAAQSRK SGTPGGRDSA
LLWQLLVLLC RQNGSMAGSD IAELLLQDCK KLEKYKKQPP VANLINLADE DWPVLSSGPR
NLLTGETPPS VETPAQVVGK FTQLLYYGRK KEALEWAMKN HLWGHALFLS SKMEPRTYKW
VMSGFTSTLA LNDPLQTLFQ LLSGRIPQAA TCCGDTQWGD WRPHLAVILS NQAGDPELRR
RVIVSMGDTL ASKGLVEAAH FCYLMAQVPF GHYTVNADRL ALLGSSHSQE FPRFASAEAI
QRTEVLEYCR TLGGRPGLIA SFQVYKLLYA SRLADYGLAS QAFHYCEAIG TAVLSQAESS
HPVLLVELIK LAERLKLADP LVLERRGGDE AWEPDWLQRL RRHQELQQKA AADAGEPHSA
NLDTPGATGT TESTFYQDLP AYQRFSDAPG CEPAPWPTPT QTGCPSPFPS QPGPAAGPAG
APVPLYSVPE THFPVSTEEP QAVGGQVWED TRQTHSAPGE NIASPETFQE PEGLEVISTP
QELLAPRAQS FSESCPGSVK EADEESSDEA GRKSARSPAH TGKLADATAS AKRSGFGWFS
WFRSKPTENA PHSGDEDSSD SPDSEQENPR APSPREAGLG LSPPPLLESP PLPGASAFGG
GTGRGEAQGA MSSQETAAGT GTGGLSGPES ASSELYSNPS VLLPPPSVKG AVPLYNPSQV
PQLPTAAGLS RPNRLAQRRY PTQPC
