Primary Information |
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BoMiProt ID | Bomi8437 |
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Protein Name | Protein transport protein Sec16B/Regucalcin gene promoter region-related protein p117/RGPR-p117/SEC16 homolog B |
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Organism | Bos taurus |
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Uniprot ID | Q75NY9 |
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Milk Fraction | Whey |
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Ref Sequence ID | NP_996854.2 |
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Aminoacid Length | 1052 |
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Molecular Weight | 117174 |
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FASTA Sequence |
Download |
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Gene Name | SEC16B |
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Gene ID | 404548 |
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Protein Existence Status | reviewed |
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Secondary Information |
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Protein Function | plays a key role in the formation of coat protein II vesicles, which mediate protein transport from the endoplasmic reticulum (ER) to the Golgi apparatus. |
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Biochemical Properties | The C-terminal region of Sec16B is rich in Gly (12.6%) and Ser (13.5%), and it is not conserved in Sec16A. This unique amino acid composition of the C-terminal region may allow Sec16B to localize to special ER domains, where it modulates the export of Pex16 and Pex3 from the ER.Deletion of the C-terminal 348 amino acids of Sec16B abrogated the ability to rescue the Sec16B depletion phenotype, suggesting the importance of the C-terminal region in peroxisome biogenesis. |
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PTMs | Phosphorylation |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q75NY9|SC16B_BOVIN Protein transport protein Sec16B OS=Bos taurus OX=9913 GN=SEC16B PE=2 SV=1
MEPWIPQWLPQPSGRPPAPSKDPDRGLWKDRYYQPIPHSWHNGERVHQRQDVGRS*55PQPQQ
DPREDLQEPHYAARS*75GEWRPPVSGVDYYEGGYPSQLYSRWSIEDLYQSYYSPALREEYAY
GSYYYHGHPQQLQEERVPRQGS*142PYIWQEDHRDQKYLNDHQHENQNS*166PFGTNRETQLQSKS
RNPYKDS*187PAS*190NSGQERPEDLFMESPLTGAQKNKLSLMEESNLLWQHESGLTSSSYELSQY
MADASELCDPMTS*253AVWS*257PVQAEDISAAGPKEPMKFYVPHMPVSFGPGGQLVCVSPSSPSD
GQTALVELHSMEVILNDSEEQEEMRTFSGPLIREDVHKVDIMTFCQQKAAQSHKSETPGS
RDSALLWQLLVLLCRQNGSMVGSDIAELLMQDWKKLEKYKRQPPVANLINLTDEDWPVLS
SGTRDLLTGEILPSVETPAQILEKFTKLLYYGRKKEALEWAMKNHLWGHALFLASKMDPR
THSRVMSGFTSTLALNDPLQTLFQLMSGRIPQAATCCGDKQWGDWRPHLAVILSNQGGDP
ELYQRTIVAMGDTLAGKGLVEAAHFCYLMAHVPFGYYTVKTDYLALLGSSHSQEFLKSAT
TEAIQRTEIFEYCQMLGRPKSFIPSFQVYKLLYASRLADYGLTSQALHYCEPVGTALLSH
GESSHPVLLVELIKLAERLKLSDPLVLERRRHRGDRDLEPDWCVHLRGHHRELQQKEAGD
IGRPQSAQAVISEARKTPENTFYQDLSGPQGNSEAYGDRSALWPTLEQSGPAQLSPQQPR
SYPTGGGSGQMGVPVPLYSVPETHLLGTSGSMAVTGAPGGTAWEEAQQIHLPPVSPETLQ
HPDGQKAISRPQVPLIPRARSIS*863ESS*866IVS*869VKEDEEEPPRRQIKIFLKYRPERKPEREGDT
KSSGFGWFSWFRSKPTHNASPSGEEDSSDSPDSEEMPRAASLPQPSPSLSLTPSPDPQSL
LGASAFSRDTGGDEVRGSVSGVGTAEGPGSGGLSGPEGVSTELCLNAGVLLPPPSVKGSV
PLYNPSQVPQLSTVTSLNRPNRLAQRRYPTQS
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Predicted Disorder Regions | 188-235, 718-867, 887-1030 |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Significance of PTMs | In Drosophila, Sec16 is shown to be phosphorylated in the C-terminal region in response to nutrient starvation.N-terminal 565 residues includes the 30 phosphorylation sites.Sec16 phosphorylation is dispensable for its function in ER export.Two distinct phosphorylation sites, Thr-415 and Ser-846, were identified in the N-terminal region of mammalian Sec16 homologue Sec16A. |
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Additional Comments | Sec16 was first characterized in yeast S. cerevisiae as a 240-kDa peripheral membrane protein that interacts with coat protein II (COPII) coat components and facilitates their assembly and vesicle budding |
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Bibliography | 1.Yonekawa S, Furuno A, Baba T, Fujiki Y, Ogasawara Y, Yamamoto A, Tagaya M, Tani K. Sec16B is involved in the endoplasmic reticulum export of the peroxisomal membrane biogenesis factor peroxin 16 (Pex16) in mammalian cells. Proc Natl Acad Sci U S A. 2011 Aug 2;108(31):12746-51. doi: 10.1073/pnas.1103283108. Epub 2011 Jul 18. PMID: 21768384; PMCID: PMC3150892. 2.Yorimitsu T, Sato K. Sec16 function in ER export and autophagy is independent of its phosphorylation in Saccharomyces cerevisiae. Mol Biol Cell. 2020 Feb 1;31(3):149-156. doi: 10.1091/mbc.E19-08-0477. Epub 2019 Dec 18. PMID: 31851588; PMCID: PMC7001475. |