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| <StructureSection load='4gky' size='350' side='right' caption='Human ERGIC-53 carbohydrate recognition domain complex with mannose (stick model), glycerol and Ca+2 ion (green) (PDB code [[4gky]])' scene='74/748868/Cv/1'> | | <StructureSection load='' size='350' side='right' caption='Human ERGIC-53 carbohydrate recognition domain complex with mannose (stick model), glycerol and Ca+2 ion (green) (PDB code [[4gky]])' scene='74/748868/Cv/1'> |
| == Function == | | == Function == |
| '''ER-Golgi Intermediate Compartment-53 (ERGIC-53)''' is a transmembrane protein which acts as a receptor of glycoproteins and transports them from the ER to ER-Golgi Intermediate Compartment and Golgi<ref>PMID:19609866</ref>. | | '''ER-Golgi Intermediate Compartment-53 (ERGIC-53)''' is a transmembrane protein which acts as a receptor of glycoproteins and transports them from the ER to ER-Golgi Intermediate Compartment and Golgi<ref>PMID:19609866</ref>. |
Revision as of 10:36, 20 October 2017
| Function
ER-Golgi Intermediate Compartment-53 (ERGIC-53) is a transmembrane protein which acts as a receptor of glycoproteins and transports them from the ER to ER-Golgi Intermediate Compartment and Golgi[1].
Relevance
Some ER storage diseases have relationship with ERGIC-53. ERGIC-53 is required for the propagation of arenavirus, coronavirus and filovirus[2].
Structural highlights
ERGIC-53 contains an N-terminal signal sequence, a calcium-dependent and pH-sensitive carbohydrate recognition domain (CRD), a stalk region, a transmembrane domain and a short cytoplasmic domain. The mannose-binding pocket of ERGIC-53 contains a Ca+2 ion as well[3].
- ↑ Zhang YC, Zhou Y, Yang CZ, Xiong DS. A review of ERGIC-53: its structure, functions, regulation and relations with diseases. Histol Histopathol. 2009 Sep;24(9):1193-204. PMID:19609866
- ↑ Klaus JP, Eisenhauer P, Russo J, Mason AB, Do D, King B, Taatjes D, Cornillez-Ty C, Boyson JE, Thali M, Zheng C, Liao L, Yates JR 3rd, Zhang B, Ballif BA, Botten JW. The intracellular cargo receptor ERGIC-53 is required for the production of infectious arenavirus, coronavirus, and filovirus particles. Cell Host Microbe. 2013 Nov 13;14(5):522-34. doi: 10.1016/j.chom.2013.10.010. PMID:24237698 doi:https://dx.doi.org/10.1016/j.chom.2013.10.010
- ↑ Zheng C, Page RC, Das V, Nix JC, Wigren E, Misra S, Zhang B. Structural characterization of carbohydrate binding by LMAN1 provides new insight into the endoplasmic reticulum export of FV and FVIII. J Biol Chem. 2013 May 24. PMID:23709226 doi:10.1074/jbc.M113.461434
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3D structures of ERGIC-53
Updated on 20-October-2017
4ygb, 4ygc, 4ygd, 4yge, 3wht, 3lcp, 3a4u – hERGIC-53 CRD domain + MCFD2 + Ca - human
3whu, 3wnx – hERGIC-53 CRD domain + MCFD2 + Ca + mannose
4gkx – hERGIC-53 CRD domain + Ca
4gky – hERGIC-53 CRD domain + Ca + mannose
1r1z – rERGIC-53 CRD domain + Ca - rat
1gv9 – rERGIC-53 CRD domain
References
