|Official Full Name||crystallin, alpha A|
|Background||Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Defects in this gene cause autosomal dominant congenital cataract (ADCC).|
|Synonyms||CRYAA; crystallin, alpha A; CRYA1; alpha-crystallin A chain; HSPB4; Heat shock protein beta 4; short form; Acry 1; Acry-1; Alpha crystallin A chain; CRYA 1; CRYAA_HUMAN; Crystallin Alpha 1; Crystallin alpha A; Heat shock protein beta-4; HSPB 4; Zonular Central Nuclear Cataract; OTTHUMP00000109430; crystallin, alpha-1; human alphaA-crystallin (CRYA1)|
|Species||Cat.#||Product name||Source (Host)||Tag||Protein Length||Price|
CRYAA involved in several pathways and played different roles in them. We selected most pathways CRYAA participated on our site, such as content, which may be useful for your reference. Also, other proteins which involved in the same pathway with CRYAA were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
|Pathway Name||Pathway Related Protein|
|Protein processing in endoplasmic reticulum||PKZ; MAN1A1; CALR; CAPN2; ERP29; HYOU1; PDIA3; UBE2D1; MAPK10; CANX|
CRYAA has several biochemical functions, for example, Content. Some of the functions are cooperated with other proteins, some of the functions could acted by CRYAA itself. We selected most functions CRYAA had, and list some proteins which have the same functions with CRYAA. You can find most of the proteins on our site.
|identical protein binding||GBP1; SRI; GRASP; CXADR; MMP9; HTT; CASP6; TOPBP1; CBS; NDE1|
|metal ion binding||TDO2; ZCCHC16; TRIM50; TRMT1L; SMAD7; RXFP1; Acsm2a; PFKP; TIMP1; ZDHHC16B|
|protein binding||PPIL1; TBX6; CD40; APLF; TRAPPC2L; RAB11A; SDCBP2; CDH23; VDAC1; SETDB2|
|structural constituent of eye lens||LIM2.5; CRYABB; BFSP1; CRYGA; LIM2.2; CRYABA; ASL1; MIP; CRYBA4; CPOX|
|unfolded protein binding||PFDN1; ERLEC1; NAP1L4; TCP1; PPIB; HSP90B1; SRSF10; DNAJA4; DNAJA1; SCG5|
CRYAA has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with CRYAA here. Most of them are supplied by our site. Hope this information will be useful for your research of CRYAA.
CRYAB; CRYGC; CRYBB2