CAPZA2: Difference between revisions
Content deleted Content added
| Line 3: | Line 3: | ||
== Structure == |
== Structure == |
||
CapZ-alpha2 is a 33.0 kDa [[protein]] comprised of 286 [[amino acid]]s.<ref>{{cite web|title=Protein sequence of human CAPZA2 (Uniprot ID: P47755)|url=http://www.heartproteome.org/copa/ProteinInfo.aspx?QType=Protein%20ID&QValue=P47755|website=Cardiac Organellar Protein Atlas Knowledgebase (COPaKB)|accessdate=18 September 2015}}</ref> ''CAPZA2'' is located on human chromosome 7, position q31.2-q31.3.<ref>{{cite journal|last1=Barron-Casella|first1=EA|last2=Torres|first2=MA|last3=Scherer|first3=SW|last4=Heng|first4=HH|last5=Tsui|first5=LC|last6=Casella|first6=JF|title=Sequence analysis and chromosomal localization of human Cap Z. Conserved residues within the actin-binding domain may link Cap Z to gelsolin/severin and profilin protein families.|journal=The Journal of biological chemistry|date=15 September 1995|volume=270|issue=37|pages=21472-9|pmid=7665558}}</ref> The primary sequence of CapZ-alpha2 contains three [[C-terminus|C-terminal]], regularly spaced [[leucine]]s at positions 258, 262 and 266 found in consensus sequence of KxxxLxxE/DLxxALxxK/R that are critical for [[actin]] binding; these residues are conserved within the [[CAPZB|CapZ-beta isoform]].<ref>{{cite journal|last1=Barron-Casella|first1=EA|last2=Torres|first2=MA|last3=Scherer|first3=SW|last4=Heng|first4=HH|last5=Tsui|first5=LC|last6=Casella|first6=JF|title=Sequence analysis and chromosomal localization of human Cap Z. Conserved residues within the actin-binding domain may link Cap Z to gelsolin/severin and profilin protein families.|journal=The Journal of biological chemistry|date=15 September 1995|volume=270|issue=37|pages=21472-9|pmid=7665558}}</ref> CapZ-alpha2 is 85% identical to [[CAPZA1|CapZ-alpha1]], and differ by a small number of key [[amino acid]]s; 21 [[amino acid]] differences perpetrate [[isoform]] specificity.<ref>{{cite journal|last1=Hart|first1=MC|last2=Korshunova|first2=YO|last3=Cooper|first3=JA|title=Vertebrates have conserved capping protein alpha isoforms with specific expression patterns.|journal=Cell motility and the cytoskeleton|date=1997|volume=38|issue=2|pages=120-32|pmid=9331217}}</ref> CapZ-alpha2 is expressed in a variety of tissues, |
CapZ-alpha2 is a 33.0 kDa [[protein]] comprised of 286 [[amino acid]]s.<ref>{{cite web|title=Protein sequence of human CAPZA2 (Uniprot ID: P47755)|url=http://www.heartproteome.org/copa/ProteinInfo.aspx?QType=Protein%20ID&QValue=P47755|website=Cardiac Organellar Protein Atlas Knowledgebase (COPaKB)|accessdate=18 September 2015}}</ref> ''CAPZA2'' is located on human chromosome 7, position q31.2-q31.3.<ref>{{cite journal|last1=Barron-Casella|first1=EA|last2=Torres|first2=MA|last3=Scherer|first3=SW|last4=Heng|first4=HH|last5=Tsui|first5=LC|last6=Casella|first6=JF|title=Sequence analysis and chromosomal localization of human Cap Z. Conserved residues within the actin-binding domain may link Cap Z to gelsolin/severin and profilin protein families.|journal=The Journal of biological chemistry|date=15 September 1995|volume=270|issue=37|pages=21472-9|pmid=7665558}}</ref> The primary sequence of CapZ-alpha2 contains three [[C-terminus|C-terminal]], regularly spaced [[leucine]]s at positions 258, 262 and 266 found in consensus sequence of KxxxLxxE/DLxxALxxK/R that are critical for [[actin]] binding; these residues are conserved within the [[CAPZB|CapZ-beta isoform]].<ref>{{cite journal|last1=Barron-Casella|first1=EA|last2=Torres|first2=MA|last3=Scherer|first3=SW|last4=Heng|first4=HH|last5=Tsui|first5=LC|last6=Casella|first6=JF|title=Sequence analysis and chromosomal localization of human Cap Z. Conserved residues within the actin-binding domain may link Cap Z to gelsolin/severin and profilin protein families.|journal=The Journal of biological chemistry|date=15 September 1995|volume=270|issue=37|pages=21472-9|pmid=7665558}}</ref> CapZ-alpha2 is 85% identical to [[CAPZA1|CapZ-alpha1]], and differ by a small number of key [[amino acid]]s; 21 [[amino acid]] differences perpetrate [[isoform]] specificity.<ref>{{cite journal|last1=Hart|first1=MC|last2=Korshunova|first2=YO|last3=Cooper|first3=JA|title=Vertebrates have conserved capping protein alpha isoforms with specific expression patterns.|journal=Cell motility and the cytoskeleton|date=1997|volume=38|issue=2|pages=120-32|pmid=9331217}}</ref> CapZ-alpha2 is expressed in a variety of tissues, including [[cardiac muscle]], where it caps [[sarcomere|sarcomeric]] [[actin]] at [[Z-disc]]s; the ratio of CapZ-alpha2 to [[CAPZA1|CapZ-alpha1]] varies significantly among different tissues.<ref>{{cite journal|last1=Hart|first1=MC|last2=Korshunova|first2=YO|last3=Cooper|first3=JA|title=Vertebrates have conserved capping protein alpha isoforms with specific expression patterns.|journal=Cell motility and the cytoskeleton|date=1997|volume=38|issue=2|pages=120-32|pmid=9331217}}</ref> |
||
== Function == |
== Function == |
||
Revision as of 15:00, 18 September 2015
Template:PBB F-actin-capping protein subunit alpha-2 also known as CapZ-alpha2 is a protein that in humans is encoded by the CAPZA2 gene.[1]
Structure
CapZ-alpha2 is a 33.0 kDa protein comprised of 286 amino acids.[2] CAPZA2 is located on human chromosome 7, position q31.2-q31.3.[3] The primary sequence of CapZ-alpha2 contains three C-terminal, regularly spaced leucines at positions 258, 262 and 266 found in consensus sequence of KxxxLxxE/DLxxALxxK/R that are critical for actin binding; these residues are conserved within the CapZ-beta isoform.[4] CapZ-alpha2 is 85% identical to CapZ-alpha1, and differ by a small number of key amino acids; 21 amino acid differences perpetrate isoform specificity.[5] CapZ-alpha2 is expressed in a variety of tissues, including cardiac muscle, where it caps sarcomeric actin at Z-discs; the ratio of CapZ-alpha2 to CapZ-alpha1 varies significantly among different tissues.[6]
Function
Clinical Significance
References
- ^ "Entrez Gene: CAPZA2 capping protein (actin filament) muscle Z-line, alpha 2".
- ^ "Protein sequence of human CAPZA2 (Uniprot ID: P47755)". Cardiac Organellar Protein Atlas Knowledgebase (COPaKB). Retrieved 18 September 2015.
- ^ Barron-Casella, EA; Torres, MA; Scherer, SW; Heng, HH; Tsui, LC; Casella, JF (15 September 1995). "Sequence analysis and chromosomal localization of human Cap Z. Conserved residues within the actin-binding domain may link Cap Z to gelsolin/severin and profilin protein families". The Journal of biological chemistry. 270 (37): 21472–9. PMID 7665558.
- ^ Barron-Casella, EA; Torres, MA; Scherer, SW; Heng, HH; Tsui, LC; Casella, JF (15 September 1995). "Sequence analysis and chromosomal localization of human Cap Z. Conserved residues within the actin-binding domain may link Cap Z to gelsolin/severin and profilin protein families". The Journal of biological chemistry. 270 (37): 21472–9. PMID 7665558.
- ^ Hart, MC; Korshunova, YO; Cooper, JA (1997). "Vertebrates have conserved capping protein alpha isoforms with specific expression patterns". Cell motility and the cytoskeleton. 38 (2): 120–32. PMID 9331217.
- ^ Hart, MC; Korshunova, YO; Cooper, JA (1997). "Vertebrates have conserved capping protein alpha isoforms with specific expression patterns". Cell motility and the cytoskeleton. 38 (2): 120–32. PMID 9331217.