HMM Summary Page: TIGR01522

Functioncalcium-transporting P-type ATPase, PMR1-type
Trusted Cutoff798.30
Domain Trusted Cutoff798.30
Noise Cutoff792.15
Domain Noise Cutoff792.15
Isology Typeequivalog
EC Number3.6.3.8
HMM Length854
AuthorSelengut J
Entry DateMay 23 2002 11:25AM
Last ModifiedFeb 14 2011 3:27PM
CommentThis model describes the P-type ATPase responsible for translocating calcium ions across the golgi membrane of fungi and animals [1,2], and is of particular importance in the sarcoplasmic reticulum of skeletal and cardiac muscle in vertebrates [2]. The calcium P-type ATPases have been characterized as Type IIA based on a phylogenetic analysis which distinguishes this group from the Type IIB PMCA calcium pump [3] modelled by TIGR01517. A separate analysis divides Type IIA into sub-types, SERCA and PMR1 [2] the former of which is modelled by TIGR01116.
ReferencesRN [1] RM PMID: 2526682 RT The yeast secretory pathway is perturbed by mutations in PMR1, a member of a Ca2+ ATPase family. RA Rudolph HK, Antebi A, Fink GR, Buckley CM, Dorman TE, LeVitre J, Davidow LS, Mao JI, Moir DT. RL Cell. 1989 Jul 14;58(1):133-45. RN [2] RM PMID: 10433975 RT Two additional type IIA Ca(2+)-ATPases are expressed in Arabidopsis thaliana: evidence that type IIA sub-groups exist. RA Pittman JK, Mills RF, O'Connor CD, Williams LE. RL Gene 1999 Aug 5;236(1):137-47 RN [3] RM PMID:9419228 RT Evolution of Substrate Specificities in the P-type ATPase Superfamily. RA Axelsen KB, Palmgren, MG. RL J Mol Evol. 1998 Jan; 46(1): 84-101.