| General information | | DisProt: | DP00467 | | Name: | Ankyrin-2 | | Synonym(s): | ANK2_HUMAN
ANK-2
Brain ankyrin
Ankyrin-B
Non-erythroid ankyrin
| | First appeared in release: | Release 3.1 (03/31/2006) | | UniProt: | Q01484 | | UniGene: | Hs.620557 | | SwissProt: | ANK2_HUMAN | | TrEMBL: | | | NCBI (GI): | 215274185 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 1839 | | Percent disordered: | 15% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MMNEDAAQKS DSGEKFNGSS QRRKRPKKSD SNASFLRAAR AGNLDKVVEY LKGGIDINTC - 60
NQNGLNALHL AAKEGHVGLV QELLGRGSSV DSATKKGNTA LHIASLAGQA EVVKVLVKEG - 120
ANINAQSQNG FTPLYMAAQE NHIDVVKYLL ENGANQSTAT EDGFTPLAVA LQQGHNQAVA - 180
ILLENDTKGK VRLPALHIAA RKDDTKSAAL LLQNDHNADV QSKMMVNRTT ESGFTPLHIA - 240
AHYGNVNVAT LLLNRGAAVD FTARNGITPL HVASKRGNTN MVKLLLDRGG QIDAKTRDGL - 300
TPLHCAARSG HDQVVELLLE RGAPLLARTK NGLSPLHMAA QGDHVECVKH LLQHKAPVDD - 360
VTLDYLTALH VAAHCGHYRV TKLLLDKRAN PNARALNGFT PLHIACKKNR IKVMELLVKY - 420
GASIQAITES GLTPIHVAAF MGHLNIVLLL LQNGASPDVT NIRGETALHM AARAGQVEVV - 480
RCLLRNGALV DARAREEQTP LHIASRLGKT EIVQLLLQHM AHPDAATTNG YTPLHISARE - 540
GQVDVASVLL EAGAAHSLAT KKGFTPLHVA AKYGSLDVAK LLLQRRAAAD SAGKNGLTPL - 600
HVAAHYDNQK VALLLLEKGA SPHATAKNGY TPLHIAAKKN QMQIASTLLN YGAETNIVTK - 660
QGVTPLHLAS QEGHTDMVTL LLDKGANIHM STKSGLTSLH LAAQEDKVNV ADILTKHGAD - 720
QDAHTKLGYT PLIVACHYGN VKMVNFLLKQ GANVNAKTKN GYTPLHQAAQ QGHTHIINVL - 780
LQHGAKPNAT TANGNTALAI AKRLGYISVV DTLKVVTEEV TTTTTTITEK HKLNVPETMT - 840
EVLDVSDEEG DDTMTGDGGE YLRPEDLKEL GDDSLPSSQF LDGMNYLRYS LEGGRSDSLR - 900
SFSSDRSHTL SHASYLRDSA VMDDSVVIPS HQVSTLAKEA ERNSYRLSWG TENLDNVALS - 960
SSPIHSGFLV IFMVDARGGA MRGCRHNGLR IIIPPRKCTA PTRVTCRLVK RHRLATMPPM - 1020
VEGEGLASRL IEVGPSGAQF LGPVIVEIPH FAALRGKERE LVVLRSENGD SWKEHFCDYT - 1080
EDELNEILNG MDEVLDSPED LEKKRICRII TRDFPQYFAV VSRIKQDSNL IGPEGGVLSS - 1140
TVVPQVQAVF PEGALTKRIR VGLQAQPMHS ELVKKILGNK ATFSPIVTLE PRRRKFHKPI - 1200
TMTIPVPKAS SDVMLNGFGG DAPTLRLLCS ITGGTTPAQW EDITGTTPLT FVNECVSFTT - 1260
NVSARFWLID CRQIQESVTF ASQVYREIIC VPYMAKFVVF AKSHDPIEAR LRCFCMTDDK - 1320
VDKTLEQQEN FAEVARSRDV EVLEGKPIYV DCFGNLVPLT KSGQHHIFSF FAFKENRLPL - 1380
FVKVRDTTQE PCGRLSFMKE PKSTRGLVHQ AICNLNITLP IYTKESESDQ EQEEEIDMTS - 1440
EKNPQDEQER IEERLAYIAD HLGFSWTELA RELDFTEEQI HQIRIENPNS LQDQSQYLLK - 1500
IWLERDGKHA TDTNLVECLT KINRMDIVHL METNTEPLQE RISHSYAEIE QTITLDHSEG - 1560
FSVLQEELCT AQHKQKEEQA VSKESETCDH PPIVSEEDIS VGYSTFQDGV PKTEGDSSST - 1620
ALFPQTHKEQ VQQDFSGKMQ DLPEESSLEY QQEYFVTTPG TETSETQKAM IVPSSPSKTP - 1680
EEVSTPAEEE KLYLQTPTSS ERGGSPIIQE PEEPSEHREE SSPRKTSLVI VESADNQPET - 1740
CERLDEDAAF EKGDDMPEIP PETVTEEEYI DEHGHTVVKK VTRKIIRRYV SSEGTEKEEI - 1800
MVQGMPQEPV NIEEGDGYSK VIKRVVLKSD TEQSEDNNE
|
| Functional narrative |
Ankyrins are a family of membrane adaptor proteins required for the localization of diverse ion channels, transporters, calciumrelease channels, and cell adhesion molecules to specialized membrane domains. The ankyrin family is comprised of three genes, ANK1, ANK2, and ANK3, that encode ankyrin-R, ankyrin-B, and ankyrin-G polypeptides, respectively. Ankyrin-B polypeptides are required for the localization of InsP3-receptor, Na/Ca exchanger, and Na/K ATPase to transverse-tubule/sarcoplasmic reticulum membranes in heart. Attaches integral membrane proteins to cytoskeletal elements. Also binds to cytoskeletal proteins. In addition, loss of function mutations in ankyrin-B causes a stress-induced cardiac arrhythmia syndrome in humans. It can be phosphorylated at multiple sites by different protein kinases and each phosphorylation event regulates the protein's structure and function. Attaches integral membrane proteins to cytoskeletal elements. Also binds to cytoskeletal proteins. Required for coordinate assembly of Na/Ca exchanger, Na/K ATPase and InsP3 receptor at sarcoplasmic reticulum sites in cardiomyocytes. Required for the coordinated expression of the Na/K ATPase, Na/Ca exchanger and beta-2-spectrin (SPTBN1) in the inner segment of rod photoreceptors. Required for expression and targeting of SPTBN1 in neonatal cardiomyocytes and for the regulation of neonatal cardiomyocyte contraction rate.
|
| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
|
| Region 1 | | Type: | Disordered - Extended | | Name: | C-terminal domain | | Location: | 1555 - 1839 | | Length: | 285 | | Region sequence: |
LDHSEGFSVLQEELCTAQHKQKEEQAVSKESETCDHPPIVSEEDISVGYSTFQDGVPKTE
GDSSSTALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTETSETQKAMIVPS
SPSKTPEEVSTPAEEEKLYLQTPTSSERGGSPIIQEPEEPSEHREESSPRKTSLVIVESA
DNQPETCERLDEDAAFEKGDDMPEIPPETVTEEEYIDEHGHTVVKKVTRKIIRRYVSSEG
TEKEEIMVQGMPQEPVNIEEGDGYSKVIKRVVLKSDTEQSEDNNE | | Modification type: | Fragment
Native
| | PDB: | | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | | | Functional subclasses: | Autoregulatory
| Detection methods:
- Circular dichroism (CD) spectroscopy, near-UV (298 K; pH: 7.4; 10 mM Na phosphate, 150 mM NaF; 150 µg/ml protein; 1mm path-length)
- Size exclusion/gel filtration chromatography (pH: 8.2; Superose 12 column)
| References:
- Abdi KM, Mohler PJ, Davis JQ, Bennett V. "Isoform specificity of ankyrin-B: A site in the divergent C-terminal domain is required for intramolecular association." J Biol Chem. 2006; 281(9): 5741-9. PubMed: 16368689
| Comments:
|
| References |
- Hryniewicz-Jankowska A, Czogalla A, Bok E, Sikorsk AF. "Ankyrins, multifunctional proteins involved in many cellular pathways." Folia Histochem Cytobiol. 2002; 40(3): 239-49. PubMed: 12219834
|
| Comments |
The brain ankyrin gene (ANK2) encodes 3 different alternatively spliced mRNAs. The 3 splice products are: isoform 1 (430KDa, 3924aa), isoform 2 (205KDa, 1872aa) and isoform 3 (202KDa, 1839aa). The structure of isoform 3 was studied in the paper given as a reference.
The isoforms specified by the previous annotator do not appear to be correct based on the sequence length. 5 isoforms actually exist for ankyrin-B in humans.
|
| If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
Disprot-footer
|
