ID MACF1_RAT Reviewed; 5430 AA.
AC D3ZHV2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Microtubule-actin cross-linking factor 1 {ECO:0000305};
DE AltName: Full=Actin cross-linking family 7;
GN Name=Macf1 {ECO:0000312|RGD:1306057}; Synonyms=Acf7, Aclp7, Macf;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP SUBCELLULAR LOCATION, INTERACTION WITH AXIN1 AND LRP6, AND IDENTIFICATION
RP IN A COMPLEX WITH AXIN1; APC; GSK3B AND CTNNB1.
RX PubMed=16815997; DOI=10.1101/gad.1411206;
RA Chen H.J., Lin C.M., Lin C.S., Perez-Olle R., Leung C.L., Liem R.K.;
RT "The role of microtubule actin cross-linking factor 1 (MACF1) in the Wnt
RT signaling pathway.";
RL Genes Dev. 20:1933-1945(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5296, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-280; SER-1860;
RP SER-2429; SER-2454 AND SER-4074, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: F-actin-binding protein which plays a role in cross-linking
CC actin to other cytoskeletal proteins and also binds to microtubules.
CC Plays an important role in ERBB2-dependent stabilization of
CC microtubules at the cell cortex (By similarity). Acts as a positive
CC regulator of Wnt receptor signaling pathway and is involved in the
CC translocation of AXIN1 and its associated complex (composed of APC,
CC CTNNB1 and GSK3B) from the cytoplasm to the cell membrane (By
CC similarity). Has actin-regulated ATPase activity and is essential for
CC controlling focal adhesions (FAs) assembly and dynamics (By
CC similarity). Interaction with CAMSAP3 at the minus ends of non-
CC centrosomal microtubules tethers microtubules minus-ends to actin
CC filaments, regulating focal adhesion size and cell migration (By
CC similarity). May play role in delivery of transport vesicles containing
CC GPI-linked proteins from the trans-Golgi network through its
CC interaction with GOLGA4 (By similarity). Plays a key role in wound
CC healing and epidermal cell migration (By similarity). Required for
CC efficient upward migration of bulge cells in response to wounding and
CC this function is primarily rooted in its ability to coordinate
CC microtubule dynamics and polarize hair follicle stem cells (By
CC similarity). As a regulator of actin and microtubule arrangement and
CC stabilization, it plays an essential role in neurite outgrowth,
CC branching and spine formation during brain development (By similarity).
CC {ECO:0000250|UniProtKB:Q9QXZ0, ECO:0000250|UniProtKB:Q9UPN3}.
CC -!- SUBUNIT: Interacts with MAPRE1, CLASP1, CLASP2 and GOLGA4 (By
CC similarity). Interacts with AXIN1 and LRP6 (PubMed:16815997). Found in
CC a complex composed of MACF1, APC; AXIN1, CTNNB1 and GSK3B
CC (PubMed:16815997). Interacts with CAMSAP3 (By similarity).
CC {ECO:0000250|UniProtKB:Q9QXZ0, ECO:0000250|UniProtKB:Q9UPN3,
CC ECO:0000269|PubMed:16815997}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9UPN3}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9UPN3}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q9UPN3}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9UPN3}. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:Q9UPN3}. Membrane {ECO:0000269|PubMed:16815997}.
CC Note=The phosphorylated form is found in the cytoplasm while the non-
CC phosphorylated form associates with the microtubules (By similarity).
CC Localizes to the tips of microtubules. Associated with the minus-end of
CC microtubules via interaction with CAMSAP3. APC controls its
CC localization to the cell membrane which is critical for its function in
CC microtubule stabilization (By similarity).
CC {ECO:0000250|UniProtKB:Q9QXZ0, ECO:0000250|UniProtKB:Q9UPN3}.
CC -!- DOMAIN: The C-terminal tail is required for phosphorylation by GSK3B
CC and for microtubule-binding. {ECO:0000250|UniProtKB:Q9QXZ0}.
CC -!- PTM: Phosphorylated on serine residues in the C-terminal tail by GSK3B.
CC Phosphorylation inhibits microtubule-binding and this plays a critical
CC role in bulge stem cell migration and skin wound repair. Wnt-signaling
CC can repress phosphorylation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the plakin or cytolinker family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC114512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_017448990.1; XM_017593501.1.
DR SMR; D3ZHV2; -.
DR CORUM; D3ZHV2; -.
DR IntAct; D3ZHV2; 1.
DR MINT; D3ZHV2; -.
DR STRING; 10116.ENSRNOP00000075119; -.
DR CarbonylDB; D3ZHV2; -.
DR iPTMnet; D3ZHV2; -.
DR jPOST; D3ZHV2; -.
DR PaxDb; 10116-ENSRNOP00000041065; -.
DR PeptideAtlas; D3ZHV2; -.
DR GeneID; 362587; -.
DR UCSC; RGD:1306057; rat.
DR AGR; RGD:1306057; -.
DR CTD; 23499; -.
DR RGD; 1306057; Macf1.
DR eggNOG; KOG0516; Eukaryota.
DR InParanoid; D3ZHV2; -.
DR OrthoDB; 5489926at2759; -.
DR PRO; PR:D3ZHV2; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0051011; F:microtubule minus-end binding; ISS:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; ISO:RGD.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; ISO:RGD.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; ISS:UniProtKB.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0001707; P:mesoderm formation; ISO:RGD.
DR GO; GO:0045773; P:positive regulation of axon extension; ISO:RGD.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0010632; P:regulation of epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0032886; P:regulation of microtubule-based process; ISS:UniProtKB.
DR GO; GO:0150011; P:regulation of neuron projection arborization; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; ISO:RGD.
DR GO; GO:0042060; P:wound healing; ISS:UniProtKB.
DR CDD; cd21240; CH_MACF1_rpt2; 1.
DR CDD; cd21188; CH_PLEC-like_rpt1; 1.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 15.
DR Gene3D; 1.20.58.1060; -; 1.
DR Gene3D; 1.20.58.60; -; 33.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 3.30.920.20; Gas2-like domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR041615; Desmoplakin_SH3.
DR InterPro; IPR041573; Desmoplakin_Spectrin-like.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR003108; GAR_dom.
DR InterPro; IPR036534; GAR_dom_sf.
DR InterPro; IPR049538; PCN-like_spectrin-like_rpt.
DR InterPro; IPR043197; Plakin.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR23169; ENVOPLAKIN; 1.
DR PANTHER; PTHR23169:SF25; MICROTUBULE-ACTIN CROSS-LINKING FACTOR 1, ISOFORMS 1_2_3_4_5; 1.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF02187; GAS2; 1.
DR Pfam; PF17902; SH3_10; 1.
DR Pfam; PF00435; Spectrin; 18.
DR Pfam; PF18373; Spectrin_2; 1.
DR Pfam; PF21019; Spectrin_3; 1.
DR Pfam; PF21020; Spectrin_4; 1.
DR Pfam; PF21097; SR_plectin_7; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM01129; DELLA; 1.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00243; GAS2; 1.
DR SMART; SM00150; SPEC; 34.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF143575; GAS2 domain-like; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 31.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS51460; GAR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Calcium; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; Golgi apparatus; Leucine-rich repeat; Membrane;
KW Metal-binding; Microtubule; Phosphoprotein; Reference proteome; Repeat;
KW SH3 domain; Wnt signaling pathway.
FT CHAIN 1..5430
FT /note="Microtubule-actin cross-linking factor 1"
FT /id="PRO_0000409709"
FT DOMAIN 78..181
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 148..171
FT /note="LRR 1"
FT DOMAIN 194..298
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 240..264
FT /note="LRR 2"
FT REPEAT 377..399
FT /note="LRR 3"
FT REPEAT 441..464
FT /note="LRR 4"
FT DOMAIN 868..925
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 1050..1073
FT /note="LRR 5"
FT REPEAT 1128..1154
FT /note="LRR 6"
FT REPEAT 1187..1210
FT /note="LRR 7"
FT REPEAT 1257..1282
FT /note="LRR 8"
FT REPEAT 1579..1602
FT /note="LRR 9"
FT REPEAT 1629..1653
FT /note="LRR 10"
FT REPEAT 1816..1891
FT /note="Spectrin 1"
FT REPEAT 1869..1891
FT /note="LRR 11"
FT REPEAT 1933..2041
FT /note="Spectrin 2"
FT REPEAT 2058..2083
FT /note="LRR 12"
FT REPEAT 2194..2220
FT /note="LRR 13"
FT REPEAT 2399..2507
FT /note="Spectrin 3"
FT REPEAT 2444..2467
FT /note="LRR 14"
FT REPEAT 2534..2557
FT /note="LRR 15"
FT REPEAT 2702..2725
FT /note="LRR 16"
FT REPEAT 2733..2837
FT /note="Spectrin 4"
FT REPEAT 2842..2945
FT /note="Spectrin 5"
FT REPEAT 2984..3009
FT /note="LRR 17"
FT REPEAT 3105..3127
FT /note="LRR 18"
FT REPEAT 3169..3274
FT /note="Spectrin 6"
FT REPEAT 3214..3237
FT /note="LRR 19"
FT REPEAT 3281..3383
FT /note="Spectrin 7"
FT REPEAT 3388..3491
FT /note="Spectrin 8"
FT REPEAT 3714..3818
FT /note="Spectrin 9"
FT REPEAT 3737..3761
FT /note="LRR 20"
FT REPEAT 3825..3927
FT /note="Spectrin 10"
FT REPEAT 3846..3870
FT /note="LRR 21"
FT REPEAT 4047..4152
FT /note="Spectrin 11"
FT REPEAT 4157..4261
FT /note="Spectrin 12"
FT REPEAT 4267..4370
FT /note="Spectrin 13"
FT REPEAT 4375..4481
FT /note="Spectrin 14"
FT REPEAT 4486..4589
FT /note="Spectrin 15"
FT REPEAT 4538..4561
FT /note="LRR 22"
FT REPEAT 4594..4700
FT /note="Spectrin 16"
FT REPEAT 4707..4808
FT /note="Spectrin 17"
FT REPEAT 4812..4916
FT /note="Spectrin 18"
FT DOMAIN 5083..5118
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 5119..5154
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 5159..5231
FT /note="GAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00792"
FT REGION 1..295
FT /note="Actin-binding"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4993..5023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 5159..5430
FT /note="C-terminal tail"
FT /evidence="ECO:0000250"
FT REGION 5247..5430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 5355..5370
FT /note="4 X 4 AA tandem repeats of [GS]-S-R-[AR]"
FT COMPBIAS 8..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 5266..5345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 5377..5430
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 5096
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 5098
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 5100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 5102
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 5107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 5132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 5134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 5136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 5138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 5143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXZ0"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXZ0"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN3"
FT MOD_RES 1367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN3"
FT MOD_RES 1376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN3"
FT MOD_RES 1860
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2429
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2769
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN3"
FT MOD_RES 2895
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN3"
FT MOD_RES 3368
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXZ0"
FT MOD_RES 4074
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 4252
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN3"
FT MOD_RES 5009
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN3"
FT MOD_RES 5296
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES 5321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN3"
FT MOD_RES 5334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN3"
FT MOD_RES 5372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UPN3"
FT MOD_RES 5375
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXZ0"
SQ SEQUENCE 5430 AA; 619600 MW; C15B030F89CD5FBF CRC64;
MSSSDEETLS ERSCRSERSC RSERSYRSER SGSLSPCPPG DTLPWNLPLH EQKKRKSQDS
VLDPAERAVV RVADERDRVQ KKTFTKWVNK HLMKVRKHIN DLYEDLRDGH NLISLLEVLS
GIKLPREKGR MRFHRLQNVQ IALDFLKQRQ VKLVNIRNDD ITDGNPKLTL GLIWTIILHF
QISDIYISGE SGDMSAKEKL LLWTQKVTAG YTGIKCTNFS SCWSDGKMFN ALIHRYRPDL
VDMERVQIQS NRENLEQAFE VAERLGVTRL LDAEDVDVPS PDEKSVITYV SSIYDAFPKV
PEGGEGISAT EVDSRWQEYQ SRVDSLIPWI RQHTILMSDK SFPQNPVELK ALYNQYIHFK
ETEILAKERE KGRIKELYKL LEVWIEFGRI KLPQGYHPNH VEEEWGKLIV EMLEREKSLR
PAVERLELLL QIANKIQNGA LNCEEKLTLA KNTLQADAAH LESGQPVQCE SDVIMYIQEC
EGLIRQLQVD LQILRDEKYY QLEELAFRVM RLQDELVTLR LECTNLYRKG HFTSLELVPP
STLTTTHLKA EPLNKTTHSS STSWFRKPMT RTELVAISSS EDEGSLRFVY ELLSWVEEMQ
MKLERAEWGN DLPSVELQWE TQQHIHTSVE ELGSSVKEAR LYEGKMSQNF HTSYVETLGK
LETQYCKLKE TSSFRMRHLQ SLHKFVSKAT AELIWLNGKE EEELACDWSD SNPNISAKKA
YFSELTMELE GKQDVFRSLQ DTAELLSLEN HPAKQTVEAY SAAVQSQLQW MKQLCLCVEQ
HIKENAAYFQ FFSDARDLES FLRNLQDSIK RKYTCDHNTS LSRLEDLLQD SMDEKEQLIQ
SKSSVASLVG RSKTIVQLKP RNPDHVLKST LSVKAICDYR QIEITICKND ECVLEDNSQR
TKWKVISPTG NEAMVPSVCL LIPPPNTEAI DVASRVEQSY QKVMALWHQL HINTKSLISW
NYLRKDIDAV QTWNLEKLRS SAPGECHQVM KNLQAHYEDF LQDSHDSALF SVADRLRIEE
EVEACKTHFQ QLMESMENED KEETLAKVYI SELKNIRLRL EECEQRLLKQ IQSSASSKTD
RDARQDVALR IAEQEHVQED LKHLRSDLDA VSVKCTTFLQ QSPSGSSATT LRSELNLMVE
KMDHVYGLSI VCLNKLKTID VIVRSIQDAE LLVKGYEIKL SQEEAVPADL SALESHRTTL
QHWLSDVKDK NSVFSVLDEE ISKAKAVAEQ LHHRAAEPNL DLERYQEKGS QLQERWHRVI
AQLETRQSEV ESIQEVLRDY RACHGTLIKW IEETTAQQEM MKPGQAEDSR VLSEQLSQQT
ELFAEIERNQ TKLDQCQKLS QQYSTTVKDY ELQLMTYKAF VESQQKSPGK RRRMISSSDA
ITQEFMDLRT RYTALVTLTT QHVKYISDAL RRLEEEEKVV EEEKQEHVEK VKDLLGWVST
LARNTQGTTT SSRTSASTDI EKAILEQQVL AEELTTKKEQ VSEAIKTSQI FLAKHGHKLS
EREKEQISEQ LCALNKTYHD LCDGSANQLQ QLQSELAQQT EQKTLQKQQD TCHKKLEDLR
SWVRQAERAL ERHRGRASQQ ELSALQQNQS DLKDLQGDIQ NHSTSFATAV KDIEGFLEEN
QNKLSPQELT ALREKLYQAK EQYEGLQDRT REAQKELEEA VTSALQQETE KSKAATELAE
NRRKIDALLD WVTSVGSSDR QPQTSLPGTE QFSGACLEKQ TLDATDGCVD VNQVPEKLDR
QYELMKARHQ ELLSQQQNFI VATQSAQSFL DQHSHNLTPE ERQMLQEKLG ELKEQYAASL
AQSEAKLRQT QTLRDELQKF LQDHREFENW LERSENELDG MHTGGSSPEA LNSLLKRQGS
FSEDVISHKG DLRFVTISGQ KVLETENNFE EGQEPSPTRN LVNEKLKDAT ERYTTLHSKC
TRLGSHLNML LGQYQQFQSS ADSLQAWMLT CEASVEKLLS DTVASDPGIL QQQLATTKQL
QEELAEHQVP VEKLQKAAHD LMDIEGEPSL DCTPIRETTE SIFSRFQSLS CSLAERSALL
QKAIAQSQSV QESMESLLQS MKEVEQNLEG EQVAALSSGL IQEALANNMK LKQDIARQKS
SLEATREMVT RFMETADGNS AAVLQDRLAE LSQRFHRLQL QQQEKESGLK KLLPQAETFE
QLSSKLQQFV EHKNRLLASG NQPDQDIAHF SQHIQELTLE MEDQKENLGT LEHLVTALGS
CGFALDLSQH QEKIQNLKKD FTELQKTVQE REKDASNCQE QLDEFRKLIR TFQKWLKETE
GNVPPAETFV SAKELEKQIE HLKGLLDDWA GKGVLVEEIN TKGTALESLI MDITAPDSQA
KTGSVLPSVG SSVGSVNGYH TCKDLTEIQC DMSDVNSKYD KLGDALRERQ ESLQTVLSRM
EEVQKEASSV LQWLESKEEV LKGMDASLSP TKTETVKAQA ESNKAFLAEL EQNSPKIQKV
KEALAGLLEA YPNSQEAENW RKMQEDLNSR WEKATEVTVA RQKQLEESAS HLACFQAAES
QLRPWLMEKE LMMGVLGPLS IDPNMLNAQK QQVQFMLKEF EARRQQHEQL TEAAQGILTG
PGDVSPSASQ VHKDLQSISQ KWVELTDKLN SRSTQIDQAI VKSTQYQDLL QDLSEKVKAV
GQRLSGQSAI STQPDAVKQQ LEETSEIRSD LGQLDDEMKE AQTLCQELSL LIGEQYLKDE
LKKRLETVAL PLQGLEDLAA DRMNRLQAAL ASTQQFQQMF DELRTWLDEK QSQQAKNCPI
SAKLERLQSQ LQENEEFQKN LNQHSGSYEV IVAEGESLLL SVPPGEEKKT LQNQLVELKS
HWEDLNKKTV DRQSRLKDCM QKAQKYQWHV EDLVPWIKDC KSKMSELQVT LDPVQLESSL
LRSKAMLNEA EKRRSLLEIL NSAADILINS SEIDEDEIRD EKAGLNQNMD AITEELQAKT
GSLEEMTQRL KEFQESFKNI EKKVEGAKHQ LEIFDALGSQ ACSNKNLEKL KAQREVLQAL
DPQVDYLRDF TRGLVEDAPD GSDASPLVHQ AELAQQEFLE VKQRVNSSCL TMENKLEGIG
QFHCRVREMF SQLADLDDEL DGMGAIGRDT DSLQSQIEDI RLFLNKIQAL RLDIEDSEAE
CRKMLEEEGT LDLLGLKREL EALNKQCGKL TERGKARQEQ LELTLGRVED FYSKLKALND
AATAAEEGEA LQWIVGTEVD VINQQLADFK MFQKEQVDPL QVKLQQVNGL GQGLIQSAGK
TCDVQGLEHD MEEVNTRWNT LNKKVAQRIA QLQEALLHCG KFQDALEPLL SWLTDTEELI
ANQKPPSAEY KVVKAQIQEQ KLLQRLLDDR KATVDMLQAE GGRIAQAAEL ADREKITGQL
ESLECRWTEL LSKAAARQKQ LEDILVLAKQ FHETAEPISD FLSVTEKKLA NSEPVGTQTA
KIHQQIIRHK ALEEEIENHA ADVQQAVKIG QSLSSLICPA EQGIMSEKLD SLQARYSEIQ
DRCCRKASLL EQALFNARLF GEDEVEVLNW LAEVEDKLSA VFVKDYRQDV LQKQHADHLA
LNEEIINRKK NVDQAIKNGQ ALLKQTTGEE VLLIQEKLDG IKTRYADITV TSSKALRTLE
QARQLATKFH STYEELTGWL REVEEELAAS GGQSPTGEQI PQFQQRQKEL KKEVMEHRLV
LDTVNEVSHA LLELVPWRAR EGLDKLVSDA NEQYKLVSDT VGQRVDEIDA AIQRSQQYEQ
AADAELAWVA ETKRKLMALG PIRLEQDQTT AQLQVQKAFS IDIIRHKDSM DELFSHRGEI
FSTCGEEQKA VLQEKTECLI QQYEAVSLLN SERYARLERA QVLVNQFWET YEELSPWAEE
TLALIAQLPP PAVDHEQLRQ QQEEMRQLRE SIAEHKPHID KILKIGPQLK ELNPEEGKMV
EEKYQKAENM YAQIKDEVRQ RALALDEAVS QSAQIAEFHD KIEPMLETLE NLSSRLRMPP
LIPAEVDKIR ECISDNKSAT MELEKLQPSF EALKRRGEEL IGRSQGADKD LAAKEIQDKL
DQMVFFWEDI KARSEEREIK FLDVLELAEK FWYDMAALLT TIKDTQEIVH DLESPGIDPS
IIKQQVEAAE TIKEETDGLH EELEFIRILG ADLIFACGET EKPEVKKSID EMNNAWENLN
RTWKERLEKL EDAMQAAVQY QDTLQAMFDW LDNTVIRLCT MPPVGTDLNT VKDQLNEMKE
FKVEVYQQQI EMEKLNHQGE LMLKKATDET DRDIIREPLT ELKHLWENLG EKIAHRQHKL
EGALLALGQF QHALEELMGW LTHTEELLDA QRPISGDPKV IEVELAKHHV LKNDVLAHQA
TVETVNKAGN ELLESSAGDD ASSLRSRLET MNQCWESVLQ KTEEREQQLQ STLQQAQGFH
SEIEEFLLEL NRMESQLSAS KPTGGLPETA REQLDAHMEL HSQLRAKEEI YNQLLDKGRL
MLLSRGDSGS GSKTEQSVAL LEQKWHVVSS KVEERKSKLE EALSLATEFQ NSLQEFINWL
TLAEQSLNIA SPPSLILNTV LSQIEEHKVF ANEVNAHRDQ IIELDQTGNQ LKFLSQKQDV
VLIKNLLVSV QSRWEKVVQR SIERGRSLDD ARKRAKQFHE AWKKLIDWLE DAESHLDSEL
EISNDPDKIK LQLSKHKEFQ KTLGGKQPVY DTTIRTGRAL KEKTLLADDA QKLDNLLGEV
RDKWDTVCGK SVERQHKLEE ALLFSGQFMD ALQALVDWLY KVEPQLAEDQ PVHGDLDLVM
NLMDAHKVFQ KELGKRTGTV QVLKRSGREL IESSRDDTTW VKGQLQELST RWDTVCKLSV
SKQSRLEQAL KQAEEFRDTV HMLLEWLSEA EQTLRFRGAL PDDTEALQSL IDTHKEFMKK
VEEKRVDVNA AVAMGEVILA VCHPDCITTI KHWITIIRAR FEEVLTWAKQ HQQRLETALS
ELVANAELLE ELLAWIQWAE TTLIQRDQEP IPQNIDRVKA LITEHQSFME EMTRKQPDVD
RVTKTYKRKN IEPTHAPFIE KSRSGSRKSL NQPTPPPMPI LSQSEAKNPR INQLSARWQQ
VWLLALERQR KLNDALDRLE ELKEFANFDF DVWRKKYMRW MNHKKSRVMD FFRRIDKDQD
GKITRQEFID GILASKFPTT KLEMTAVADI FDRDGDGYID YYEFVAALHP NKDAYRPTTD
ADKIEDEVTR QVAQCKCAKR FQVEQIGENK YRFGDSQQLR LVRILRSTVM VRVGGGWMAL
DEFLVKNDPC RARGRTNIEL REKFILPEGA SQGMTPFRSR GRRSKPSSRA ASPTRSSSSA
SQSNHSCTSM PSSPATPASG TKVISSTGSK LKRPTPTFHS SRTSLAGDTS NSSSPASTGA
KTNRADPKKS ASRPGSRAGS RAGSRASSRR GSDASDFDLL ETQSACSDTS ESSAAGGQGS
SRRGLTKPSK IPTMSKKTTT ASPRTPCPKR
//
