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MACF1_RAT
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   03-AUG-2022, entry version 80.
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}.
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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.ENSRNOP00000041065; -.
DR   CarbonylDB; D3ZHV2; -.
DR   iPTMnet; D3ZHV2; -.
DR   jPOST; D3ZHV2; -.
DR   PaxDb; D3ZHV2; -.
DR   PeptideAtlas; D3ZHV2; -.
DR   PRIDE; D3ZHV2; -.
DR   GeneID; 362587; -.
DR   UCSC; RGD:1306057; rat.
DR   CTD; 23499; -.
DR   RGD; 1306057; Macf1.
DR   eggNOG; KOG0516; Eukaryota.
DR   InParanoid; D3ZHV2; -.
DR   OrthoDB; 24858at2759; -.
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: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; cd00014; CH; 2.
DR   CDD; cd00051; EFh; 1.
DR   CDD; cd00176; SPEC; 15.
DR   Gene3D; 1.10.418.10; -; 2.
DR   Gene3D; 3.30.920.20; -; 1.
DR   InterPro; IPR001589; Actinin_actin-bd_CS.
DR   InterPro; IPR001715; CH-domain.
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; IPR043197; Plakin.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   PANTHER; PTHR23169; PTHR23169; 8.
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_like; 1.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00054; EFh; 2.
DR   SMART; SM00243; GAS2; 1.
DR   SMART; SM00150; SPEC; 34.
DR   SUPFAM; SSF143575; SSF143575; 1.
DR   SUPFAM; SSF47473; SSF47473; 1.
DR   SUPFAM; SSF47576; SSF47576; 1.
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
 
 
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