MACF1_HUMAN
ID MACF1_HUMAN Reviewed; 7388 AA.
AC Q9UPN3; B1ALC5; E9PJT0; O75053; Q5VW20; Q8WXY1; Q8WXY2; Q96PK2; Q9H540;
AC Q9UKP0; Q9ULG9;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 4.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Microtubule-actin cross-linking factor 1, isoforms 1/2/3/4/5 {ECO:0000305};
DE AltName: Full=620 kDa actin-binding protein;
DE Short=ABP620;
DE AltName: Full=Actin cross-linking family protein 7 {ECO:0000303|PubMed:20937854};
DE AltName: Full=Macrophin-1 {ECO:0000303|PubMed:10529403};
DE AltName: Full=Trabeculin-alpha;
GN Name=MACF1 {ECO:0000312|HGNC:HGNC:13664};
GN Synonyms=ABP620, ACF7 {ECO:0000303|PubMed:20937854}, KIAA0465, KIAA0754,
GN KIAA1251;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=10529403; DOI=10.1006/bbrc.1999.1538;
RA Okuda T., Matsuda S., Nakatsugawa S., Ichigotani Y., Iwahashi N.,
RA Takahashi M., Ishigaki T., Hamaguchi M.;
RT "Molecular cloning of macrophin, a human homologue of Drosophila kakapo
RT with a close structural similarity to plectin and dystrophin.";
RL Biochem. Biophys. Res. Commun. 264:568-574(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANTS VAL-4357 AND THR-6628.
RX PubMed=10559237; DOI=10.1074/jbc.274.47.33522;
RA Sun Y., Zhang J., Kraeft S.-K., Auclair D., Chang M.-S., Liu Y.,
RA Sutherland R., Salgia R., Griffin J.D., Ferland L.H., Chen L.B.;
RT "Molecular cloning and characterization of human trabeculin-alpha, a giant
RT protein defining a new family of actin-binding proteins.";
RL J. Biol. Chem. 274:33522-33530(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 4), NUCLEOTIDE SEQUENCE
RP [GENOMIC DNA] OF 182-6770 (ISOFORM 1), ALTERNATIVE SPLICING, TISSUE
RP SPECIFICITY, AND VARIANT THR-6628.
RX PubMed=11845288; DOI=10.1007/s00335-001-3037-3;
RA Gong T.-W.L., Besirli C.G., Lomax M.I.;
RT "MACF1 gene structure: a hybrid of plectin and dystrophin.";
RL Mamm. Genome 12:852-861(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 868-4417 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 868-7388 (ISOFORM 5).
RC TISSUE=Brain;
RX PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA Nomura N., Ohara O.;
RT "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT human brain.";
RL DNA Res. 4:345-349(1997).
RN [7]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [8]
RP SEQUENCE REVISION.
RA Ohara O.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH GOLGA4.
RX PubMed=15265687; DOI=10.1016/j.yexcr.2004.04.047;
RA Kakinuma T., Ichikawa H., Tsukada Y., Nakamura T., Toh B.H.;
RT "Interaction between p230 and MACF1 is associated with transport of a
RT glycosyl phosphatidyl inositol-anchored protein from the Golgi to the cell
RT periphery.";
RL Exp. Cell Res. 298:388-398(2004).
RN [10]
RP IDENTIFICATION OF ISOFORM 1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16076900; DOI=10.1242/jcs.02510;
RA Lin C.-M., Chen H.-J., Leung C.L., Parry D.A.D., Liem R.K.H.;
RT "Microtubule actin crosslinking factor 1b: a novel plakin that localizes to
RT the Golgi complex.";
RL J. Cell Sci. 118:3727-3738(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4521, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1376; SER-3927; SER-4495;
RP SER-4496; SER-6967; THR-7254; SER-7292 AND SER-7330, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1376; SER-4521 AND SER-7330,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6210, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20937854; DOI=10.1073/pnas.1000975107;
RA Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.;
RT "ErbB2 receptor controls microtubule capture by recruiting ACF7 to the
RT plasma membrane of migrating cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-1376; SER-3927 AND
RP SER-4521, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-1376; SER-4496;
RP SER-4521 AND SER-4962, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1122; SER-1367; SER-1376;
RP SER-2006; SER-2051; SER-3331; SER-3927; SER-4496; SER-4521; SER-4836;
RP SER-5808; SER-6967; SER-7279 AND SER-7330, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-814; SER-1376;
RP SER-3927; SER-5808; SER-6032 AND SER-7330, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [23]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CAMSAP3.
RX PubMed=27693509; DOI=10.1016/j.devcel.2016.09.003;
RA Ning W., Yu Y., Xu H., Liu X., Wang D., Wang J., Wang Y., Meng W.;
RT "The CAMSAP3-ACF7 complex couples noncentrosomal microtubules with actin
RT filaments to coordinate their dynamics.";
RL Dev. Cell 39:61-74(2016).
RN [24]
RP INTERACTION WITH CAMSAP3.
RX PubMed=27802168; DOI=10.1242/jcs.194878;
RA Noordstra I., Liu Q., Nijenhuis W., Hua S., Jiang K., Baars M.,
RA Remmelzwaal S., Martin M., Kapitein L.C., Akhmanova A.;
RT "Control of apico-basal epithelial polarity by the microtubule minus-end-
RT binding protein CAMSAP3 and spectraplakin ACF7.";
RL J. Cell Sci. 129:4278-4288(2016).
RN [25]
RP INVOLVEMENT IN LIS9, AND VARIANTS LIS9 ARG-6664; PHE-7135; TYR-7186;
RP GLY-7188 AND PHE-7188.
RX PubMed=30471716; DOI=10.1016/j.ajhg.2018.10.019;
RG University of Washington Center for Mendelian Genomics;
RG Center for Mendelian Genomics at the Broad Institute of MIT and Harvard;
RA Dobyns W.B., Aldinger K.A., Ishak G.E., Mirzaa G.M., Timms A.E.,
RA Grout M.E., Dremmen M.H.G., Schot R., Vandervore L., van Slegtenhorst M.A.,
RA Wilke M., Kasteleijn E., Lee A.S., Barry B.J., Chao K.R., Szczaluba K.,
RA Kobori J., Hanson-Kahn A., Bernstein J.A., Carr L., D'Arco F., Miyana K.,
RA Okazaki T., Saito Y., Sasaki M., Das S., Wheeler M.M., Bamshad M.J.,
RA Nickerson D.A., Engle E.C., Verheijen F.W., Doherty D., Mancini G.M.S.;
RT "MACF1 mutations encoding highly conserved zinc-binding residues of the GAR
RT domain cause defects in neuronal migration and axon guidance.";
RL Am. J. Hum. Genet. 103:1009-1021(2018).
RN [26]
RP VARIANTS [LARGE SCALE ANALYSIS] VAL-302; GLN-6462 AND GLU-7093.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: [Isoform 2]: F-actin-binding protein which plays a role in
CC cross-linking actin to other cytoskeletal proteins and also binds to
CC microtubules (PubMed:15265687, PubMed:20937854). Plays an important
CC role in ERBB2-dependent stabilization of microtubules at the cell
CC cortex (PubMed:20937854). Acts as a positive regulator of Wnt receptor
CC signaling pathway and is involved in the translocation of AXIN1 and its
CC associated complex (composed of APC, CTNNB1 and GSK3B) from the
CC cytoplasm to the cell membrane (By similarity). Has actin-regulated
CC ATPase activity and is essential for controlling focal adhesions (FAs)
CC assembly and dynamics (By similarity). Interaction with CAMSAP3 at the
CC minus ends of non-centrosomal microtubules tethers microtubules minus-
CC ends to actin filaments, regulating focal adhesion size and cell
CC migration (PubMed:27693509). May play role in delivery of transport
CC vesicles containing GPI-linked proteins from the trans-Golgi network
CC through its interaction with GOLGA4 (PubMed:15265687). Plays a key role
CC in wound healing and epidermal cell migration (By similarity). Required
CC for efficient upward migration of bulge cells in response to wounding
CC and 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:0000269|PubMed:15265687,
CC ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:27693509}.
CC -!- SUBUNIT: Isoform 2: Interacts with MAPRE1, CLASP1, CLASP2, AXIN1 and
CC LRP6 (By similarity). Isoform 2: Found in a complex composed of MACF1,
CC APC, AXIN1, CTNNB1 and GSK3B (By similarity). Isoform 2: Interacts with
CC GOLGA4 (PubMed:15265687). Isoform 2: Interacts with CAMSAP3
CC (PubMed:27693509, PubMed:27802168). {ECO:0000250|UniProtKB:Q9QXZ0,
CC ECO:0000269|PubMed:15265687, ECO:0000269|PubMed:27693509,
CC ECO:0000269|PubMed:27802168}.
CC -!- INTERACTION:
CC Q9UPN3; Q9NRI5: DISC1; NbExp=4; IntAct=EBI-522925, EBI-529989;
CC Q9UPN3; Q9NRI5-1: DISC1; NbExp=3; IntAct=EBI-522925, EBI-15881455;
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:15265687, ECO:0000269|PubMed:27693509}. Cytoplasm
CC {ECO:0000269|PubMed:15265687}. Golgi apparatus
CC {ECO:0000269|PubMed:15265687}. Cell membrane
CC {ECO:0000269|PubMed:20937854}. Cell projection, ruffle membrane
CC {ECO:0000269|PubMed:20937854}. Note=The phosphorylated form is found in
CC the cytoplasm while the non-phosphorylated form associates with the
CC microtubules (By similarity). Localizes to the tips of microtubules
CC (PubMed:27693509). Associated with the minus-end of microtubules via
CC interaction with CAMSAP3 (PubMed:27693509). APC controls its
CC localization to the cell membrane which is critical for its function in
CC microtubule stabilization (PubMed:20937854).
CC {ECO:0000250|UniProtKB:Q9QXZ0, ECO:0000269|PubMed:20937854,
CC ECO:0000269|PubMed:27693509}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:16076900}. Golgi apparatus
CC {ECO:0000269|PubMed:16076900}. Note=Localizes to the tips of
CC microtubules. {ECO:0000269|PubMed:16076900}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=Macf1b;
CC IsoId=Q9UPN3-1; Sequence=Displayed;
CC Name=2; Synonyms=Macf1a;
CC IsoId=Q9UPN3-2; Sequence=VSP_041391, VSP_041393;
CC Name=3;
CC IsoId=Q9UPN3-3; Sequence=VSP_041390, VSP_041391, VSP_041392,
CC VSP_041393;
CC Name=5;
CC IsoId=Q9UPN3-4; Sequence=VSP_041391, VSP_041392;
CC Name=4;
CC IsoId=Q9UPN3-5; Sequence=VSP_043626, VSP_041393, VSP_043627;
CC Name=6;
CC IsoId=O94854-3; Sequence=External;
CC Name=7;
CC IsoId=O94854-4; Sequence=External;
CC -!- TISSUE SPECIFICITY: Isoform 2: Ubiquitously expressed. Isoform 1:
CC Expressed in cell lines NCI-H460, A-549 and HaCaT. Isoform 4: Expressed
CC in heart, lung, pituitary and placenta, not found in brain, kidney,
CC liver, pancreas or skeletal muscle. {ECO:0000269|PubMed:11845288,
CC ECO:0000269|PubMed:16076900}.
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).
CC {ECO:0000250|UniProtKB:Q9QXZ0}.
CC -!- DISEASE: Lissencephaly 9 with complex brainstem malformation (LIS9)
CC [MIM:618325]: A form of lissencephaly, a disorder of cortical
CC development characterized by agyria or pachygyria and disorganization
CC of the clear neuronal lamination of normal six-layered cortex. LIS9 is
CC an autosomal dominant form clinically characterized by global
CC developmental delay apparent since infancy, impaired intellectual
CC development with poor or absent speech, and sometimes abnormal or
CC involuntary movements. Brain imaging shows malformation of the
CC brainstem, in addition to pachygyria and lissencephaly.
CC {ECO:0000269|PubMed:30471716}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the plakin or cytolinker family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA83821.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB029290; BAA83821.1; ALT_FRAME; mRNA.
DR EMBL; AF141968; AAF06360.1; -; mRNA.
DR EMBL; AF317696; AAL09459.1; -; mRNA.
DR EMBL; AF325341; AAL38997.1; -; Genomic_DNA.
DR EMBL; AF325333; AAL38997.1; JOINED; Genomic_DNA.
DR EMBL; AF325334; AAL38997.1; JOINED; Genomic_DNA.
DR EMBL; AF325335; AAL38997.1; JOINED; Genomic_DNA.
DR EMBL; AF325336; AAL38997.1; JOINED; Genomic_DNA.
DR EMBL; AF325339; AAL38997.1; JOINED; Genomic_DNA.
DR EMBL; AF325340; AAL38997.1; JOINED; Genomic_DNA.
DR EMBL; AF325341; AAL39000.1; -; Genomic_DNA.
DR EMBL; AF325330; AAL39000.1; JOINED; Genomic_DNA.
DR EMBL; AF325331; AAL39000.1; JOINED; Genomic_DNA.
DR EMBL; AF325332; AAL39000.1; JOINED; Genomic_DNA.
DR EMBL; AF325333; AAL39000.1; JOINED; Genomic_DNA.
DR EMBL; AF325334; AAL39000.1; JOINED; Genomic_DNA.
DR EMBL; AF325335; AAL39000.1; JOINED; Genomic_DNA.
DR EMBL; AF325336; AAL39000.1; JOINED; Genomic_DNA.
DR EMBL; AF325339; AAL39000.1; JOINED; Genomic_DNA.
DR EMBL; AF325340; AAL39000.1; JOINED; Genomic_DNA.
DR EMBL; AL137853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL365277; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL442071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB033077; BAA86565.1; -; mRNA.
DR EMBL; AB007934; BAA32310.3; -; mRNA.
DR CCDS; CCDS435.1; -. [Q9UPN3-2]
DR PIR; T00079; T00079.
DR RefSeq; NP_036222.3; NM_012090.5. [Q9UPN3-2]
DR PDB; 4Z6G; X-ray; 2.65 A; A=74-421.
DR PDB; 5VE9; X-ray; 2.79 A; A/B=7024-7108, C=7118-7191.
DR PDB; 5X57; X-ray; 1.45 A; A=7113-7193.
DR PDBsum; 4Z6G; -.
DR PDBsum; 5VE9; -.
DR PDBsum; 5X57; -.
DR SMR; Q9UPN3; -.
DR BioGRID; 117048; 139.
DR DIP; DIP-50616N; -.
DR IntAct; Q9UPN3; 61.
DR MINT; Q9UPN3; -.
DR STRING; 9606.ENSP00000354573; -.
DR TCDB; 8.A.66.1.8; the dystrophin (dystrophin) family.
DR GlyGen; Q9UPN3; 7 sites, 1 O-linked glycan (7 sites).
DR iPTMnet; Q9UPN3; -.
DR PhosphoSitePlus; Q9UPN3; -.
DR SwissPalm; Q9UPN3; -.
DR BioMuta; MACF1; -.
DR DMDM; 338817989; -.
DR EPD; Q9UPN3; -.
DR jPOST; Q9UPN3; -.
DR MassIVE; Q9UPN3; -.
DR MaxQB; Q9UPN3; -.
DR PaxDb; Q9UPN3; -.
DR PeptideAtlas; Q9UPN3; -.
DR PRIDE; Q9UPN3; -.
DR ProteomicsDB; 85382; -. [Q9UPN3-1]
DR ProteomicsDB; 85383; -. [Q9UPN3-2]
DR ProteomicsDB; 85384; -. [Q9UPN3-3]
DR ProteomicsDB; 85385; -. [Q9UPN3-4]
DR ProteomicsDB; 85386; -. [Q9UPN3-5]
DR Antibodypedia; 31853; 71 antibodies from 18 providers.
DR DNASU; 23499; -.
DR Ensembl; ENST00000361689.7; ENSP00000354573.2; ENSG00000127603.32. [Q9UPN3-2]
DR GeneID; 23499; -.
DR KEGG; hsa:23499; -.
DR UCSC; uc031pmd.2; human. [Q9UPN3-1]
DR CTD; 23499; -.
DR DisGeNET; 23499; -.
DR GeneCards; MACF1; -.
DR HGNC; HGNC:13664; MACF1.
DR HPA; ENSG00000127603; Low tissue specificity.
DR MalaCards; MACF1; -.
DR MIM; 608271; gene.
DR MIM; 618325; phenotype.
DR neXtProt; NX_Q9UPN3; -.
DR OpenTargets; ENSG00000127603; -.
DR Orphanet; 572013; Posterior-predominant lissencephaly-broad flat pons and medulla-midline crossing defects syndrome.
DR PharmGKB; PA30518; -.
DR VEuPathDB; HostDB:ENSG00000127603; -.
DR eggNOG; KOG0516; Eukaryota.
DR GeneTree; ENSGT00940000155824; -.
DR HOGENOM; CLU_000015_1_0_1; -.
DR InParanoid; Q9UPN3; -.
DR OrthoDB; 24858at2759; -.
DR PhylomeDB; Q9UPN3; -.
DR TreeFam; TF335163; -.
DR PathwayCommons; Q9UPN3; -.
DR SignaLink; Q9UPN3; -.
DR SIGNOR; Q9UPN3; -.
DR BioGRID-ORCS; 23499; 13 hits in 1078 CRISPR screens.
DR ChiTaRS; MACF1; human.
DR GeneWiki; MACF1; -.
DR GenomeRNAi; 23499; -.
DR Pharos; Q9UPN3; Tbio.
DR PRO; PR:Q9UPN3; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UPN3; protein.
DR Bgee; ENSG00000127603; Expressed in inferior olivary complex and 210 other tissues.
DR ExpressionAtlas; Q9UPN3; baseline and differential.
DR Genevisible; Q9UPN3; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; NAS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0051011; F:microtubule minus-end binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IDA:UniProtKB.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0045773; P:positive regulation of axon extension; IDA:UniProtKB.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0010632; P:regulation of epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; IDA:UniProtKB.
DR GO; GO:0032886; P:regulation of microtubule-based process; IMP:UniProtKB.
DR GO; GO:0150011; P:regulation of neuron projection arborization; ISS:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0042060; P:wound healing; ISS:UniProtKB.
DR CDD; cd00014; CH; 2.
DR CDD; cd00051; EFh; 1.
DR CDD; cd00176; SPEC; 16.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 3.30.920.20; -; 1.
DR Gene3D; 3.90.1290.10; -; 5.
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; IPR035915; Plakin_repeat_sf.
DR InterPro; IPR001101; Plectin_repeat.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR23169; PTHR23169; 7.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF02187; GAS2; 1.
DR Pfam; PF00681; Plectin; 8.
DR Pfam; PF17902; SH3_10; 1.
DR Pfam; PF00435; Spectrin; 17.
DR Pfam; PF18373; Spectrin_like; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM00054; EFh; 2.
DR SMART; SM00243; GAS2; 1.
DR SMART; SM00250; PLEC; 20.
DR SMART; SM00150; SPEC; 33.
DR SUPFAM; SSF143575; SSF143575; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF75399; SSF75399; 6.
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 3D-structure; Acetylation; Actin-binding; Alternative splicing; Calcium;
KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; Disease variant;
KW Golgi apparatus; Leucine-rich repeat; Lissencephaly; Membrane;
KW Metal-binding; Microtubule; Phosphoprotein; Reference proteome; Repeat;
KW SH3 domain; Wnt signaling pathway.
FT CHAIN 1..7388
FT /note="Microtubule-actin cross-linking factor 1, isoforms
FT 1/2/3/4/5"
FT /id="PRO_0000073449"
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 1577..1621
FT /note="Plectin 1"
FT REPEAT 1654..1696
FT /note="Plectin 2"
FT REPEAT 1769..1809
FT /note="Plectin 3"
FT REPEAT 1811..1848
FT /note="Plectin 4"
FT REPEAT 1855..1886
FT /note="Plectin 5"
FT REPEAT 2290..2332
FT /note="Plectin 6"
FT REPEAT 2367..2410
FT /note="Plectin 7"
FT REPEAT 2411..2437
FT /note="Plectin 8"
FT REPEAT 2501..2543
FT /note="Plectin 9"
FT REPEAT 2581..2612
FT /note="Plectin 10"
FT REPEAT 2686..2730
FT /note="Plectin 11"
FT REPEAT 3239..3262
FT /note="LRR 9"
FT REPEAT 3264..3283
FT /note="LRR 10"
FT REPEAT 3646..3669
FT /note="LRR 11"
FT REPEAT 3696..3720
FT /note="LRR 12"
FT REPEAT 3883..3957
FT /note="Spectrin 1"
FT REPEAT 3936..3958
FT /note="LRR 13"
FT REPEAT 4000..4108
FT /note="Spectrin 2"
FT REPEAT 4125..4150
FT /note="LRR 14"
FT REPEAT 4261..4287
FT /note="LRR 15"
FT REPEAT 4466..4574
FT /note="Spectrin 3"
FT REPEAT 4511..4534
FT /note="LRR 16"
FT REPEAT 4601..4624
FT /note="LRR 17"
FT REPEAT 4769..4792
FT /note="LRR 18"
FT REPEAT 4800..4904
FT /note="Spectrin 4"
FT REPEAT 4909..5012
FT /note="Spectrin 5"
FT REPEAT 5051..5076
FT /note="LRR 19"
FT REPEAT 5172..5194
FT /note="LRR 20"
FT REPEAT 5236..5341
FT /note="Spectrin 6"
FT REPEAT 5281..5304
FT /note="LRR 21"
FT REPEAT 5348..5450
FT /note="Spectrin 7"
FT REPEAT 5455..5557
FT /note="Spectrin 8"
FT REPEAT 5695..5719
FT /note="LRR 22"
FT REPEAT 5783..5885
FT /note="Spectrin 9"
FT REPEAT 5804..5828
FT /note="LRR 23"
FT REPEAT 6005..6110
FT /note="Spectrin 10"
FT REPEAT 6115..6219
FT /note="Spectrin 11"
FT REPEAT 6225..6328
FT /note="Spectrin 12"
FT REPEAT 6333..6439
FT /note="Spectrin 13"
FT REPEAT 6443..6547
FT /note="Spectrin 14"
FT REPEAT 6496..6519
FT /note="LRR 24"
FT REPEAT 6552..6658
FT /note="Spectrin 15"
FT REPEAT 6665..6766
FT /note="Spectrin 16"
FT REPEAT 6771..6874
FT /note="Spectrin 17"
FT DOMAIN 7041..7076
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 7077..7112
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 7117..7189
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 2051..2085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3013..3034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3104..3174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3321..3350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 5583..5603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 6951..6981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7117..7388
FT /note="C-terminal tail"
FT /evidence="ECO:0000250"
FT REGION 7205..7388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 7313..7328
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 2053..2076
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3125..3164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 5587..5602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7224..7303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7335..7388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 7054
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7056
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7058
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7060
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7065
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7090
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7092
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7094
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7096
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 7101
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:0000250|UniProtKB:D3ZHV2"
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:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 814
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 2006
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2051
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2077
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXZ0"
FT MOD_RES 3122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXZ0"
FT MOD_RES 3331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 3927
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 4495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 4496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 4521
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 4836
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 4962
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 5435
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXZ0"
FT MOD_RES 5808
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 6032
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 6210
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 6967
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 7254
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 7279
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 7292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 7330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 7333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXZ0"
FT VAR_SEQ 1..1565
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11845288"
FT /id="VSP_043626"
FT VAR_SEQ 1..72
FT /note="MSSSDEETLSERSCRSERSCRSERSYRSERSGSLSPCPPGDTLPWNLPLHEQ
FT KKRKSQDSVLDPAERAVVRV -> MFPVLWAGIPGRDVGSLQPLPPGFKQFCTSASRVA
FT VI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10559237"
FT /id="VSP_041390"
FT VAR_SEQ 1543..3609
FT /note="Missing (in isoform 2, isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10529403,
FT ECO:0000303|PubMed:10559237, ECO:0000303|PubMed:10574462,
FT ECO:0000303|PubMed:9455484"
FT /id="VSP_041391"
FT VAR_SEQ 4410..4430
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10559237,
FT ECO:0000303|PubMed:9455484"
FT /id="VSP_041392"
FT VAR_SEQ 5497
FT /note="K -> KALEEDIENHATDVHQAVKIGQSLSSLTSPAEQGVLSEKIDSLQARY
FT SEIQDRCCRKAALLDQALSNARLFGEDEVEVLNWLAEVEDKLSSVFVKDFKQDVLHRQH
FT ADHL (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10529403,
FT ECO:0000303|PubMed:10559237, ECO:0000303|PubMed:10574462,
FT ECO:0000303|PubMed:11845288"
FT /id="VSP_041393"
FT VAR_SEQ 7150
FT /note="R -> RFFLGNQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11845288"
FT /id="VSP_043627"
FT VARIANT 302
FT /note="E -> V (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035451"
FT VARIANT 4357
FT /note="M -> V (in dbSNP:rs2296172)"
FT /evidence="ECO:0000269|PubMed:10559237"
FT /id="VAR_048625"
FT VARIANT 6201
FT /note="K -> R (in dbSNP:rs682351)"
FT /id="VAR_048626"
FT VARIANT 6308
FT /note="A -> T (in dbSNP:rs587404)"
FT /id="VAR_048627"
FT VARIANT 6462
FT /note="E -> Q (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035452"
FT VARIANT 6628
FT /note="S -> T (in dbSNP:rs668556)"
FT /evidence="ECO:0000269|PubMed:10559237,
FT ECO:0000269|PubMed:11845288"
FT /id="VAR_048628"
FT VARIANT 6664
FT /note="G -> R (in LIS9; unknown pathological significance;
FT dbSNP:rs1488808726)"
FT /evidence="ECO:0000269|PubMed:30471716"
FT /id="VAR_081966"
FT VARIANT 6752
FT /note="T -> I (in dbSNP:rs2296174)"
FT /id="VAR_048629"
FT VARIANT 6855
FT /note="I -> V (in dbSNP:rs12068423)"
FT /id="VAR_048630"
FT VARIANT 7093
FT /note="G -> E (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_065256"
FT VARIANT 7135
FT /note="C -> F (in LIS9; dbSNP:rs1557668270)"
FT /evidence="ECO:0000269|PubMed:30471716"
FT /id="VAR_081967"
FT VARIANT 7186
FT /note="D -> Y (in LIS9; dbSNP:rs1557670503)"
FT /evidence="ECO:0000269|PubMed:30471716"
FT /id="VAR_081968"
FT VARIANT 7188
FT /note="C -> F (in LIS9; dbSNP:rs1557670520)"
FT /evidence="ECO:0000269|PubMed:30471716"
FT /id="VAR_081969"
FT VARIANT 7188
FT /note="C -> G (in LIS9; dbSNP:rs1557670515)"
FT /evidence="ECO:0000269|PubMed:30471716"
FT /id="VAR_081970"
FT CONFLICT 1295..1296
FT /note="TA -> LP (in Ref. 4; AAL39000)"
FT /evidence="ECO:0000305"
FT CONFLICT 1487
FT /note="T -> A (in Ref. 1; BAA83821 and 4; AAL39000)"
FT /evidence="ECO:0000305"
FT CONFLICT 3277
FT /note="P -> S (in Ref. 3; AAL38997)"
FT /evidence="ECO:0000305"
FT CONFLICT 4030
FT /note="V -> A (in Ref. 1; BAA83821)"
FT /evidence="ECO:0000305"
FT CONFLICT 4119
FT /note="E -> D (in Ref. 1; BAA83821)"
FT /evidence="ECO:0000305"
FT CONFLICT 4150
FT /note="E -> K (in Ref. 2; AAF06360)"
FT /evidence="ECO:0000305"
FT CONFLICT 4388
FT /note="C -> Y (in Ref. 1; BAA83821)"
FT /evidence="ECO:0000305"
FT CONFLICT 4411..4417
FT /note="SILPSVG -> EYRLFKI (in Ref. 5; BAA86565)"
FT /evidence="ECO:0000305"
FT CONFLICT 4590
FT /note="R -> Q (in Ref. 1; BAA83821)"
FT /evidence="ECO:0000305"
FT CONFLICT 6791
FT /note="Missing (in Ref. 2; AAF06360)"
FT /evidence="ECO:0000305"
FT HELIX 75..93
FT /evidence="ECO:0007829|PDB:4Z6G"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:4Z6G"
FT TURN 102..108
FT /evidence="ECO:0007829|PDB:4Z6G"
FT HELIX 110..120
FT /evidence="ECO:0007829|PDB:4Z6G"
FT HELIX 132..148
FT /evidence="ECO:0007829|PDB:4Z6G"
FT HELIX 158..162
FT /evidence="ECO:0007829|PDB:4Z6G"
FT HELIX 166..180
FT /evidence="ECO:0007829|PDB:4Z6G"
FT TURN 181..183
FT /evidence="ECO:0007829|PDB:4Z6G"
FT HELIX 196..208
FT /evidence="ECO:0007829|PDB:4Z6G"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:4Z6G"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:4Z6G"
FT HELIX 227..236
FT /evidence="ECO:0007829|PDB:4Z6G"
FT HELIX 243..246
FT /evidence="ECO:0007829|PDB:4Z6G"
FT HELIX 251..264
FT /evidence="ECO:0007829|PDB:4Z6G"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:4Z6G"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:4Z6G"
FT HELIX 283..296
FT /evidence="ECO:0007829|PDB:4Z6G"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:4Z6G"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:4Z6G"
FT HELIX 312..332
FT /evidence="ECO:0007829|PDB:4Z6G"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:4Z6G"
FT HELIX 358..361
FT /evidence="ECO:0007829|PDB:4Z6G"
FT HELIX 363..386
FT /evidence="ECO:0007829|PDB:4Z6G"
FT HELIX 398..418
FT /evidence="ECO:0007829|PDB:4Z6G"
FT STRAND 7024..7026
FT /evidence="ECO:0007829|PDB:5VE9"
FT HELIX 7028..7041
FT /evidence="ECO:0007829|PDB:5VE9"
FT HELIX 7046..7053
FT /evidence="ECO:0007829|PDB:5VE9"
FT STRAND 7058..7062
FT /evidence="ECO:0007829|PDB:5VE9"
FT HELIX 7063..7072
FT /evidence="ECO:0007829|PDB:5VE9"
FT HELIX 7079..7089
FT /evidence="ECO:0007829|PDB:5VE9"
FT STRAND 7094..7098
FT /evidence="ECO:0007829|PDB:5VE9"
FT HELIX 7099..7106
FT /evidence="ECO:0007829|PDB:5VE9"
FT HELIX 7118..7130
FT /evidence="ECO:0007829|PDB:5X57"
FT STRAND 7141..7143
FT /evidence="ECO:0007829|PDB:5X57"
FT STRAND 7148..7151
FT /evidence="ECO:0007829|PDB:5X57"
FT STRAND 7157..7163
FT /evidence="ECO:0007829|PDB:5X57"
FT STRAND 7166..7171
FT /evidence="ECO:0007829|PDB:5X57"
FT STRAND 7174..7177
FT /evidence="ECO:0007829|PDB:5X57"
FT HELIX 7178..7185
FT /evidence="ECO:0007829|PDB:5X57"
FT HELIX 7187..7192
FT /evidence="ECO:0007829|PDB:5X57"
SQ SEQUENCE 7388 AA; 838308 MW; B044DC183C048416 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 KQHTILMSDK TFPQNPVELK ALYNQYIHFK
ETEILAKERE KGRIEELYKL LEVWIEFGRI KLPQGYHPND VEEEWGKLII EMLEREKSLR
PAVERLELLL QIANKIQNGA LNCEEKLTLA KNTLQADAAH LESGQPVQCE SDVIMYIQEC
EGLIRQLQVD LQILRDENYY QLEELAFRVM RLQDELVTLR LECTNLYRKG HFTSLELVPP
STLTTTHLKA EPLTKATHSS STSWFRKPMT RAELVAISSS EDEGNLRFVY ELLSWVEEMQ
MKLERAEWGN DLPSVELQLE TQQHIHTSVE ELGSSVKEAR LYEGKMSQNF HTSYAETLGK
LETQYCKLKE TSSFRMRHLQ SLHKFVSRAT AELIWLNEKE EEELAYDWSD NNSNISAKRN
YFSELTMELE EKQDVFRSLQ DTAELLSLEN HPAKQTVEAY SAAVQSQLQW MKQLCLCVEQ
HVKENTAYFQ FFSDARELES FLRNLQDSIK RKYSCDHNTS LSRLEDLLQD SMDEKEQLIQ
SKSSVASLVG RSKTIVQLKP RSPDHVLKNT ISVKAVCDYR QIEITICKND ECVLEDNSQR
TKWKVISPTG NEAMVPSVCF LIPPPNKDAI EMASRVEQSY QKVMALWHQL HVNTKSLISW
NYLRKDLDLV QTWNLEKLRS SAPGECHQIM KNLQAHYEDF LQDSRDSVLF SVADRLRLEE
EVEACKARFQ HLMKSMENED KEETVAKMYI SELKNIRLRL EEYEQRVVKR IQSLASSRTD
RDAWQDNALR IAEQEHTQED LQQLRSDLDA VSMKCDSFLH QSPSSSSVPT LRSELNLLVE
KMDHVYGLST VYLNKLKTVD VIVRSIQDAE LLVKGYEIKL SQEEVVLADL SALEAHWSTL
RHWLSDVKDK NSVFSVLDEE IAKAKVVAEQ MSRLTPERNL DLERYQEKGS QLQERWHRVI
AQLEIRQSEL ESIQEVLGDY RACHGTLIKW IEETTAQQEM MKPGQAEDSR VLSEQLSQQT
ALFAEIERNQ TKLDQCQKFS QQYSTIVKDY ELQLMTYKAF VESQQKSPGK RRRMLSSSDA
ITQEFMDLRT RYTALVTLTT QHVKYISDAL RRLEEEEKVV EEEKQEHVEK VKELLGWVST
LARNTQGKAT SSETKESTDI EKAILEQQVL SEELTTKKEQ VSEAIKTSQI FLAKHGHKLS
EKEKKQISEQ LNALNKAYHD LCDGSANQLQ QLQSQLAHQT EQKECRAVAG VIDLGTVEIF
PIFKAMQKGL LDQDTGLVLL ESQVIMSGLI APETGENLSL EEGIARNLIN PQMYQQLREL
QDALALISRL TESRGPLSVV EAIEKRIISE TVGLKILEAH LATGGFSLSP SENCINLEEA
FHQGLISAWL HSVLESYLRT SKNLIDPNTA EKIGLLDLMQ RCIVHQESGF KLLPVKQLAG
GMVSLKSGRK VSIFRAVQEG LIDRQVTVRL LEAQLFAGGI VDPRTGHRLT VEEAVRHNLI
DQDMACAILI RQLQTGGIID TVTGQRLTID EAVSNDLVAA KIALVILESL WSFMGLLWPE
SGEILPITDA LEQGIVSTEL AHKILSNRQH IKALFLPATT EILSWKKAIE SGILDRDLAN
NLKSICIPDV MPHMQLADSA EQNINPGAAV LPCSKSHPKA TASQSENLLF QLMTHSYINV
QNGQRLLLLD KELMETLTSR DEYQTSPPKV VEIGHQRQKT PEGLQESANV KISGTFSSGW
TVRLPEFQFS SQNKEYPDRE DCTTEKGKKT TVETEDSSVE NPEQDLFVEQ KERNPNIDAL
KVINKVKLEV QRQLIGTQRE DQTAVSVREN ASRGHLLTIP PAEAEGVPLV VDKDVFSVET
PKKEHQPLRN TSFTCQNEQA HTLETEYIHD ETGGSHIKPQ SKKLQVQVKK TLGIKLELKS
ETDGNVHPLD KKEMLKKTFL AKDDHKESQE AQNIAGGSMM MSEKTDEEDS GREIFLSCSH
PLELLEEATL NVLSAQLLDG GIFHEQTGQK LLLNEAISRG IVPSHTAVKL MEKLNMFQGF
FDSQTCESLT TEEVINEGLM DEKLLHNVLM ADKAISGVLD PRTQTLCSVK DAVTVGLLDK
ETATRILERQ VVTGGIIDLK RGKKVSVTLA STLGLVDVAD QPELINLEKA SKGRDAEKTV
RERLISLQME TTGLIDPDSK APLTVVQSID RGLLEREEAV RLLTKQVVDG GIIHHISGMR
LSVDNAFRHG LIGEDLAEKL KRVENLNIHQ IFNPETKENI SLPKAIKLDL ITSDLKREIQ
EVQAFTGNFV DLISGQRLTL AEAKKEGLLT NEAVLSPGMM HGIVDPENCR IVPYSELVKK
CKIDIESGQR YLEVIPFSDI KDGVSDKVLT LSQAIQLGKV DFASTLKVLE AQANTGGIID
TATGKRLTLA SALEEKLVDE NMVRIIASHQ VLNGGIVDIF SDQRVTLVEA IEKRLISPEL
ANMIQIDSSE FSDHRAQIEK QEGIEVCALQ NEFLGKDMLI ACNQTAEMSC NKVEESERLF
QVENQSAQEK VKVRVSDGEQ AKKSREISLK EFGCKDQRKP RMSSDAKEFI SIINPHNLKG
KSLGQVSLTH PYSECDFKLK EVARNNMGND TNEEQEKAVT KIEIISHMKQ STSCLDSEEI
RENQGEVILE VQETYCETSG KLPSEQVLQQ PMNARVKSKR EKREVIVEES IRTCKPAFLS
EEKLYQETAI RDEHDSHIKS QPREMTSSEK GKEADTEMGF SITFKIEESS SQVVPQGISV
KHLDALTLFS SKQANEGKVN NLSLCLTLKP EENLSREIAC GAQSEPFPCM TPRPEGLHYQ
ESDGKAQVTG PSQISKTDKS FQGTTRQETN YQDSWVTSKT KETKHQISSS NECKEKSYQE
VSFDPARGLK LEEITVSRPD SKEVRYLEFS DRKDLHHQGS KSDDKLCGTL KSEIATQELT
GEKFLEMANP NVAGLEAGSI EDIVTQRGSR VLGSFLPEKL FKGVSQKENT GQQNAIISPT
VLETSEEKTV SLTVCSAVKT EKTPQEKLRE SPGSEQTPFM TAPEGKGNGG VNPEPFRATQ
NVFTRQLCLE HDEKLVSYLS LLRNIEMRTK QIQPLELNLA ELQDLLCQAK VLERELKDLT
TLVSQELECV NQIIISQPQE VPAQLLKALE KDAKNLQKSL SSVSDTWNSR LLHFQNAVEI
EKTKVLNQHT QLEGRLQDLR AWVGNKNLIL NSKGSNSEID VDSLNLCLQQ YEDLKQPMAE
RKAQLDALAF DIQFFISEHA QDLSPQQNRQ MLRLLNELQR SFQDILEQTA AQVDALQGHL
QQMEQEALVK TLQKQQNTCH QQLEDLCSWV GQAERALAGH QGRTTQQDLS ALQKNQSDLK
DLQDDIQNRA TSFATVVKDI EGFMEENQTK LSPRELTALR EKLHQAKEQY EALQEETRVA
QKELEEAVTS ALQQETEKSK AAKELAENKK KIDALLDWVT SVGSSGGQLL TNLPGMEQLS
GASLEKGALD TTDGYMGVNQ APEKLDKQCE MMKARHQELL SQQQNFILAT QSAQAFLDQH
GHNLTPEEQQ MLQQKLGELK EQYSTSLAQS EAELKQVQTL QDELQKFLQD HKEFESWLER
SEKELENMHK GGSSPETLPS LLKRQGSFSE DVISHKGDLR FVTISGQKVL DMENSFKEGK
EPSEIGNLVK DKLKDATERY TALHSKCTRL GSHLNMLLGQ YHQFQNSADS LQAWMQACEA
NVEKLLSDTV ASDPGVLQEQ LATTKQLQEE LAEHQVPVEK LQKVARDIME IEGEPAPDHR
HVQETTDSIL SHFQSLSYSL AERSSLLQKA IAQSQSVQES LESLLQSIGE VEQNLEGKQV
SSLSSGVIQE ALATNMKLKQ DIARQKSSLE ATREMVTRFM ETADSTTAAV LQGKLAEVSQ
RFEQLCLQQQ EKESSLKKLL PQAEMFEHLS GKLQQFMENK SRMLASGNQP DQDITHFFQQ
IQELNLEMED QQENLDTLEH LVTELSSCGF ALDLCQHQDR VQNLRKDFTE LQKTVKEREK
DASSCQEQLD EFRKLVRTFQ KWLKETEGSI PPTETSMSAK ELEKQIEHLK SLLDDWASKG
TLVEEINCKG TSLENLIMEI TAPDSQGKTG SILPSVGSSV GSVNGYHTCK DLTEIQCDMS
DVNLKYEKLG GVLHERQESL QAILNRMEEV HKEANSVLQW LESKEEVLKS MDAMSSPTKT
ETVKAQAESN KAFLAELEQN SPKIQKVKEA LAGLLVTYPN SQEAENWKKI QEELNSRWER
ATEVTVARQR QLEESASHLA CFQAAESQLR PWLMEKELMM GVLGPLSIDP NMLNAQKQQV
QFMLKEFEAR RQQHEQLNEA AQGILTGPGD VSLSTSQVQK ELQSINQKWV ELTDKLNSRS
SQIDQAIVKS TQYQELLQDL SEKVRAVGQR LSVQSAISTQ PEAVKQQLEE TSEIRSDLEQ
LDHEVKEAQT LCDELSVLIG EQYLKDELKK RLETVALPLQ GLEDLAADRI NRLQAALAST
QQFQQMFDEL RTWLDDKQSQ QAKNCPISAK LERLQSQLQE NEEFQKSLNQ HSGSYEVIVA
EGESLLLSVP PGEEKRTLQN QLVELKNHWE ELSKKTADRQ SRLKDCMQKA QKYQWHVEDL
VPWIEDCKAK MSELRVTLDP VQLESSLLRS KAMLNEVEKR RSLLEILNSA ADILINSSEA
DEDGIRDEKA GINQNMDAVT EELQAKTGSL EEMTQRLREF QESFKNIEKK VEGAKHQLEI
FDALGSQACS NKNLEKLRAQ QEVLQALEPQ VDYLRNFTQG LVEDAPDGSD ASQLLHQAEV
AQQEFLEVKQ RVNSGCVMME NKLEGIGQFH CRVREMFSQL ADLDDELDGM GAIGRDTDSL
QSQIEDVRLF LNKIHVLKLD IEASEAECRH MLEEEGTLDL LGLKRELEAL NKQCGKLTER
GKARQEQLEL TLGRVEDFYR KLKGLNDATT AAEEAEALQW VVGTEVEIIN QQLADFKMFQ
KEQVDPLQMK LQQVNGLGQG LIQSAGKDCD VQGLEHDMEE INARWNTLNK KVAQRIAQLQ
EALLHCGKFQ DALEPLLSWL ADTEELIANQ KPPSAEYKVV KAQIQEQKLL QRLLDDRKAT
VDMLQAEGGR IAQSAELADR EKITGQLESL ESRWTELLSK AAARQKQLED ILVLAKQFHE
TAEPISDFLS VTEKKLANSE PVGTQTAKIQ QQIIRHKALN EEIVNRKKNV DQAIKNGQAL
LKQTTGEEVL LIQEKLDGIK TRYADITVTS SKALRTLEQA RQLATKFQST YEELTGWLRE
VEEELATSGG QSPTGEQIPQ FQQRQKELKK EVMEHRLVLD TVNEVSRALL ELVPWRAREG
LDKLVSDANE QYKLVSDTIG QRVDEIDAAI QRSQQYEQAA DAELAWVAET KRKLMALGPI
RLEQDQTTAQ LQVQKAFSID IIRHKDSMDE LFSHRSEIFG TCGEEQKTVL QEKTESLIQQ
YEAISLLNSE RYARLERAQV LVNQFWETYE ELSPWIEETR ALIAQLPSPA IDHEQLRQQQ
EEMRQLRESI AEHKPHIDKL LKIGPQLKEL NPEEGEMVEE KYQKAENMYA QIKEEVRQRA
LALDEAVSQS TQITEFHDKI EPMLETLENL SSRLRMPPLI PAEVDKIREC ISDNKSATVE
LEKLQPSFEA LKRRGEELIG RSQGADKDLA AKEIQDKLDQ MVFFWEDIKA RAEEREIKFL
DVLELAEKFW YDMAALLTTI KDTQDIVHDL ESPGIDPSII KQQVEAAETI KEETDGLHEE
LEFIRILGAD LIFACGETEK PEVRKSIDEM NNAWENLNKT WKERLEKLED AMQAAVQYQD
TLQAMFDWLD NTVIKLCTMP PVGTDLNTVK DQLNEMKEFK VEVYQQQIEM EKLNHQGELM
LKKATDETDR DIIREPLTEL KHLWENLGEK IAHRQHKLEG ALLALGQFQH ALEELMSWLT
HTEELLDAQR PISGDPKVIE VELAKHHVLK NDVLAHQATV ETVNKAGNEL LESSAGDDAS
SLRSRLEAMN QCWESVLQKT EEREQQLQST LQQAQGFHSE IEDFLLELTR MESQLSASKP
TGGLPETARE QLDTHMELYS QLKAKEETYN QLLDKGRLML LSRDDSGSGS KTEQSVALLE
QKWHVVSSKM EERKSKLEEA LNLATEFQNS LQEFINWLTL AEQSLNIASP PSLILNTVLS
QIEEHKVFAN EVNAHRDQII ELDQTGNQLK FLSQKQDVVL IKNLLVSVQS RWEKVVQRSI
ERGRSLDDAR KRAKQFHEAW KKLIDWLEDA ESHLDSELEI SNDPDKIKLQ LSKHKEFQKT
LGGKQPVYDT TIRTGRALKE KTLLPEDSQK LDNFLGEVRD KWDTVCGKSV ERQHKLEEAL
LFSGQFMDAL QALVDWLYKV EPQLAEDQPV HGDLDLVMNL MDAHKVFQKE LGKRTGTVQV
LKRSGRELIE NSRDDTTWVK GQLQELSTRW DTVCKLSVSK QSRLEQALKQ AEVFRDTVHM
LLEWLSEAEQ TLRFRGALPD DTEALQSLID THKEFMKKVE EKRVDVNSAV AMGEVILAVC
HPDCITTIKH WITIIRARFE EVLTWAKQHQ QRLETALSEL VANAELLEEL LAWIQWAETT
LIQRDQEPIP QNIDRVKALI AEHQTFMEEM TRKQPDVDRV TKTYKRKNIE PTHAPFIEKS
RSGGRKSLSQ PTPPPMPILS QSEAKNPRIN QLSARWQQVW LLALERQRKL NDALDRLEEL
KEFANFDFDV WRKKYMRWMN HKKSRVMDFF RRIDKDQDGK ITRQEFIDGI LASKFPTTKL
EMTAVADIFD RDGDGYIDYY EFVAALHPNK DAYRPTTDAD KIEDEVTRQV AQCKCAKRFQ
VEQIGENKYR FGDSQQLRLV RILRSTVMVR VGGGWMALDE FLVKNDPCRA RGRTNIELRE
KFILPEGASQ GMTPFRSRGR RSKPSSRAAS PTRSSSSASQ SNHSCTSMPS SPATPASGTK
VIPSSGSKLK RPTPTFHSSR TSLAGDTSNS SSPASTGAKT NRADPKKSAS RPGSRAGSRA
GSRASSRRGS DASDFDLLET QSACSDTSES SAAGGQGNSR RGLNKPSKIP TMSKKTTTAS
PRTPGPKR
