SYNE2_MOUSE
ID SYNE2_MOUSE Reviewed; 6874 AA.
AC Q6ZWQ0; Q640M5;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Nesprin-2 {ECO:0000305};
DE AltName: Full=KASH domain-containing protein 2;
DE Short=KASH2;
DE AltName: Full=Nuclear envelope spectrin repeat protein 2;
DE AltName: Full=Nucleus and actin connecting element protein;
DE Short=Protein NUANCE;
DE AltName: Full=Synaptic nuclear envelope protein 2;
DE Short=Syne-2;
GN Name=Syne2 {ECO:0000312|MGI:MGI:2449316};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=18477613; DOI=10.1242/jcs.019075;
RA Luke Y., Zaim H., Karakesisoglou I., Jaeger V.M., Sellin L., Lu W.,
RA Schneider M., Neumann S., Beijer A., Munck M., Padmakumar V.C., Gloy J.,
RA Walz G., Noegel A.A.;
RT "Nesprin-2 Giant (NUANCE) maintains nuclear envelope architecture and
RT composition in skin.";
RL J. Cell Sci. 121:1887-1898(2008).
RN [5]
RP SUBCELLULAR LOCATION, INTERACTION WITH TMEM67, AND FUNCTION.
RX PubMed=19596800; DOI=10.1242/jcs.043794;
RA Dawe H.R., Adams M., Wheway G., Szymanska K., Logan C.V., Noegel A.A.,
RA Gull K., Johnson C.A.;
RT "Nesprin-2 interacts with meckelin and mediates ciliogenesis via
RT remodelling of the actin cytoskeleton.";
RL J. Cell Sci. 122:2716-2726(2009).
RN [6]
RP FUNCTION, AND SUBUNIT.
RX PubMed=19874786; DOI=10.1016/j.neuron.2009.08.018;
RA Zhang X., Lei K., Yuan X., Wu X., Zhuang Y., Xu T., Xu R., Han M.;
RT "SUN1/2 and Syne/Nesprin-1/2 complexes connect centrosome to the nucleus
RT during neurogenesis and neuronal migration in mice.";
RL Neuron 64:173-187(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4096; SER-6371; SER-6400;
RP SER-6417; SER-6418 AND SER-6419, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, INTERACTION WITH F-ACTIN, AND MUTAGENESIS OF ILE-128 AND ILE-131.
RX PubMed=20724637; DOI=10.1126/science.1189072;
RA Luxton G.W., Gomes E.R., Folker E.S., Vintinner E., Gundersen G.G.;
RT "Linear arrays of nuclear envelope proteins harness retrograde actin flow
RT for nuclear movement.";
RL Science 329:956-959(2010).
RN [9]
RP FUNCTION, AND SUBUNIT.
RX PubMed=21177258; DOI=10.1093/hmg/ddq549;
RA Yu J., Lei K., Zhou M., Craft C.M., Xu G., Xu T., Zhuang Y., Xu R., Han M.;
RT "KASH protein Syne-2/Nesprin-2 and SUN proteins SUN1/2 mediate nuclear
RT migration during mammalian retinal development.";
RL Hum. Mol. Genet. 20:1061-1073(2011).
RN [10]
RP FUNCTION, AND SUBUNIT.
RX PubMed=23071752; DOI=10.1371/journal.pone.0047180;
RA Razafsky D., Blecher N., Markov A., Stewart-Hutchinson P.J., Hodzic D.;
RT "LINC complexes mediate the positioning of cone photoreceptor nuclei in
RT mouse retina.";
RL PLoS ONE 7:E47180-E47180(2012).
CC -!- FUNCTION: Multi-isomeric modular protein which forms a linking network
CC between organelles and the actin cytoskeleton to maintain the
CC subcellular spatial organization. As a component of the LINC (LInker of
CC Nucleoskeleton and Cytoskeleton) complex involved in the connection
CC between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic
CC interactions established by the LINC complex play an important role in
CC the transmission of mechanical forces across the nuclear envelope and
CC in nuclear movement and positioning. Specifically, SYNE2 and SUN2
CC assemble in arrays of transmembrane actin-associated nuclear (TAN)
CC lines which are bound to F-actin cables and couple the nucleus to
CC retrograde actin flow during actin-dependent nuclear movement. May be
CC involved in nucleus-centrosome attachment. During interkinetic nuclear
CC migration (INM) at G2 phase and nuclear migration in neural progenitors
CC its LINC complex association with SUN1/2 and probable association with
CC cytoplasmic dynein-dynactin motor complexes functions to pull the
CC nucleus toward the centrosome; SYNE1 and SYNE2 seem to act redundantly
CC in cerebellum, midbrain, brain stem, and other brain regions except
CC cerebral cortex and hippocampus. During INM at G1 phase mediates
CC respective LINC complex association with kinesin to push the nucleus
CC away from the centrosome. Involved in nuclear migration in retinal
CC photoreceptor progenitors. Required for centrosome migration to the
CC apical cell surface during early ciliogenesis.
CC {ECO:0000250|UniProtKB:Q8WXH0, ECO:0000269|PubMed:18477613,
CC ECO:0000269|PubMed:19596800, ECO:0000269|PubMed:19874786,
CC ECO:0000269|PubMed:20724637, ECO:0000269|PubMed:21177258,
CC ECO:0000269|PubMed:23071752}.
CC -!- SUBUNIT: Core component of LINC complexes which are composed of inner
CC nuclear membrane SUN domain-containing proteins coupled to outer
CC nuclear membrane KASH domain-containing nesprins. SUN and KASH domain-
CC containing proteins seem to bind each other promiscuously; however,
CC some LINC complex constituents are tissue- or cell type-specific. At
CC least SUN1/2-containing core LINC complexes are proposed to be
CC hexameric composed of three protomers of each KASH and SUN domain-
CC containing protein. The SUN2:SYNE2/KASH2 complex is a heterohexamer;
CC the homotrimeric cloverleave-like conformation of the SUN domain is a
CC prerequisite for LINC complex formation in which three separate
CC SYNE2/KASH2 peptides bind at the interface of adjacent SUN domains.
CC Interacts with EMD, LMNA, MKS3 and F-actin via its N-terminal domain.
CC Interacts with DCTN1 and DYNC1I1/2; suggesting the association with the
CC dynein-dynactin motor complex. Associates with kinesin motor complexes.
CC Interacts with TMEM67. Interacts (via KASH domain) with TMEM258 (By
CC similarity). {ECO:0000250|UniProtKB:Q8WXH0,
CC ECO:0000269|PubMed:19596800, ECO:0000269|PubMed:19874786,
CC ECO:0000269|PubMed:20724637, ECO:0000269|PubMed:21177258,
CC ECO:0000269|PubMed:23071752}.
CC -!- INTERACTION:
CC Q6ZWQ0-1; Q8BJS4-3: Sun2; NbExp=2; IntAct=EBI-16108623, EBI-16189250;
CC Q6ZWQ0-1; Q9Y613: FHOD1; Xeno; NbExp=2; IntAct=EBI-16108623, EBI-348433;
CC -!- SUBCELLULAR LOCATION: Nucleus outer membrane; Single-pass type IV
CC membrane protein; Cytoplasmic side. Sarcoplasmic reticulum membrane
CC {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Cell
CC membrane; Single-pass membrane protein. Cytoplasm, cytoskeleton.
CC Mitochondrion {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}.
CC Note=Different isoform patterns are found in the different compartments
CC of the cell. The isoforms having the C-terminal transmembrane span can
CC be found in several organellar membranes like the nuclear envelope, the
CC sarcoplasmic reticulum of myoblasts, or the lamellipodia and focal
CC adhesions at the cell membrane. The largest part of the outer nuclear
CC membrane-associated protein is cytoplasmic, while its C-terminal part
CC is associated with the nuclear envelope, most probably the outer
CC nuclear membrane. Remains associated with the nuclear envelope during
CC its breakdown in mitotic cells. Shorter soluble isoforms can be found
CC in the cytoplasm and within the nucleus (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Nesprin-2 Giant, Nesp2G, NUANCE;
CC IsoId=Q6ZWQ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZWQ0-2; Sequence=VSP_038800, VSP_038801;
CC Name=3;
CC IsoId=Q6ZWQ0-3; Sequence=VSP_038799, VSP_038802;
CC -!- TISSUE SPECIFICITY: C-terminal isoforms are highly expressed in the
CC brain, hert and skeletal muscle. Isoform 1 (Nesprin-2 Giant) is most
CC prevalent in the brain, skin, kidney and skeletal muscle.
CC {ECO:0000269|PubMed:18477613}.
CC -!- DOMAIN: The KASH domain, which contains a transmembrane domain,
CC mediates the nuclear envelope targeting and is involved in the binding
CC to SUN1 and SUN2 through recognition of their SUN domains.
CC {ECO:0000250}.
CC -!- PTM: The disulfid bond with SUN2 is required for stability of the
CC SUN2:SYNE2/KASH2 LINC complex under tensile forces though not required
CC for the interaction. {ECO:0000250|UniProtKB:Q8WXH0}.
CC -!- SIMILARITY: Belongs to the nesprin family. {ECO:0000305}.
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DR EMBL; AK052521; BAC35023.1; -; mRNA.
DR EMBL; AC115714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC164121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC166991; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC082586; AAH82586.1; -; mRNA.
DR CCDS; CCDS49091.1; -. [Q6ZWQ0-1]
DR RefSeq; NP_001005510.2; NM_001005510.2. [Q6ZWQ0-1]
DR SMR; Q6ZWQ0; -.
DR BioGRID; 235364; 56.
DR DIP; DIP-61049N; -.
DR IntAct; Q6ZWQ0; 9.
DR MINT; Q6ZWQ0; -.
DR STRING; 10090.ENSMUSP00000047697; -.
DR iPTMnet; Q6ZWQ0; -.
DR PhosphoSitePlus; Q6ZWQ0; -.
DR EPD; Q6ZWQ0; -.
DR jPOST; Q6ZWQ0; -.
DR MaxQB; Q6ZWQ0; -.
DR PaxDb; Q6ZWQ0; -.
DR PeptideAtlas; Q6ZWQ0; -.
DR PRIDE; Q6ZWQ0; -.
DR ProteomicsDB; 254736; -. [Q6ZWQ0-1]
DR ProteomicsDB; 254737; -. [Q6ZWQ0-2]
DR ProteomicsDB; 254738; -. [Q6ZWQ0-3]
DR Antibodypedia; 189; 189 antibodies from 23 providers.
DR Ensembl; ENSMUST00000044217; ENSMUSP00000047697; ENSMUSG00000063450. [Q6ZWQ0-1]
DR GeneID; 319565; -.
DR KEGG; mmu:319565; -.
DR UCSC; uc007nxm.1; mouse. [Q6ZWQ0-2]
DR UCSC; uc007nxp.1; mouse. [Q6ZWQ0-1]
DR UCSC; uc007nxs.1; mouse. [Q6ZWQ0-3]
DR CTD; 23224; -.
DR MGI; MGI:2449316; Syne2.
DR VEuPathDB; HostDB:ENSMUSG00000063450; -.
DR eggNOG; KOG0516; Eukaryota.
DR GeneTree; ENSGT00940000154656; -.
DR InParanoid; Q6ZWQ0; -.
DR OMA; AEHGKYQ; -.
DR OrthoDB; 47at2759; -.
DR PhylomeDB; Q6ZWQ0; -.
DR TreeFam; TF329280; -.
DR BioGRID-ORCS; 319565; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Syne2; mouse.
DR PRO; PR:Q6ZWQ0; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q6ZWQ0; protein.
DR Bgee; ENSMUSG00000063450; Expressed in ventricular zone and 259 other tissues.
DR ExpressionAtlas; Q6ZWQ0; baseline and differential.
DR Genevisible; Q6ZWQ0; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031527; C:filopodium membrane; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0031258; C:lamellipodium membrane; ISO:MGI.
DR GO; GO:0034993; C:meiotic nuclear membrane microtubule tethering complex; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0030016; C:myofibril; IDA:MGI.
DR GO; GO:0005635; C:nuclear envelope; IDA:WormBase.
DR GO; GO:0031981; C:nuclear lumen; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; IDA:MGI.
DR GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISO:MGI.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0140444; F:cytoskeleton-nuclear membrane anchor activity; ISO:MGI.
DR GO; GO:0051642; P:centrosome localization; IMP:UniProtKB.
DR GO; GO:0007097; P:nuclear migration; ISO:MGI.
DR GO; GO:0031022; P:nuclear migration along microfilament; IMP:UniProtKB.
DR GO; GO:0021817; P:nucleokinesis involved in cell motility in cerebral cortex radial glia guided migration; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:1902017; P:regulation of cilium assembly; IMP:UniProtKB.
DR CDD; cd00014; CH; 2.
DR CDD; cd00176; SPEC; 4.
DR Gene3D; 1.10.418.10; -; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR012315; KASH.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR InterPro; IPR030266; SYNE2.
DR PANTHER; PTHR47535:SF6; PTHR47535:SF6; 1.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF10541; KASH; 1.
DR Pfam; PF00435; Spectrin; 2.
DR SMART; SM00033; CH; 2.
DR SMART; SM01249; KASH; 1.
DR SMART; SM00150; SPEC; 17.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS51049; KASH; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoskeleton; Disulfide bond; Membrane; Mitochondrion; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Sarcoplasmic reticulum;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..6874
FT /note="Nesprin-2"
FT /id="PRO_0000392210"
FT TOPO_DOM 1..6823
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT TRANSMEM 6824..6844
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT TOPO_DOM 6845..6874
FT /note="Perinuclear space"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT DOMAIN 31..136
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 183..288
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 299..380
FT /note="Spectrin 1"
FT REPEAT 381..474
FT /note="Spectrin 2"
FT REPEAT 475..577
FT /note="Spectrin 3"
FT REPEAT 578..680
FT /note="Spectrin 4"
FT REPEAT 727..834
FT /note="Spectrin 5"
FT REPEAT 835..928
FT /note="Spectrin 6"
FT REPEAT 929..1030
FT /note="Spectrin 7"
FT REPEAT 1120..1211
FT /note="Spectrin 8"
FT REPEAT 1262..1322
FT /note="Spectrin 9"
FT REPEAT 1323..1409
FT /note="Spectrin 10"
FT REPEAT 1410..1514
FT /note="Spectrin 11"
FT REPEAT 1515..1626
FT /note="Spectrin 12"
FT REPEAT 1627..1728
FT /note="Spectrin 13"
FT REPEAT 1729..1820
FT /note="Spectrin 14"
FT REPEAT 1821..1928
FT /note="Spectrin 15"
FT REPEAT 1929..2026
FT /note="Spectrin 16"
FT REPEAT 2027..2122
FT /note="Spectrin 17"
FT REPEAT 2123..2233
FT /note="Spectrin 18"
FT REPEAT 2234..2350
FT /note="Spectrin 19"
FT REPEAT 2422..2503
FT /note="Spectrin 20"
FT REPEAT 2504..2610
FT /note="Spectrin 21"
FT REPEAT 2611..2707
FT /note="Spectrin 22"
FT REPEAT 2708..2821
FT /note="Spectrin 23"
FT REPEAT 2822..2923
FT /note="Spectrin 24"
FT REPEAT 2924..3027
FT /note="Spectrin 25"
FT REPEAT 3028..3133
FT /note="Spectrin 26"
FT REPEAT 3134..3239
FT /note="Spectrin 27"
FT REPEAT 3240..3343
FT /note="Spectrin 28"
FT REPEAT 3344..3456
FT /note="Spectrin 29"
FT REPEAT 3457..3563
FT /note="Spectrin 30"
FT REPEAT 3564..3669
FT /note="Spectrin 31"
FT REPEAT 3670..3767
FT /note="Spectrin 32"
FT REPEAT 3768..3870
FT /note="Spectrin 33"
FT REPEAT 3871..3976
FT /note="Spectrin 34"
FT REPEAT 3977..4074
FT /note="Spectrin 35"
FT REPEAT 4218..4337
FT /note="Spectrin 36"
FT REPEAT 4507..4626
FT /note="Spectrin 37"
FT REPEAT 4627..4714
FT /note="Spectrin 38"
FT REPEAT 4715..4823
FT /note="Spectrin 39"
FT REPEAT 4824..4929
FT /note="Spectrin 40"
FT REPEAT 4930..5037
FT /note="Spectrin 41"
FT REPEAT 5038..5150
FT /note="Spectrin 42"
FT REPEAT 5151..5252
FT /note="Spectrin 43"
FT REPEAT 5253..5377
FT /note="Spectrin 44"
FT REPEAT 5378..5473
FT /note="Spectrin 45"
FT REPEAT 5474..5576
FT /note="Spectrin 46"
FT REPEAT 5577..5691
FT /note="Spectrin 47"
FT REPEAT 5692..5786
FT /note="Spectrin 48"
FT REPEAT 5787..5894
FT /note="Spectrin 49"
FT REPEAT 5895..6004
FT /note="Spectrin 50"
FT REPEAT 6005..6122
FT /note="Spectrin 51"
FT REPEAT 6123..6230
FT /note="Spectrin 52"
FT REPEAT 6231..6342
FT /note="Spectrin 53"
FT REPEAT 6450..6534
FT /note="Spectrin 54"
FT REPEAT 6535..6650
FT /note="Spectrin 55"
FT REPEAT 6651..6767
FT /note="Spectrin 56"
FT DOMAIN 6815..6874
FT /note="KASH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00385"
FT REGION 1..286
FT /note="Actin-binding"
FT REGION 675..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2338..2397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4062..4152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4171..4193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4326..4348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4401..4429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 5435..5459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 6336..6473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 6790..6812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 6861..6874
FT /note="Sufficient for interaction with SUN2"
FT /evidence="ECO:0000250|UniProtKB:Q8WXH0"
FT COILED 299..6767
FT /evidence="ECO:0000255"
FT COMPBIAS 679..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..723
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4106..4122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4329..4343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 6336..6375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 6414..6428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 6446..6465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4096
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 5772
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXH0"
FT MOD_RES 6348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXH0"
FT MOD_RES 6371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 6400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 6417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 6418
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 6419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 6448
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXH0"
FT DISULFID 6851
FT /note="Interchain (with C-577 in SUN2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8WXH0"
FT DISULFID 6851
FT /note="Interchain (with C-759 in SUN1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8WXH0"
FT VAR_SEQ 1..4994
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038799"
FT VAR_SEQ 472..482
FT /note="INNVLGKNFIP -> FVIVPVHKLCE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_038800"
FT VAR_SEQ 483..6874
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_038801"
FT VAR_SEQ 6781..6789
FT /note="SPRPRWTFL -> FGV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038802"
FT MUTAGEN 128
FT /note="I->A: Impairs interaction with F-actin; when
FT assocoated with A-131."
FT /evidence="ECO:0000269|PubMed:20724637"
FT MUTAGEN 131
FT /note="I->A: Impairs interaction with F-actin; when
FT assocoated with A-128."
FT /evidence="ECO:0000269|PubMed:20724637"
SQ SEQUENCE 6874 AA; 782725 MW; 379792E42B95B7DB CRC64;
MAASPVLPTE DGEGFLGIDD LHFSLQAEQE DTQKKTFTCW INSQLAKHTP PSVVSDLFAD
IKKGHVLLDL LEVLSGQQLP RDKGSNTFQC RINIEHALTF LKNRSIKLIN IHVADIVEGN
PSIILGLIWT IILHFHIEKL AQTLSCDYNQ PSPEVVSVAA SSPTSSPPTK KCSKAQAQAR
WQWSAKKALL QWAQEQCARS ESVNVTDFKS SWRNGMAFLA VIHALRPDLI DMDSMRHRSN
KDNLKEAFRI AEHELKIPKL LEPEDVDVVN PDEKSIMTYV AQFLKYSKDA PGPGDSTQAK
VRDALVWLTL QEKRFQKMLK DSASETYCNK YHSLLSFMES LNEEKESFID VLSLKGRMGE
LNEDESRLRQ GWTSLMHQVA AWRAQLDDAL PSPLKETEAW LKDIEGVVQE GVPTSQSYSE
ARTLIQGKLS SFKSLMGSFD YHSDVLMAFQ SNAEKSLPAV PPVKLEEMTR RINNVLGKNF
IPLLEFHDSK CSVLALLDEA KAKLDVWNGT YESKESVEVL LEDWHKFTGE KKFLIQLDAS
FQKCEEMYKN SARECESIRE EYMMLEKNVH SCRQYIHNTK ATLQRALMSW ATFEEDLALL
KASFDLTKKE QIKEVPVETL LQWNTKHTSL NEVGSFLIGV SSREVAASIS KELRRLNKRW
RKFITKTPLL KLPLVKIQDQ PPGNSSGTSL SKESAMAAEP GGSRGEDVKA AEKQEVEDEE
SAGQLKVNEE VEGLIKQVTI WESQTKSILD LLQHGDHADG SSADTLQHLI AKGSVYEELL
ARTEDTLQMD VQSPSNLEPF QNVLRAGLQA KIQEAKQGVQ ITMVELSAVL KNLSDEPLEL
DLGLKVEEAQ KELEVSILRA EQLLGQRERP GGFLLKYKEA LEILNTNSLA KYLRAVEELK
RTVPGGAKLQ LEEQSRVASA KWEPLRHEIS LYLQQLKIAI EEEKLRDNIA RLEKQINKEK
KLIRRGRTRG LRKEHEACLS PESIKCQLEH HVGVLRVLCE ELTSPEDQQE LKRALRDYEQ
KIARLLKCAS EIHTTLQSSQ GGALEERSAL ITTENGRRDA DGEVPLEIPD NQLSTEKAME
PIKNFSQTSE LKPQQEESIM EKEGKDCSAS LSDLQERYDT QRGLLEQHLQ DSKSRVTSDF
ASEQERSSAC LQSKLAELQV LLADTDAHWE KFEITSLNLR RLMSDAEKPV LNQERDLLKG
NEQVLHGLLN TRMESLEMAL QIVLPLEKEC SLLCASDLPL CTVAVQDLHP VEIDGVYQNL
RDIRDSIAKQ IRVCTSLEEP SNSVPRELHT LDQCAIQDIV LKCRLQLETM NQKVEMREDA
LDALEGFLAS LRAAKLSAEL PADRPAPKAP EVLSEDILLM KEKAGPLDER LRTLGINIKD
AEGGENTTCE RLVGALSVNL VAMDGQSKEE GPPEDKKLLE ACSSKNLELF KNIQDLQNQI
SKIGLKDPTA PAVKHRKKSL LRLDKDLDGL EEEKVRIQKI AGSLPRFKDG SEKNVIQQCE
DTAALWESTK ASVTESLEQC GSALELLRQY QNIKNNLTAL IQKEEGIISQ QASYMGKDNL
KKKIAEIETV KEEFSDHLEV VDKINQICKN LQYHLNKMKT FEDPPFEKEA NAIVDRWLDI
NEKTEEYGEN LGRALALWDK LFIIKNNIDE WTEQILGKAE SHELTEEDRG RLKEELKVLE
EQSAEFSRRV ADIQSLLQSN EKPLELQVME SSVLSKMKDV KTHVAGGSNS YAPSGSTAEL
REDLDQAKTQ MGMTESLLNA LSPSDSLEIF TKLEEIQQQI FQQKHSMTVL ENQIGCLTPE
LSELKRQYAS VSNLFNTKKN ALQDHFATFL NEQCKNFNDW FSNVKTNLQE CFEPPETKLS
LEQRLQKLSD FLTLGGGNSK IQQVETVLQH VKMLLPKAHV KELDSWLRSQ ELELENMESI
CQARAGELNN SFQQLLRLED DCRSLSKWLT NQEENWGKME VSGERMDLFS QALTRKREQF
ETVAQLSDSL KEHGLTEGEE TIKESTHLID RYQALWRQLH EIEEEDKLPA AEDQSFNDLA
DDVIHWIKEI KESLMALNSS EGKMPLEERI QKIKEIIALK PEGDAKIQMV MRQAEHCEAP
LAQETFTDLS NQWDSTLHLA NTYLSHQEKL VLEGEKYLQS KEDLRLMLTE LKKQQEAGFA
LQPGLPEKQA QLKIYKKFLQ KAQDLTSLLE ELKSQGNYLL ECTKNPSFSE EPWLEVKHLH
ESLLQQLQDS VQKLEGHVQE HSSYQVCLTD LSSTLDDISK EYFSLCDGSK DQIMAKERMQ
KLQELESRLR FQGGALKKAS ALAKSIKQNT SSVGQKIIKD DIRSLKYKQK DLENRIESAK
QETENGLNSI LKSKSSTEKH VKFSLPVEEM PATSEVPKPT RESAAVGESG GARETNTNSA
VEMILSKQLS LNVQESMQNA QDEREVNELQ NQPLELDIML RNEQLKGMEE LSTHLEARRA
AIELLEQSQH LNQTEEQALV LPAARPSVCH LGSLQQELHT LKKTKERQYG LLSGFQDQLV
MAEASLNTSL AEVESLKIGS LDSATYLGKI KKFLGSVENQ QGSLSKLRTE WAHLSSLLAA
ADQKLVESQM KHLEHGWELV EQLAHRKCFQ QATEHSELTC LLEKLQDLKV SLHQQQQRLT
LSLNSPGQQA AIVDMVTPAA ELQAIKCEFS GLKWQAELHM KRLWGEKDKK TLEDAINNLN
KQMEALEPLN REVENRIKKC ELQNRIKETL SWVKNTMAEL VVPIALLPDN ILSQIRKCKL
IHDGILGNQQ AVELLVEEVR GITPSLAPCE GDGLNALLED LQSQHQALLL KSTERSQQLE
LKLEEKSKLF AIIGKVQLTL EESETLMSPT GDRASTEAEL ERRLAILKAS QQQLQDTESA
LSAHLQELTN AYKDANVFER LFLDDQLKNL KARTNRTQRF LQNNGSELKQ KMESYREFHD
KAAVLQKEAE CILHGGLLPL RQELEQDAKE QLGNLRDKLA AIRGSLSQVL TSEEVFDTIG
LSWDGSLLAR LQTQVLERER EVEGKIKQLD TFLIARDRHQ ASISKIRAVD LQIKKGAESL
LKVPSMSPES TLLNAQTLIQ KIEKSKRLRD EIIRKLSKNE AFDDSFKESE MQRLKLCAEE
NSRLQEALQN MLLELQPREM GEKEFREKLE NALHVLKQIQ SRLQQPLCVN LGVQHIQHEK
ETWEAFGEQV EAEMCGLRAV RITEEQREEN DSGTGGMEAK LRDIEGLHME LSKSISLRAD
VLNDAYDSAN RYDELVAGAL RIITSLEATL LSYRVDLHNP QKTLELAHLK QEELQSSVAD
LRSLTETLGA ISSPEAKEQL RCTLEVLAAK NSALKAGLEA QEAEEERCLE NYKCFRKMKE
EICSRLRKME MDLGQSIFPL PRSYKEALAR LEQSKALTSN LLSTKEDLVK LRQLLRHLRC
RSTENDATCA LGVASALWEK WLSLLEAARE WQQWGGELKR EWKFISEEIE REAIILETLQ
EDLPEISKTN AAPTEELWQL LDSLCQHQES VEKQQLLLAL LLQRVRSIQN IPEGTETGET
IPALQEIGSM QERCDRLLHT TRKNKDLVQA EIQAQQSFLK EIKDVKRVFE QISTSFPNLA
PEGHPERAEQ FEELRSILQK GKLSFENIME KLRIKYSEMY SIVPAEIGSQ VEECRSALED
AEEKMSSEVS KSSPSSIMRR KIERINNGLH CVEKMLQQKS RNIEEAHEIQ KKIWDELDLW
HSKLNELDSE VQDFVEQDPG QAQEWMDNLM APFQQHQQVS QRAESRTSQL NKATIKMEEY
NDLLKSTEVW IEKTSCLLAN PACYDSSRTL SHRASTLQMA LEDSEQKHSL LHSIFTDLED
LSIIFETDDL IQTIHELSDQ VAALQQQIME ALPHVQQVAD DVVAIESEVK AMEKKVAKIK
AILLSKEIFD FPPEEHLKHG EVILENIHPM KKTIAEIMTY QVELRLPQTG TKPLPVFQRT
SQLLQDVKLL ENVTQEQNEL LKVVIKQTAE CDEEIDSLKQ MLTNYSAEIS PEHVSQNQVA
DLPSLQGEME RLEKQILNLN QKKEDLLVDL KTAVLNLHEH LKQEQQEVGD KPSAGASECT
VAERDASERK LSRTNSMSFL PVVKEEAEES SVKSEDGRRR TEPPSASWSF LGKHSKDLEG
DGASSSSSAT IVQDADGRIS TCDSSMVHII APDSGSTEEG PAPSPRLSQT DEGATPPIEA
ALLDFPREQG AFESTVERSR PRPADILRVC KTQVAKLELW LQQANVAFEP ETVDADMQQV
VEEELAGCQA MLTEIEYKVA SLLETCKDQG LGDCGTTQQE AEALSWKLKT VKCNLEKVQM
VLQEKFSEDQ HPSTLKKPSE PHDVDQPAGL SELDSVLTER PQFSRQKDAP QPQILELKPS
EQKDLIKFTE LNAKKTWLQG HQENEDANRQ SASSSKVPSP GNAASDSTLP LQAQSGDKWQ
YLHHELTSRP NPSVPQLVEP QVALTTSTLP SVSVYNFRCP TADELQAYTT QLEELRQEAN
TIQTQGSMTE ETYISLDKRL FELFLSLSRC LGSVEGLLQR PGLLREDACA QQVFFQKLAL
ELKKLYLALG DKKDDFLKAV TWPGKEATLL PECIDALTVS LESVQSRAAW RDASLKAGLE
HSRSYQNEVK RLYSQLIKKK TALQQSLNEI SGQSISKQLQ KADVHTAELQ NSEKQVAKLR
DEGERLRFPH GLLQDVYKLE DVLDSMWGIL RARYLELSSP FLSKSLQTLL QGMAELVSIG
KGKLAADPLQ HAKSKAALQA QLQDHKAFFQ KLVADMLLIQ TYSATMFPPS LQKGEGFGAE
QVAEVRALEE EACLRGAQLQ SMLQKWEEFD DNYASLEKDL EALISSLPSV SLVEETEERL
LERISFYQQI KRNIDGKHAR LCQTLNEGRQ LAASVSCPEP EGQIARLEEQ WLSLNKRIDQ
ELHRLQTLLK HLLSYSRDSD ELTRWLETSQ QTLNYWKEQS LNVSQDLNTI RSNIDRFFKF
SKEVDERSSL KSAVMSTGNQ LLHLKEADTA TLRASLAQFE QKWTVLITQL PDIQEKLHQL
QMEKLPSREA ISEMISWMNA VEPQAAGKDT ELSKSSASQV KHLLQKLKEF RMEMDYKQWV
VDFVNQSLLQ LSTCDVESKR YERTEFAEHL GEMNRQWQRV HGTLNRKIQH LEQLLESITE
NENKVQNLNS WLEAQEERLK MLQKPESAVS MEKLLLDCQD IENQLALKSK ALDELRQSSL
TMDGGDVPLL EDMASGIVEL FQKKNNVTSQ VHQLRASVQS VLQEWKACDK LYDEATMRTT
QLTYSMEHSK PAVLSLQALA CQVQNLEALQ DEAENGERSW EKLQEVIGRL KASCPSMAGI
IEEKCQDAHS RWTQVNQDLA DQLQEARGQL QLWKAPHNAH AEAAAWLQQQ EAKFQQLANT
NLSGDNLADI LPRALKDIKG LQSDLQKTKE AFLENSTLSD QLPQPEERST PGLHSGQRHS
LQTAAYLEKM LLAKSNEFEI VLAQFKDFTD RLAYSKDLIV HKEENLNKLY HEEKEEVPDL
FLNHVLALTA QSPDIERLNE ESLRLPLSDV TIKTLQSLNR QWIRATATAL DHYSELQGNG
LNEKFLHYCE RWIQVLEKIQ ESLSVEVAHS LPALLEQQKT YEILEAEVST NQAVADAYVT
QSLQLLDTAE IEKRPEFVSE FSKLSDQWQR AARGVRQRKC DISRLVTQWR FFTTSVEDLL
RFLADTSQLL SAVKEQDCYS LCQTRRLVHE LKSKEIHLQR WRTTYALALE AGEKLRNTPS
PETREFVDGQ ISRLQESWKD TELSLGEVIS RLQSTAETWD QCKKKIKKLK KRLQALKAQS
EDPLPELHEA LHEEKELIKE VEKSLANWTH SLKELQTMKA DLSQHILAED VTVLKEQIQL
LHRQWEDLCL RVAIRKQEIE DRLNSWIVFN EKNKELCAWL VQMENKVLQT ADVSIEEMIE
KLQKDCMEEI SLFTENKLQL KQMGDQLIKA SSKAKAAELE EKLSKINDRW QHLFDVIGSR
VKKLKETFAF IQQLDKNMSN LRTWLARIES ELSKPVVYDV CDNQEIQKRL AEQQDLQRDI
EQHSAGVESV FNICDVLLHD SDACANETEC DSIQQTTRSL DRRWRNICAM SMERRMKIEE
TWRLWQKFLD DYSRFEDWLK SAERTAACPN SSEVLYTNAK EELKRFEAFQ RQIHERLTQL
ELINKQYRRL ARENRTDTAS KLKQMVHEGN QRWDNLQKRV TAILRRLRYF TNQREEFEGT
RESILVWLTE MDLQLTNVEH FSESDAEDKM RQLNGFQQEI TLNTNKIDQL IVFGEQLIQK
SEPLDAVLIE DELEELHRYC QEVFGRVSRF HRRLTSHTPG LDDEKEASEN ETDIEDPREI
QADSWRKRRE SEEPTSPQSL CHLVPPALGH ERSGCETPVS VDSIPLEWDH TGDVGGSSSH
EDDEEGPFYS ALSGKSISEG HPWHVPDSPS HSKHHYKHME GDRTEAPVPT DASTPFKSDY
VKLLLRQGTD DSKEGLKEAQ QEDEQLATLT GQQPGAFDRW ELIQAQELHS KLRLKQTVQQ
LKSDIGSIAA WLGKTEAELE ALKLAEPPSD IQEIALRVKR LQEILKAFDT YKALMVSVNV
SHKEYLPSQS PEATELQNRL HQLSLSWDSV QGVLDSWRGD LRQSLMQCQD FHQLSQDLLL
WLATAESRRQ KAHVTSPEAD RQVLLECQKD LMRLEKELVA RQPQVSSLRE ISSSLLVKGQ
GEDYIEAEEK VHVIEKKLKQ LQEQVAQDLM SLQRSLDPDA SLTSFDEVDS GEQLPAAFAK
SPRPRWTFLE EEEEEEETDS RMPHLDSPGS SQPRRSFLSR VIRAALPLQL LLLLLLLLAC
LLPASEDDYS CTQANNFARS FYPMLRYTNG PPPT
