NEXN_MOUSE
ID NEXN_MOUSE Reviewed; 607 AA.
AC Q7TPW1; E9QJX5; Q3TQP3; Q3UWU2; Q3UWU6; Q3UX39;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Nexilin;
DE AltName: Full=F-actin-binding protein;
GN Name=Nexn {ECO:0000312|MGI:MGI:1916060};
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 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 [2] {ECO:0000312|EMBL:AAH52878.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH52878.1};
RC TISSUE=Egg {ECO:0000312|EMBL:AAH52878.1};
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 [3] {ECO:0000305, ECO:0000312|EMBL:BAE22822.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-314 AND 386-607.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE22822.1};
RC TISSUE=Egg {ECO:0000312|EMBL:BAE22822.1};
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-281; SER-288 AND
RP SER-495, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, 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).
CC -!- FUNCTION: Involved in regulating cell migration through association
CC with the actin cytoskeleton. Has an essential role in the maintenance
CC of Z line and sarcomere integrity. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with F-actin. {ECO:0000250|UniProtKB:Q0ZGT2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q0ZGT2, ECO:0000250|UniProtKB:Q9Z2J4}. Cell
CC junction, adherens junction {ECO:0000250|UniProtKB:Q0ZGT2,
CC ECO:0000250|UniProtKB:Q9Z2J4}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000250|UniProtKB:Q9Z2J4}. Note=Localizes to the cell-matrix AJ.
CC Not found at the cell-cell AJ. {ECO:0000250|UniProtKB:Q0ZGT2,
CC ECO:0000250|UniProtKB:Q9Z2J4}.
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DR EMBL; AC123075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052878; AAH52878.1; -; mRNA.
DR EMBL; AK135919; BAE22724.1; -; mRNA.
DR EMBL; AK136097; BAE22818.1; -; mRNA.
DR EMBL; AK136102; BAE22822.1; -; mRNA.
DR EMBL; AK163414; BAE37339.1; -; mRNA.
DR CCDS; CCDS38673.1; -.
DR RefSeq; NP_955759.2; NM_199465.2.
DR RefSeq; XP_006502061.1; XM_006501998.3.
DR AlphaFoldDB; Q7TPW1; -.
DR SMR; Q7TPW1; -.
DR BioGRID; 213062; 3.
DR IntAct; Q7TPW1; 1.
DR MINT; Q7TPW1; -.
DR STRING; 10090.ENSMUSP00000037120; -.
DR iPTMnet; Q7TPW1; -.
DR PhosphoSitePlus; Q7TPW1; -.
DR jPOST; Q7TPW1; -.
DR MaxQB; Q7TPW1; -.
DR PaxDb; Q7TPW1; -.
DR PRIDE; Q7TPW1; -.
DR ProteomicsDB; 287487; -.
DR Antibodypedia; 2776; 75 antibodies from 16 providers.
DR DNASU; 68810; -.
DR Ensembl; ENSMUST00000046045; ENSMUSP00000037120; ENSMUSG00000039103.
DR GeneID; 68810; -.
DR KEGG; mmu:68810; -.
DR UCSC; uc008rtb.2; mouse.
DR CTD; 91624; -.
DR MGI; MGI:1916060; Nexn.
DR VEuPathDB; HostDB:ENSMUSG00000039103; -.
DR eggNOG; ENOG502QU7W; Eukaryota.
DR GeneTree; ENSGT00730000111176; -.
DR InParanoid; Q7TPW1; -.
DR TreeFam; TF328960; -.
DR BioGRID-ORCS; 68810; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Nexn; mouse.
DR PRO; PR:Q7TPW1; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q7TPW1; protein.
DR Bgee; ENSMUSG00000039103; Expressed in animal zygote and 175 other tissues.
DR ExpressionAtlas; Q7TPW1; baseline and differential.
DR Genevisible; Q7TPW1; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0030055; C:cell-substrate junction; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0030018; C:Z disc; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0008307; F:structural constituent of muscle; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR043204; Basigin-like.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR PANTHER; PTHR10075; PTHR10075; 1.
DR Pfam; PF07679; I-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cell junction; Cytoplasm; Cytoskeleton;
KW Immunoglobulin domain; Phosphoprotein; Reference proteome.
FT CHAIN 1..607
FT /note="Nexilin"
FT /id="PRO_0000302086"
FT DOMAIN 513..601
FT /note="Ig-like"
FT /evidence="ECO:0000255"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0ZGT2"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0ZGT2"
FT MOD_RES 301
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q0ZGT2"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2J4"
FT MOD_RES 502
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2J4"
FT CONFLICT 123
FT /note="D -> N (in Ref. 2; AAH52878)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="I -> L (in Ref. 2; AAH52878)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="A -> T (in Ref. 2; AAH52878)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 72108 MW; AFD6488C345F28E5 CRC64;
MNDVSQKAEI KEMLASDDEE ESSPKIEKAY VPKLTGTVKG KFDEMEKHRQ EEQRKRTEEE
RKRRIEQDLL EKRKIQRELA KRAEQIEDIN NTGTESASEE GDDSLLITVV PAKSYKTPGK
TKDPEDLDRE EGNGRTNHEE DKMRYEEECR VLKEAKCLSL VMDDETEAKK ESHFPGKLKS
TFEELERQRQ ENRKKQAEEE ARRRLEEERR SFEEARRHMV NEEDENQDRE TVFKEYRPGK
LKLSFEEIER QRREDEKRKA EEEARRRIEE EKAAFAEARR SMVLDDDSPE IYKTVSQESL
TPGKLEINFE QLLRQKMEEE RRRTEEERRH KLEMEKQEFE QLRQEMGKEE EENESFGLSR
EYEELIKLKR SGSIQAKNLK SKFEKIGQLS EKEVQKKIEE ERAKRRAIDL EIKEREAENF
HEDDDVDVRP AKKSESPFTH KVNMKARFEQ MAKAREEEEQ RRIEEQKLLR MQFEQKEIDA
ALQKKREDEE EEEGSIVNGS TTEDEEQTRS GAPWFKKPLR NTSVVDSEPV RFTVKVTGEP
KPEITWWFEG EILQDGEDYQ YIERGETYCL YLPETFPEDG GEYMCKAVNN KGSAASTCIL
TIEMDDY
