NEXN_RAT
ID NEXN_RAT Reviewed; 656 AA.
AC Q9Z2J4; Q9Z2J3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Nexilin;
GN Name=Nexn {ECO:0000312|RGD:708354};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC95128.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH F-ACTIN,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9832551; DOI=10.1083/jcb.143.5.1227;
RA Ohtsuka T., Nakanishi H., Ikeda W., Satoh A., Momose Y., Nishioka H.,
RA Takai Y.;
RT "Nexilin: a novel actin filament-binding protein localized at cell-matrix
RT adherens junction.";
RL J. Cell Biol. 143:1227-1238(1998).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=19881492; DOI=10.1038/nm.2037;
RA Hassel D., Dahme T., Erdmann J., Meder B., Huge A., Stoll M., Just S.,
RA Hess A., Ehlermann P., Weichenhan D., Grimmler M., Liptau H., Hetzer R.,
RA Regitz-Zagrosek V., Fischer C., Nurnberg P., Schunkert H., Katus H.A.,
RA Rottbauer W.;
RT "Nexilin mutations destabilize cardiac Z-disks and lead to dilated
RT cardiomyopathy.";
RL Nat. Med. 15:1281-1288(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-330; SER-337;
RP SER-345; SER-544; SER-549 AND THR-551, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: 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:0000269|PubMed:9832551}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:9832551}. Cell junction, adherens junction
CC {ECO:0000269|PubMed:9832551}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000269|PubMed:19881492}. Note=Localizes to the cell-matrix AJ
CC (PubMed:9832551). Not found at the cell-cell AJ (PubMed:9832551).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:9832551}; Synonyms=b-Nexilin
CC {ECO:0000269|PubMed:9832551};
CC IsoId=Q9Z2J4-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:9832551}; Synonyms=s-Nexilin
CC {ECO:0000269|PubMed:9832551};
CC IsoId=Q9Z2J4-2; Sequence=VSP_052528, VSP_052529;
CC -!- TISSUE SPECIFICITY: Expressed in brain, testis, spleen and fibroblasts
CC (at protein level). Not detected in liver, kidney or epithelial cells
CC (at protein level). {ECO:0000269|PubMed:9832551}.
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DR EMBL; AF056034; AAC95128.1; -; mRNA.
DR EMBL; AF056035; AAC95129.1; -; mRNA.
DR RefSeq; NP_631976.1; NM_139230.1. [Q9Z2J4-1]
DR RefSeq; NP_631977.1; NM_139231.1. [Q9Z2J4-2]
DR RefSeq; XP_006233545.1; XM_006233483.3. [Q9Z2J4-1]
DR RefSeq; XP_006233546.1; XM_006233484.2. [Q9Z2J4-2]
DR AlphaFoldDB; Q9Z2J4; -.
DR SMR; Q9Z2J4; -.
DR STRING; 10116.ENSRNOP00000016968; -.
DR iPTMnet; Q9Z2J4; -.
DR PhosphoSitePlus; Q9Z2J4; -.
DR PaxDb; Q9Z2J4; -.
DR PRIDE; Q9Z2J4; -.
DR Ensembl; ENSRNOT00000099274; ENSRNOP00000080182; ENSRNOG00000012512. [Q9Z2J4-1]
DR GeneID; 246172; -.
DR KEGG; rno:246172; -.
DR CTD; 91624; -.
DR RGD; 708354; Nexn.
DR eggNOG; ENOG502QU7W; Eukaryota.
DR GeneTree; ENSGT00730000111176; -.
DR InParanoid; Q9Z2J4; -.
DR PhylomeDB; Q9Z2J4; -.
DR PRO; PR:Q9Z2J4; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000012512; Expressed in quadriceps femoris and 20 other tissues.
DR ExpressionAtlas; Q9Z2J4; baseline and differential.
DR Genevisible; Q9Z2J4; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
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; IDA:RGD.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:RGD.
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; ISO:RGD.
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; Alternative splicing; Cell junction; Cytoplasm;
KW Cytoskeleton; Immunoglobulin domain; Phosphoprotein; Reference proteome.
FT CHAIN 1..656
FT /note="Nexilin"
FT /id="PRO_0000302087"
FT DOMAIN 562..650
FT /note="Ig-like"
FT /evidence="ECO:0000255"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q0ZGT2"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 350
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q0ZGT2"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 549
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 551
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 11..74
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9832551"
FT /id="VSP_052528"
FT VAR_SEQ 148
FT /note="Q -> QIEDINNTGTESASE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9832551"
FT /id="VSP_052529"
SQ SEQUENCE 656 AA; 78393 MW; 98A4F2AF0396A7F2 CRC64;
MNDVSQKAEI LLSSSKPVPK SYVPKLGKGD VKDKFEAMQR AREERNQRRS RDEKQRRKEQ
YIREREWNRR KQEIKDMLAS DEEEEPSKVE KAYVPKLTGT VKGKFDEMEK HRQEEQRKRT
EEERKRRIEQ DLLEKRKMQR ELAKRAEQEG DDSLLITVVP AKSYRAAANR KDPEDLDREH
RNGRVSQEEE KTRHEEECRA LKEAKCLSLV MDDETEAKKE SRFPGKLKST FEELERQRQE
NRKKQAEEEA RRRLEEERRA FEEARRNMVN EEDESQDTET VFKEYRPGKL RLSFEEIERQ
RREEEKRKAE EEARRRMEEE KKAFAEARRS MVLDDDSPEI YKAVSQESLT PGKLEINFEQ
LLRQKMEEER RRTEEERRQK LEMEKQEFEQ LRQEMGKEEE ENESFGLSRE YEELIKLKRS
GSIQAKNLKS KFEKIGQLSE KEVQKKIEEE RAKRRAIDLE IKEREAENFH EDDDVDVKPA
KKSESPFTHK VNMKARFEQM AKARQEEEQR RIEEQKLLRM QFEQKEIDAA LQKKREDDEE
EEGSIVNGST TEDEEQTRSG APWFKKPLRN TSVVDSEPVR FTVKVTGEPK PEVTWWFEGE
LLQDGEDYQY IERGETYCLY LPETFPEDGG EYMCKAVNSK GSAASTCILT IEMDDY
