ID   MYPN_MOUSE              Reviewed;        1315 AA.
AC   Q5DTJ9; Q7TPW5; Q8BZ76;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Myopalladin;
GN   Name=Mypn; Synonyms=Kiaa4170;
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].
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT   complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT   screening of terminal sequences of cDNA clones randomly sampled from size-
RT   fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-754.
RC   STRAIN=C57BL/6J; TISSUE=Bone;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1053-1315.
RC   STRAIN=C57BL/6J; TISSUE=Blastocyst;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129 AND SER-924, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, and Lung;
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: Component of the sarcomere that tethers together nebulin
CC       (skeletal muscle) and nebulette (cardiac muscle) to alpha-actinin, at
CC       the Z lines. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with TTN/titin, NEB, NEBL, ACTN2 and CARP.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86TC9}. Nucleus
CC       {ECO:0000250|UniProtKB:Q86TC9}. Cytoplasm, myofibril, sarcomere
CC       {ECO:0000250|UniProtKB:Q86TC9}. Cytoplasm, myofibril, sarcomere, Z line
CC       {ECO:0000250|UniProtKB:Q86TC9}. Note=Bound to sarcomere both at the Z-
CC       line periphery and in the central I-band region.
CC       {ECO:0000250|UniProtKB:Q86TC9}.
CC   -!- SIMILARITY: Belongs to the myotilin/palladin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90521.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK220521; BAD90521.1; ALT_INIT; mRNA.
DR   EMBL; AK036458; BAC29439.1; -; mRNA.
DR   EMBL; BC052872; AAH52872.1; -; mRNA.
DR   CCDS; CCDS48584.1; -.
DR   RefSeq; NP_892037.2; NM_182992.2.
DR   AlphaFoldDB; Q5DTJ9; -.
DR   SMR; Q5DTJ9; -.
DR   BioGRID; 213060; 8.
DR   IntAct; Q5DTJ9; 1.
DR   STRING; 10090.ENSMUSP00000093240; -.
DR   GlyGen; Q5DTJ9; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q5DTJ9; -.
DR   PhosphoSitePlus; Q5DTJ9; -.
DR   MaxQB; Q5DTJ9; -.
DR   PaxDb; 10090-ENSMUSP00000093240; -.
DR   PeptideAtlas; Q5DTJ9; -.
DR   ProteomicsDB; 287599; -.
DR   Antibodypedia; 28426; 140 antibodies from 22 providers.
DR   DNASU; 68802; -.
DR   Ensembl; ENSMUST00000095580.3; ENSMUSP00000093240.3; ENSMUSG00000020067.9.
DR   GeneID; 68802; -.
DR   KEGG; mmu:68802; -.
DR   UCSC; uc007fjy.2; mouse.
DR   AGR; MGI:1916052; -.
DR   CTD; 84665; -.
DR   MGI; MGI:1916052; Mypn.
DR   VEuPathDB; HostDB:ENSMUSG00000020067; -.
DR   eggNOG; ENOG502QSRV; Eukaryota.
DR   GeneTree; ENSGT00940000153441; -.
DR   HOGENOM; CLU_006487_2_0_1; -.
DR   InParanoid; Q5DTJ9; -.
DR   OMA; DEMDHKP; -.
DR   OrthoDB; 5356884at2759; -.
DR   PhylomeDB; Q5DTJ9; -.
DR   TreeFam; TF343193; -.
DR   BioGRID-ORCS; 68802; 5 hits in 77 CRISPR screens.
DR   ChiTaRS; Mypn; mouse.
DR   PRO; PR:Q5DTJ9; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q5DTJ9; Protein.
DR   Bgee; ENSMUSG00000020067; Expressed in gastrocnemius medialis and 90 other cell types or tissues.
DR   ExpressionAtlas; Q5DTJ9; baseline and differential.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0031674; C:I band; IDA:BHF-UCL.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030018; C:Z disc; ISO:MGI.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR   GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI.
DR   GO; GO:0051371; F:muscle alpha-actinin binding; ISO:MGI.
DR   GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
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:0045214; P:sarcomere organization; ISO:MGI.
DR   CDD; cd20972; IgI_2_Titin_Z1z2-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 5.
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   InterPro; IPR003598; Ig_sub2.
DR   PANTHER; PTHR10075; BASIGIN RELATED; 1.
DR   PANTHER; PTHR10075:SF14; DOWN SYNDROME CELL ADHESION MOLECULE 3, ISOFORM E-RELATED; 1.
DR   Pfam; PF07679; I-set; 5.
DR   SMART; SM00409; IG; 5.
DR   SMART; SM00408; IGc2; 5.
DR   SUPFAM; SSF48726; Immunoglobulin; 5.
DR   PROSITE; PS50835; IG_LIKE; 5.
DR   Genevisible; Q5DTJ9; MM.
PE   1: Evidence at protein level;
KW   Actin-binding; Coiled coil; Cytoplasm; Disulfide bond;
KW   Immunoglobulin domain; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..1315
FT                   /note="Myopalladin"
FT                   /id="PRO_0000240490"
FT   DOMAIN          267..357
FT                   /note="Ig-like 1"
FT   DOMAIN          432..528
FT                   /note="Ig-like 2"
FT   DOMAIN          941..1025
FT                   /note="Ig-like 3"
FT   DOMAIN          1068..1157
FT                   /note="Ig-like 4"
FT   DOMAIN          1167..1257
FT                   /note="Ig-like 5"
FT   REGION          19..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          81..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          166..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          230..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          359..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..652
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          674..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          725..747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          762..814
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          840..865
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          219..240
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        20..36
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..103
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        122..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        538..562
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..627
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        795..814
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         99
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86TC9"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         249
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86TC9"
FT   MOD_RES         641
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86TC9"
FT   MOD_RES         754
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86TC9"
FT   MOD_RES         809
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86TC9"
FT   MOD_RES         814
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86TC9"
FT   MOD_RES         903
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q86TC9"
FT   MOD_RES         924
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   DISULFID        288..339
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        453..512
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        1089..1141
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   CONFLICT        1120
FT                   /note="E -> G (in Ref. 3; AAH52872)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1315 AA;  144114 MW;  3CBA735F63983B3F CRC64;
     MQEDSIEAST SISQLLRESY LAETRHRGDN ERSRAEPSSN PFHFSGPGAA EGGGPEDLPD
     LSAFLSQEEL DESVNLARLA INHDPLERVD EAQARKRLSS DQTKHASKPS FEPAFHQDSS
     RGPASPKDSP PETKRPQYSS ETQSKKVFLN KAADFIEELS SLFKAHSSKR IRPRACKNHK
     SKTESQNKVL QENSPTFSDL TERRERASVP IPIPADSRDN ELNHAIEQRE AKRREAELAA
     GEAAAGDSTP GSSPSSLYYE EPLGQPPRFT QKLRSREVPE GSRVQLDCIV VGIPPPQVRW
     YCEGKELENS PDIHIVQAGN LHSLTIAEAF EEDTGRYSCF ASNIYGTDST SAEIYIEGVS
     SSDSEGDPNK EEMNRIQKPN EVSSPPTTSA AIPPAAEAQP LAAQPRVSTV QQCQSPTNYL
     QGLNGKPIIA APVFTKMLQN LSASEGQLVV FECRVKGAPS PKVEWYREGT LIEDSPDFRI
     LQKKPRSMAE PEEICTLVIA EVFSEDSGCF TCTASNKYGT VSSIAQLDVR GNEDISDNGA
     LHSANSTTNP AVAEHQPSPL NPQPLSEEQP PKPKLEGVLV NHNEPRSSSR IGLRVHFNLP
     EDDKDMEASS GSGAANTSQT RPNSFPERFN GQEARIPEPS SPIKEPPPVL AKPKLDSTQL
     QQLHNQVLLE QQQLQNTSPS SPKESLHMSA LNSAPPAVTI SSKQVKGPAP QMFNLARPKH
     FFPASSTSTA TVSPSSSPVF TLSNTPQTIQ RTVSKESLLM AHPSTQGRSP GGLSIQNEPA
     PPSPAEPAAP PTAAYSIPSG NQFQPHCVSP TPVSPTGRIQ NPVAFLSSVL PSLPSIPPTN
     AMGLPKSAPS VPSQGLMKKT TKAPQAVSDD YIRETKNSVI LDLGKKVNFG DVRSHQQEYK
     ISSFEQRLMN EIEFRLERTP VDESDDEIEH DEIPTGKCIA PIFDKRLKHF RVTEGSPVTF
     TCKIVGIPVP KVYWFKDGKQ ISKRNEHCKM RREGDGTCSL HIESTHGDDD GNYTIMAANP
     QGRISCSGHL MVQGLPIRSR LSPALSHRGR SRMQERDKEP LQERFFRPHF LQAPGDMVAH
     EGRLCRLDCK VSGLPPPELT WLLNGQPVLP DASHKMLVRE TGVHSLLIDP LTQRDAGTYT
     CVATNKTGQN SFSLELTVVA KEVKKAPVIL EKLQNSGVPE GHPVRLEGRV IGMPPPVFYW
     KKDNETIPFT RERISMHQDT TGYVCLLIQP AKKSDAGWYT LSAKNEAGIV SCTARLDIYA
     QWHQQIPTPI SIRPSGSRYG SLTSKGLDIF SAFSSVESTM LYSCTSRSVV ESDEL
//