LOCUS       NP_113663                854 aa            linear   PRI 05-DEC-2024
DEFINITION  espin isoform 1 [Homo sapiens].
ACCESSION   NP_113663
VERSION     NP_113663.2
DBSOURCE    REFSEQ: accession NM_031475.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 854)
  AUTHORS   Wang,L., Wei,B., Fu,X., Wang,Y., Sui,Y., Ma,J., Gong,X., Hao,J. and
            Xing,S.
  TITLE     Identification of whirlin domains interacting with espin: A study
            of the mechanism of Usher syndrome type II
  JOURNAL   Mol Med Rep 20 (6), 5111-5117 (2019)
   PUBMED   31638198
  REMARK    GeneRIF: whirlin-espin interaction is important for the
            architecture of the USH2 complex and actin bundles cross-linked by
            espin. Our demonstration of whirlin N-terminal fragment interaction
            with espin, is significantly novel, providing insight into how
            these two proteins interact to form the USH2 complex.
REFERENCE   2  (residues 1 to 854)
  AUTHORS   Ahmed,Z.M., Jaworek,T.J., Sarangdhar,G.N., Zheng,L., Gul,K.,
            Khan,S.N., Friedman,T.B., Sisk,R.A., Bartles,J.R., Riazuddin,S. and
            Riazuddin,S.
  TITLE     Inframe deletion of human ESPN is associated with deafness,
            vestibulopathy and vision impairment
  JOURNAL   J Med Genet 55 (7), 479-488 (2018)
   PUBMED   29572253
  REMARK    GeneRIF: ur study uncovers an additional USH gene, assigns the USH1
            phenotype to a variant of ESPN and provides a 12th molecular
            component to the USH proteome
REFERENCE   3  (residues 1 to 854)
  AUTHORS   Zhu,Y., Zhang,H.L., Wang,Q.Y., Chen,M.J. and Liu,L.B.
  TITLE     Overexpression of microRNA-612 Restrains the Growth, Invasion, and
            Tumorigenesis of Melanoma Cells by Targeting Espin
  JOURNAL   Mol Cells 41 (2), 119-126 (2018)
   PUBMED   29385671
  REMARK    GeneRIF: A significant inverse correlation was observed between
            miR-612 and Espin protein expression in melanoma tissues.
REFERENCE   4  (residues 1 to 854)
  AUTHORS   Taura,A., Taura,K., Koyama,Y., Yamamoto,N., Nakagawa,T., Ito,J. and
            Ryan,A.F.
  TITLE     Hair cell stereociliary bundle regeneration by espin gene
            transduction after aminoglycoside damage and hair cell induction by
            Notch inhibition
  JOURNAL   Gene Ther 23 (5), 415-423 (2016)
   PUBMED   26886463
  REMARK    GeneRIF: The utricles were then treated with a gamma-secretase
            inhibitor, followed by espin or control transduction and
            histochemistry. Although gamma-secretase inhibition increased the
            number of HCs, few had stereociliary arrays. In contrast, 46 h
            after espin1 transduction, a significant increase in
            hair-bundle-like structures was observed
REFERENCE   5  (residues 1 to 854)
  AUTHORS   Liu,H., Li,J., Raval,M.H., Yao,N., Deng,X., Lu,Q., Nie,S., Feng,W.,
            Wan,J., Yengo,C.M., Liu,W. and Zhang,M.
  TITLE     Myosin III-mediated cross-linking and stimulation of actin bundling
            activity of Espin
  JOURNAL   Elife 5, e12856 (2016)
   PUBMED   26785147
  REMARK    GeneRIF: The structures of Myo3 in complex with Espin1 not only
            elucidate the mechanism of the binding, but also reveal a
            Myo3-induced release of Espin1 auto-inhibition mechanism.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 854)
  AUTHORS   Sekerkova,G., Loomis,P.A., Changyaleket,B., Zheng,L., Eytan,R.,
            Chen,B., Mugnaini,E. and Bartles,J.R.
  TITLE     Novel espin actin-bundling proteins are localized to Purkinje cell
            dendritic spines and bind the Src homology 3 adapter protein
            insulin receptor substrate p53
  JOURNAL   J Neurosci 23 (4), 1310-1319 (2003)
   PUBMED   12598619
REFERENCE   7  (residues 1 to 854)
  AUTHORS   Zheng,L., Sekerkova,G., Vranich,K., Tilney,L.G., Mugnaini,E. and
            Bartles,J.R.
  TITLE     The deaf jerker mouse has a mutation in the gene encoding the espin
            actin-bundling proteins of hair cell stereocilia and lacks espins
  JOURNAL   Cell 102 (3), 377-385 (2000)
   PUBMED   10975527
REFERENCE   8  (residues 1 to 854)
  AUTHORS   Bartles,J.R., Zheng,L., Li,A., Wierda,A. and Chen,B.
  TITLE     Small espin: a third actin-bundling protein and potential forked
            protein ortholog in brush border microvilli
  JOURNAL   J Cell Biol 143 (1), 107-119 (1998)
   PUBMED   9763424
REFERENCE   9  (residues 1 to 854)
  AUTHORS   Bartles,J.R., Wierda,A. and Zheng,L.
  TITLE     Identification and characterization of espin, an actin-binding
            protein localized to the F-actin-rich junctional plaques of Sertoli
            cell ectoplasmic specializations
  JOURNAL   J Cell Sci 109 (Pt 6), 1229-1239 (1996)
   PUBMED   8799813
REFERENCE   10 (residues 1 to 854)
  AUTHORS   Shearer,A.E., Hildebrand,M.S., Odell,A.M. and Smith,R.J.H.
  TITLE     Genetic Hearing Loss Overview
  JOURNAL   (in) Adam MP, Feldman J, Mirzaa GM, Pagon RA, Wallace SE and
            Amemiya A (Eds.);
            GENEREVIEWS(R);
            (1993)
   PUBMED   20301607
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from HY016927.1, AL136880.1,
            BM713713.1, AL031848.11 and AL158217.25.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Jul 18, 2006 this sequence version replaced NP_113663.1.
            
            Summary: This gene encodes a multifunctional actin-bundling
            protein. It plays a major role in regulating the organization,
            dimensions, dynamics, and signaling capacities of the actin
            filament-rich, microvillus-type specializations that mediate
            sensory transduction in various mechanosensory and chemosensory
            cells. Mutations in this gene are associated with autosomal
            recessive neurosensory deafness, and autosomal dominant
            sensorineural deafness without vestibular involvement. [provided by
            RefSeq, Nov 2009].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AL136880.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1968540, SAMEA1968968
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000645284.1/ ENSP00000496593.1
            RefSeq Select criteria :: based on conservation
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..854
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="1"
                     /map="1p36.31"
     Protein         1..854
                     /product="espin isoform 1"
                     /note="ectoplasmic specialization protein; autosomal
                     recessive deafness type 36 protein"
                     /calculated_mol_wt=91602
     Region          1..31
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AK53.1)"
     Region          2..277
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Region          35..64
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AK53.1)"
     Region          39..67
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          69..101
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          69..99
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AK53.1)"
     Region          103..135
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          103..133
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AK53.1)"
     Site            order(137,139,143..144,147..149,151..152,156,159,169,171,
                     173,177..178,181..183,185..186,190,194,203,205,207,
                     211..212,215..217,219..220,224,227)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          137..169
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          137..167
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AK53.1)"
     Region          171..203
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          171..201
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AK53.1)"
     Region          <196..365
                     /region_name="PLN03192"
                     /note="Voltage-dependent potassium channel; Provisional"
                     /db_xref="CDD:215625"
     Region          205..235
                     /region_name="ANK 7"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AK53.1)"
     Region          239..269
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          239..268
                     /region_name="ANK 8"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AK53.1)"
     Region          271..302
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          271..300
                     /region_name="ANK 9"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AK53.1)"
     Region          338..400
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AK53.1)"
     Site            338
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63618; propagated from
                     UniProtKB/Swiss-Prot (B1AK53.1)"
     Site            342
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ET47; propagated from
                     UniProtKB/Swiss-Prot (B1AK53.1)"
     Region          415..474
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AK53.1)"
     Region          487..713
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AK53.1)"
     Site            515
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63618; propagated from
                     UniProtKB/Swiss-Prot (B1AK53.1)"
     Site            647
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ET47; propagated from
                     UniProtKB/Swiss-Prot (B1AK53.1)"
     Region          648..673
                     /region_name="WH2"
                     /note="WH2 motif; pfam02205"
                     /db_xref="CDD:460490"
     Site            690
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9ET47; propagated from
                     UniProtKB/Swiss-Prot (B1AK53.1)"
     Site            696
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q63618; propagated from
                     UniProtKB/Swiss-Prot (B1AK53.1)"
     Region          765..788
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AK53.1)"
     Region          800..832
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (B1AK53.1)"
     CDS             1..854
                     /gene="ESPN"
                     /gene_synonym="DFNB36; LP2654; USH1M"
                     /coded_by="NM_031475.3:181..2745"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS70.1"
                     /db_xref="GeneID:83715"
                     /db_xref="HGNC:HGNC:13281"
                     /db_xref="MIM:606351"
ORIGIN      
        1 maleqalqaa rqgeldvlrs lhaagllgps lrdpldalpv hhaaragklh clrflveeaa
       61 lpaaararng atpahdasat ghlaclqwll sqggcrvqdk dnsgatvlhl aarfghpevv
      121 nwllhhgggd ptaatdmgal pihyaaakgd fpslrllveh ypegvnaqtk ngatplylac
      181 qeghlevtqy lvqecgadph arahdgmtpl haaaqmghsp vivwlvsctd vslseqdkdg
      241 atamhfaasr ghtkvlswll lhggeisadl wggtplhdaa engeleccqi lvvngaeldv
      301 rdrdgytaad lsdfnghshc trylrtvenl svehrvlsrd psaeleakqp dsgmsspntt
      361 vsvqplnfdl ssptstlsny dscssshssi kgqhppcgls saraadiqsy mdmlnpelgl
      421 prgtigkptp pppppsfppp ppppgtqlpp pppgypapkp pvgpqaadiy mqtknklrhv
      481 etealkkels scdghdglrr qdssrkpraf skqpstgdyy rqlgrcpget laarpgmahs
      541 eevrarqpar agcprlgpaa rgslegpsap pqaallpgnh vpngcaadpk asrelppppp
      601 ppppplpeaa sspppapplp lesagpgcgq rrsssstgst ksfnmmsptg dnsellaeik
      661 agkslkptpq skglttvfsg igqpafqpds plpsvspals pvrsptppaa gfqpllngsl
      721 vpvppttpap gvqldveali pthdeqgrpi pewkrqvmvr kmqlkmqeee eqrrkeeeee
      781 arlasmpawr rdllrkklee ereqkrkeee rqkqeelrre keqseklrtl gydesklapw
      841 qrqvilkkgd iaky
//
