ESPN_RAT
ID ESPN_RAT Reviewed; 837 AA.
AC Q63618; Q6GYS2; Q6GYS3; Q80ZB6; Q80ZB7; Q80ZB8; Q80ZB9; Q9Z2B4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Espin;
DE AltName: Full=Ectoplasmic specialization protein;
GN Name=Espn;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 20-39; 556-568;
RP 662-684; 775-779 AND 820-822, INTERACTION WITH F-ACTIN, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=8799813; DOI=10.1242/jcs.109.6.1229;
RA Bartles J.R., Wierda A., Zheng L.;
RT "Identification and characterization of espin, an actin-binding protein
RT localized to the F-actin-rich junctional plaques of Sertoli cell
RT ectoplasmic specializations.";
RL J. Cell Sci. 109:1229-1239(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBUNIT, INTERACTION WITH
RP F-ACTIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=9763424; DOI=10.1083/jcb.143.1.107;
RA Bartles J.R., Zheng L., Li A., Wierda A., Chen B.;
RT "Small espin: a third actin-bundling protein and potential forked protein
RT ortholog in brush border microvilli.";
RL J. Cell Biol. 143:107-119(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 6 AND 8), TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, AND INTERACTION WITH BAIAP2.
RC STRAIN=Sprague-Dawley; TISSUE=Cerebellum;
RX PubMed=12598619; DOI=10.1523/jneurosci.23-04-01310.2003;
RA Sekerkova G., Loomis P.A., Changyaleket B., Zheng L., Eytan R., Chen B.,
RA Mugnaini E., Bartles J.R.;
RT "Novel espin actin-bundling proteins are localized to Purkinje cell
RT dendritic spines and bind the Src homology 3 adapter protein insulin
RT receptor substrate p53.";
RL J. Neurosci. 23:1310-1319(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 7), AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=15190118; DOI=10.1523/jneurosci.1279-04.2004;
RA Sekerkova G., Zheng L., Loomis P.A., Changyaleket B., Whitlon D.S.,
RA Mugnaini E., Bartles J.R.;
RT "Espins are multifunctional actin cytoskeletal regulatory proteins in the
RT microvilli of chemosensory and mechanosensory cells.";
RL J. Neurosci. 24:5445-5456(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337; SER-341; SER-400;
RP SER-401; SER-497; SER-504; SER-531; SER-670; SER-674 AND SER-680, AND
RP IDENTIFICATION BY MASS 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: Multifunctional actin-bundling protein. Plays a major role in
CC regulating the organization, dimension, dynamics and signaling
CC capacities of the actin filament-rich microvilli in the mechanosensory
CC and chemosensory cells (PubMed:9763424). Required for the assembly and
CC stabilization of the stereociliary parallel actin bundles. Plays a
CC crucial role in the formation and maintenance of inner ear hair cell
CC stereocilia. Involved in the elongation of actin in stereocilia. In
CC extrastriolar hair cells, required for targeting MYO3B to stereocilia
CC tips, and for regulation of stereocilia diameter and staircase
CC formation (By similarity). {ECO:0000250|UniProtKB:Q9ET47,
CC ECO:0000269|PubMed:9763424}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with PFN2 (By similarity).
CC Binds F-actin in a Ca(2+)-resistant fashion (PubMed:8799813,
CC PubMed:9763424). Interacts (via N-terminal) with BAIAP2 (via SH3-
CC domain) (PubMed:12598619). Interacts with MYO3A (via C-terminus).
CC Interacts with MYO3B (via C-terminus) (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9ET47, ECO:0000269|PubMed:12598619,
CC ECO:0000269|PubMed:8799813, ECO:0000269|PubMed:9763424}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection,
CC stereocilium {ECO:0000250|UniProtKB:Q9ET47}. Cell projection,
CC microvillus. Cell junction.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton. Cell
CC junction. Note=Isoform 1 localizes to parallel actin bundles of
CC ectoplasmic specializations between neighboring Sertoli cells and at
CC sites where Sertoli cells contact the heads of elongate spermatids.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton. Cell
CC projection, microvillus. Note=Isoform 2 localizes to parallel actin
CC bundles of brush border microvilli of small intestine and kidney.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cytoskeleton. Cell
CC projection, dendritic spine.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm, cytoskeleton. Cell
CC projection, dendritic spine.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm, cytoskeleton. Cell
CC projection, dendritic spine.
CC -!- SUBCELLULAR LOCATION: [Isoform 8]: Cytoplasm, cytoskeleton. Cell
CC projection, dendritic spine.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1; Synonyms=large;
CC IsoId=Q63618-1; Sequence=Displayed;
CC Name=2; Synonyms=small;
CC IsoId=Q63618-2; Sequence=VSP_033741, VSP_033748, VSP_033750;
CC Name=3; Synonyms=Purkinje cell espin 1;
CC IsoId=Q63618-3; Sequence=VSP_033744, VSP_033745;
CC Name=4; Synonyms=Purkinje cell espin 1+;
CC IsoId=Q63618-4; Sequence=VSP_033744, VSP_033745, VSP_033749;
CC Name=5; Synonyms=3B;
CC IsoId=Q63618-5; Sequence=VSP_033743, VSP_033747;
CC Name=6; Synonyms=Purkinje cell espin 2;
CC IsoId=Q63618-6; Sequence=VSP_033744, VSP_033745, VSP_033746;
CC Name=7; Synonyms=3A;
CC IsoId=Q63618-7; Sequence=VSP_033742;
CC Name=8; Synonyms=Purkinje cell espin 2+;
CC IsoId=Q63618-8; Sequence=VSP_033744, VSP_033745, VSP_033746,
CC VSP_033749;
CC -!- TISSUE SPECIFICITY: Expressed at high concentration in the microvillar
CC parallel actin bundle (PAB) of hair cells stereocilia in the cochlea
CC and vestibular system. Detected also at high levels of a number of
CC other sensory cell types, including taste receptor cells, solitary
CC chemoreceptor cells, vomeronasal sensory neurons and Merkel cells.
CC Isoform 1 is detected in testis. Isoforms 2 is detected in small
CC intestine and kidney (at protein level). Isoforms 3, 4, 6 and 8 are
CC expressed in Purkinje cells dendritic spines.
CC {ECO:0000269|PubMed:12598619, ECO:0000269|PubMed:15190118,
CC ECO:0000269|PubMed:8799813, ECO:0000269|PubMed:9763424}.
CC -!- DEVELOPMENTAL STAGE: Isoform 2 accumulates in the brush border during
CC enterocyte differentiation and migration along the crypt-villus axis in
CC adults. {ECO:0000269|PubMed:9763424}.
CC -!- DOMAIN: The WH2-domain binds actin monomer and mediated actin bundle
CC assembly. {ECO:0000250|UniProtKB:Q9ET47}.
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DR EMBL; U46007; AAC53594.1; -; mRNA.
DR EMBL; AF076856; AAC69563.1; -; mRNA.
DR EMBL; AF540946; AAO50330.1; -; mRNA.
DR EMBL; AF540947; AAO50331.1; -; mRNA.
DR EMBL; AF540948; AAO50332.1; -; mRNA.
DR EMBL; AF540949; AAO50333.1; -; mRNA.
DR EMBL; AY587568; AAT46470.1; -; mRNA.
DR EMBL; AY587569; AAT46471.1; -; mRNA.
DR RefSeq; XP_006239546.1; XM_006239484.3. [Q63618-2]
DR AlphaFoldDB; Q63618; -.
DR SMR; Q63618; -.
DR BioGRID; 248563; 2.
DR MINT; Q63618; -.
DR STRING; 10116.ENSRNOP00000039445; -.
DR iPTMnet; Q63618; -.
DR PhosphoSitePlus; Q63618; -.
DR PaxDb; Q63618; -.
DR PRIDE; Q63618; -.
DR Ensembl; ENSRNOT00000013646; ENSRNOP00000013645; ENSRNOG00000010270. [Q63618-2]
DR GeneID; 56227; -.
DR UCSC; RGD:620652; rat. [Q63618-1]
DR CTD; 83715; -.
DR RGD; 620652; Espn.
DR VEuPathDB; HostDB:ENSRNOG00000010270; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000160408; -.
DR HOGENOM; CLU_086871_0_0_1; -.
DR InParanoid; Q63618; -.
DR OrthoDB; 347029at2759; -.
DR PhylomeDB; Q63618; -.
DR PRO; PR:Q63618; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000010270; Expressed in jejunum and 13 other tissues.
DR ExpressionAtlas; Q63618; baseline and differential.
DR Genevisible; Q63618; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0031941; C:filamentous actin; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IDA:MGI.
DR GO; GO:0032420; C:stereocilium; ISO:RGD.
DR GO; GO:0032421; C:stereocilium bundle; ISO:RGD.
DR GO; GO:0032426; C:stereocilium tip; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; ISO:RGD.
DR GO; GO:0007015; P:actin filament organization; NAS:UniProtKB.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0030034; P:microvillar actin bundle assembly; ISO:RGD.
DR GO; GO:0051494; P:negative regulation of cytoskeleton organization; ISO:RGD.
DR GO; GO:0030046; P:parallel actin filament bundle assembly; ISO:RGD.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; ISO:RGD.
DR GO; GO:0007605; P:sensory perception of sound; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR030233; Espn.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR24153:SF14; PTHR24153:SF14; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00248; ANK; 8.
DR SMART; SM00246; WH2; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 6.
DR PROSITE; PS51082; WH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; ANK repeat; Cell junction;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Hearing; Phosphoprotein; Reference proteome;
KW Repeat; Synapse.
FT CHAIN 1..837
FT /note="Espin"
FT /id="PRO_0000334668"
FT REPEAT 1..31
FT /note="ANK 1"
FT REPEAT 35..66
FT /note="ANK 2"
FT REPEAT 69..99
FT /note="ANK 3"
FT REPEAT 103..132
FT /note="ANK 4"
FT REPEAT 137..167
FT /note="ANK 5"
FT REPEAT 171..201
FT /note="ANK 6"
FT REPEAT 205..235
FT /note="ANK 7"
FT REPEAT 238..267
FT /note="ANK 8"
FT REPEAT 270..299
FT /note="ANK 9"
FT DOMAIN 635..652
FT /note="WH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT REGION 339..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 738..814
FT /evidence="ECO:0000255"
FT COMPBIAS 348..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..454
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..605
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..696
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 531
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ET47"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..609
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9763424"
FT /id="VSP_033741"
FT VAR_SEQ 1..552
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:15190118"
FT /id="VSP_033742"
FT VAR_SEQ 1..522
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15190118"
FT /id="VSP_033743"
FT VAR_SEQ 1..326
FT /note="Missing (in isoform 3, isoform 4, isoform 6 and
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:12598619"
FT /id="VSP_033744"
FT VAR_SEQ 327..329
FT /note="QTL -> MGD (in isoform 3, isoform 4, isoform 6 and
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:12598619"
FT /id="VSP_033745"
FT VAR_SEQ 483..558
FT /note="Missing (in isoform 6 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:12598619"
FT /id="VSP_033746"
FT VAR_SEQ 523..558
FT /note="QRSFSKQPSTGDYYRQLGRSPGEPLAARPGMAHSEE -> MAHSEEVRVHQP
FT APAGCTGSNPVSHSSLSGPSAPPQ (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15190118"
FT /id="VSP_033747"
FT VAR_SEQ 610..622
FT /note="AACGQRRSSSSTG -> MNSQGPLRGGRMP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9763424"
FT /id="VSP_033748"
FT VAR_SEQ 622
FT /note="G -> GKVRILRHRK (in isoform 4 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:12598619"
FT /id="VSP_033749"
FT VAR_SEQ 671
FT /note="Q -> QVGTGRVPRPGSQCLPSAQPYRFSRQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9763424"
FT /id="VSP_033750"
SQ SEQUENCE 837 AA; 90569 MW; 64F3C2C23980CA72 CRC64;
MALEQAMQAA RRGDLDVLRS LHAAGLLGPS LRDPLDALPV HHAARSGKLH CLRYLVEEVA
LPAVSRARNG ATPAHDAAAT GYLSCLQWLL TQGGCRVQEK DNSGATVLHL AARFGHPDVV
NWLLYQGGAN SAITTDTGAL PIHYAAAKGD LPSMKLLVGH YPEGVNAQTN NGATPLYLAC
QEGHLEVTKY LVQECSADPH LRAQDGMTPL HAAAQMGHNP VLVWLVSFAD VSFEQDHDGA
TAMHFAASRG HTKVLSWLLL HGAEISQDLW GGTPLHDAAE NGELECCQIL AVNGAGLDVR
DHDGYTAADL ADFNGHTHCS RYLRTVQTLS LEHRVLSRDP SMDLEAKQPD SGMSSPNTTM
SVQPPNFDLG SPTSTLSNYD SCSSSHSSSK GQRSTRGARS SDLQSYMDML NPEPRSKQGK
PSSLPPPPPP SFPPPPPPGT QLPPPPPGYP APNPPVGLHL DNIYMQTKNK LRHVEVDSLK
KEPSSGDGYS GLRRQDSGLL RQDSELLLRH NTGLRRQDSD RKQRSFSKQP STGDYYRQLG
RSPGEPLAAR PGMAHSEEAA LLPGNHVHNG CSADSKASRE LPPPPPPPPL PEALSSPPPA
PPLPIEGAGA ACGQRRSSSS TGSTKSFNMM SPTGDNSELL AEIKAGKSLK PTPQSKGLTT
VFSGSGQPAS QPESPQPAVS PGPSRARSPT PPASGPQPLL NGSIVPAPPA TLAPGVHLDV
EALIPTLDEQ GRPIPEWKRQ VMVRKLQQKM QEEEEQRRKE EEEEARLASL PAWRRDILRK
KLEEEREQKR KEEERQKLEE IQRAKEQSEK LRTLGYDEAK LAPWQRQVIL KKGEIPK
