ID A0A1S2ZNL7_ERIEU Unreviewed; 580 AA.
AC A0A1S2ZNL7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Leiomodin-1 {ECO:0000313|RefSeq:XP_007522151.1};
GN Name=LMOD1 {ECO:0000313|RefSeq:XP_007522151.1};
OS Erinaceus europaeus (Western European hedgehog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC Erinaceus.
OX NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007522151.1};
RN [1] {ECO:0000313|RefSeq:XP_007522151.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere
CC {ECO:0000256|ARBA:ARBA00004204}.
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DR RefSeq; XP_007522151.1; XM_007522089.2.
DR AlphaFoldDB; A0A1S2ZNL7; -.
DR GeneID; 103112626; -.
DR CTD; 25802; -.
DR eggNOG; KOG3735; Eukaryota.
DR InParanoid; A0A1S2ZNL7; -.
DR OrthoDB; 2883785at2759; -.
DR Proteomes; UP000079721; Unplaced.
DR GO; GO:0030017; C:sarcomere; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0005523; F:tropomyosin binding; IEA:InterPro.
DR GO; GO:0051694; P:pointed-end actin filament capping; IEA:InterPro.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR004934; TMOD.
DR InterPro; IPR003124; WH2_dom.
DR PANTHER; PTHR10901:SF5; LEIOMODIN-1; 1.
DR PANTHER; PTHR10901; TROPOMODULIN; 1.
DR Pfam; PF03250; Tropomodulin; 1.
DR Pfam; PF02205; WH2; 1.
DR SMART; SM00246; WH2; 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS51082; WH2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000079721}.
FT DOMAIN 554..573
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 37..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..500
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..525
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 580 AA; 64106 MW; FDF39E01373C9C71 CRC64;
MSKVAKYRRQ VSEDPDIDSL LSTLSPEEME ELEKELDVVD PDGSVPVGLL QRNQTDKPAT
GTYNREAMLN FCEKETKKIL QKEMSMEESK PVEPQTDTKN GGDKGSSKKS LGPRRDSDIR
KEPRKGVLKK SFSKDLEASD GRSGERPKEE KIIRGIDKGR VRAAVDKKEA GRDGKGEEKA
AAPLKDEEKK ETKGRDRSLG LGRDGVKRDE TTTETAKKED AGKTPGDPRK EEEKVKTARG
SSDVKKKEEE QVKRRSAETK REDEKAPEKA PPSEKAAKED SKSKQAPGVA PKAEEEAAPS
IFDEPLEKVR NNDPEMTEVN VNNSDCITTE ILVRFTEALE FNSVVKVFAL ANTRADDHVA
FAIALMLKAN KTITSLNLDS NHITGKGILA IFRALLQNST LTELRFHNQR HICGGKTEME
IAKLLKDNST LLKLGYHFEL AGPRMTVTNL LSRNMDKQRQ RRLQEQRQAL EAQGTLQPPK
APALPRISPQ ASPQPSPKAP AKNSPKKGVT PAAPPPPPPP LAPPLIVENL KNSLSPATQR
KMGDKALPAQ EKNSRDQLLA AIRSSNLKQL KKVEVPKLLQ
//
