ID B4E3F8_HUMAN Unreviewed; 507 AA.
AC B4E3F8;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=cDNA FLJ54257, highly similar to Leiomodin-1 {ECO:0000313|EMBL:BAG65470.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG65470.1};
RN [1] {ECO:0000313|EMBL:BAG65470.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Uterus {ECO:0000313|EMBL:BAG65470.1};
RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA Sugano S., Nomura N., Isogai T.;
RT "NEDO human cDNA sequencing project focused on splicing variants.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere
CC {ECO:0000256|ARBA:ARBA00004204}.
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DR EMBL; AK304700; BAG65470.1; -; mRNA.
DR AlphaFoldDB; B4E3F8; -.
DR MaxQB; B4E3F8; -.
DR PeptideAtlas; B4E3F8; -.
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; PF02205; WH2; 1.
DR SMART; SM00246; WH2; 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS51082; WH2; 1.
PE 2: Evidence at transcript level;
FT DOMAIN 481..500
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 1..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..452
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 56404 MW; BF06D26A3125DE4A CRC64;
MSRVAKYRRQ VSEDPDIDSL LETLSPEEME EPKRGGLKKS FSRDRDEAGG KSGEKPKEEK
IIRGIDKGRV RAAVDKKEAG KDGRGEERAV ATKKEEEKKG SDRNTGLSRD KDKKREEMKE
VAKKEDDEKV KGERRNTDTR KEGEKMKRAG GNTDMKKEDE KVKRGTGNTD TKKDDEKVKK
NEPLHEKEAK DDSKTKTPEK QTPSGPTKPS EGPAKVEEEA APSIFDEPLE RVKNNDPEMT
EVNVNNSDCI TNEILVRFTE ALEFNTVVKL FALANTRADD HVAFAIAIML KANKTITSLN
LDSNHITGKG ILAIFRALLQ NNTLTELRFH NQRHICGGKT EMEIAKLLKE NTTLLKLGYH
FELAGPRMTV TNLLSRNMDK QRQKRLQEQR QAQEAEGEKK DLLEVPKAGA VAKGSPKPSP
QPSPKPSPKN SPKKGGAPAA PPPPPPPLAP PLIMENLKNS LSPATQRKMG DKVLPAQGKN
SRDQLLAAIR SSNLKQLKKV EVPKLLQ
//
