ID B4E3S9_HUMAN Unreviewed; 549 AA.
AC B4E3S9;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=cDNA FLJ53443, highly similar to Leiomodin-1 {ECO:0000313|EMBL:BAG65591.1};
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:BAG65591.1};
RN [1] {ECO:0000313|EMBL:BAG65591.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Uterus {ECO:0000313|EMBL:BAG65591.1};
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; AK304852; BAG65591.1; -; mRNA.
DR AlphaFoldDB; B4E3S9; -.
DR MaxQB; B4E3S9; -.
DR PeptideAtlas; B4E3S9; -.
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 2: Evidence at transcript level;
FT DOMAIN 523..542
FT /note="WH2"
FT /evidence="ECO:0000259|PROSITE:PS51082"
FT REGION 40..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..494
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 549 AA; 61534 MW; 3FB593115CECFC32 CRC64;
MSRVAKYRRQ VSEDPDIDSL LETLSPEEME ELEKELDVVD PDGSVPVGLR QRNQTEKQST
GVYNREAMLN FCEKETKKLM QREMSMDESK QVETKTDPKE EKIIRGIDKG RVRAAVDKKE
AGKDGRGEER AVATKKEEEK KGSDRNTGLS RDKDKKREEM KEVAKKEDDE KVKGERRNTD
TRKEGEKMKR AGGNTDMKKE DEKVKRGTGN TDTKKDDEKV KKNEPLHEKE AKDDSKTKTP
EKQTPSGPTK PSEGPAKVEE EAAPSIFDEP LERVKNNDPE MTEVNVNNSD CITNEILVRF
TEALEFNTVV KLFALANTRA DDHVAFAIAI MLKANKTITS LNLDSNHITG KGILAIFRAL
LQNNTLTELR FHNQRHICGG KTEMEIAKLL KENTTLLKLG YHFELAGPRM TVTNLLSRNM
DKQRQKRLQE QRQAQEAKGE KKDLLEVPKA GAVAKGSPKP SPQPSPKPSP KNSPKKGGAP
AAPPPPPPPL APPLIMENLK NSLSPATQRK MGDKVLPAQE KNSRDQLLAA IRSSNLKQLK
KVEVPKLLQ
//
