SMTL1_HUMAN
ID SMTL1_HUMAN Reviewed; 494 AA.
AC A8MU46; E9PPJ3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Smoothelin-like protein 1;
GN Name=SMTNL1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [2]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18310078; DOI=10.1074/jbc.m708628200;
RA Wooldridge A.A., Fortner C.N., Lontay B., Akimoto T., Neppl R.L.,
RA Facemire C., Datto M.B., Kwon A., McCook E., Li P., Wang S., Thresher R.J.,
RA Miller S.E., Perriard J.C., Gavin T.P., Hickner R.C., Coffman T.M.,
RA Somlyo A.V., Yan Z., Haystead T.A.;
RT "Deletion of the protein kinase A/protein kinase G target SMTNL1 promotes
RT an exercise-adapted phenotype in vascular smooth muscle.";
RL J. Biol. Chem. 283:11850-11859(2008).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=20634291; DOI=10.1074/jbc.m110.143966;
RA Lontay B., Bodoor K., Weitzel D.H., Loiselle D., Fortner C., Lengyel S.,
RA Zheng D., Devente J., Hickner R., Haystead T.A.;
RT "Smoothelin-like 1 protein regulates myosin phosphatase-targeting subunit 1
RT expression during sexual development and pregnancy.";
RL J. Biol. Chem. 285:29357-29366(2010).
CC -!- FUNCTION: Plays a role in the regulation of contractile properties of
CC both striated and smooth muscles. When unphosphorylated, may inhibit
CC myosin dephosphorylation. Phosphorylation at Ser-299 reduces this
CC inhibitory activity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PPP1R12A. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril
CC {ECO:0000269|PubMed:18310078}. Cytoplasm, myofibril, sarcomere, I band
CC {ECO:0000250}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000250}.
CC Nucleus {ECO:0000250}. Note=Colocalizes with MYH2. In its
CC unphosphorylated state, localizes to the cytoplasm (By similarity).
CC Phosphorylation at Ser-301 promotes translocation to the nucleus (By
CC similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in striated muscles, specifically in type
CC 2a fibers (at protein level). {ECO:0000269|PubMed:18310078,
CC ECO:0000269|PubMed:20634291}.
CC -!- PTM: Maximal phosphorylation of Ser-336 correlates with maximal
CC relaxation of aorta in response to acetylcholine. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the smoothelin family. {ECO:0000305}.
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DR EMBL; AP002893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS44599.2; -.
DR RefSeq; NP_001099035.2; NM_001105565.2.
DR RefSeq; XP_005273876.1; XM_005273819.3.
DR AlphaFoldDB; A8MU46; -.
DR SMR; A8MU46; -.
DR IntAct; A8MU46; 1.
DR STRING; 9606.ENSP00000432651; -.
DR iPTMnet; A8MU46; -.
DR PhosphoSitePlus; A8MU46; -.
DR BioMuta; SMTNL1; -.
DR MassIVE; A8MU46; -.
DR PeptideAtlas; A8MU46; -.
DR PRIDE; A8MU46; -.
DR ProteomicsDB; 2081; -.
DR ProteomicsDB; 22736; -.
DR Antibodypedia; 48478; 73 antibodies from 15 providers.
DR DNASU; 219537; -.
DR Ensembl; ENST00000527972.6; ENSP00000432651.1; ENSG00000214872.9.
DR GeneID; 219537; -.
DR KEGG; hsa:219537; -.
DR MANE-Select; ENST00000527972.6; ENSP00000432651.1; NM_001105565.3; NP_001099035.2.
DR UCSC; uc058bmq.1; human.
DR CTD; 219537; -.
DR DisGeNET; 219537; -.
DR GeneCards; SMTNL1; -.
DR HGNC; HGNC:32394; SMTNL1.
DR HPA; ENSG00000214872; Group enriched (skeletal muscle, tongue).
DR MIM; 613664; gene.
DR neXtProt; NX_A8MU46; -.
DR OpenTargets; ENSG00000214872; -.
DR VEuPathDB; HostDB:ENSG00000214872; -.
DR eggNOG; KOG1808; Eukaryota.
DR eggNOG; KOG4678; Eukaryota.
DR GeneTree; ENSGT00940000162276; -.
DR HOGENOM; CLU_040651_5_1_1; -.
DR InParanoid; A8MU46; -.
DR OMA; EWPESPS; -.
DR OrthoDB; 168604at2759; -.
DR PhylomeDB; A8MU46; -.
DR PathwayCommons; A8MU46; -.
DR SignaLink; A8MU46; -.
DR BioGRID-ORCS; 219537; 2 hits in 245 CRISPR screens.
DR GenomeRNAi; 219537; -.
DR Pharos; A8MU46; Tbio.
DR PRO; PR:A8MU46; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; A8MU46; protein.
DR Bgee; ENSG00000214872; Expressed in skeletal muscle tissue of rectus abdominis and 116 other tissues.
DR ExpressionAtlas; A8MU46; baseline and differential.
DR Genevisible; A8MU46; HS.
DR GO; GO:0043292; C:contractile fiber; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0031674; C:I band; IBA:GO_Central.
DR GO; GO:0031430; C:M band; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0051401; F:CH domain binding; IEA:Ensembl.
DR GO; GO:0097718; F:disordered domain specific binding; IEA:Ensembl.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IBA:GO_Central.
DR GO; GO:0043621; F:protein self-association; IEA:Ensembl.
DR GO; GO:0005523; F:tropomyosin binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0048644; P:muscle organ morphogenesis; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; ISS:UniProtKB.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0042310; P:vasoconstriction; IEA:Ensembl.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR Pfam; PF00307; CH; 1.
DR SMART; SM00033; CH; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Coiled coil; Cytoplasm; Muscle protein; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..494
FT /note="Smoothelin-like protein 1"
FT /id="PRO_0000317275"
FT DOMAIN 378..484
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 1..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..494
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT COILED 123..145
FT /evidence="ECO:0000255"
FT COMPBIAS 75..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..258
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..321
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99LM3"
SQ SEQUENCE 494 AA; 52987 MW; 2444F76AC2154D45 CRC64;
MEQKEGKLSE DGTTVSPAAD NPEMSGGGAP AEETKGTAGK AINEGPPTES GKQEKAPAED
GMSAELQGEA NGLDEVKVES QREAGGKEDA EAELKKEDGE KEETTVGSQE MTGRKEETKS
EPKEAEEKES TLASEKQKAE EKEAKPESGQ KADANDRDKP EPKATVEEED AKTASQEETG
QRKECSTEPK EKATDEEAKA ESQKAVVEDE AKAEPKEPDG KEEAKHGAKE EADAKEEAED
AEEAEPGSPS EEQEQDVEKE PEGGAGVIPS SPEEWPESPT GEGHNLSTDG LGPDCVASGQ
TSPSASESSP SDVPQSPPES PSSGEKKEKA PERRVSAPAR PRGPRAQNRK AIVDKFGGAA
SGPTALFRNT KAAGAAIGGV KNMLLEWCRA MTKKYEHVDI QNFSSSWSSG MAFCALIHKF
FPDAFDYAEL DPAKRRHNFT LAFSTAEKLA DCAQLLDVDD MVRLAVPDSK CVYTYIQELY
RSLVQKGLVK TKKK
