SMTL2_MOUSE
ID SMTL2_MOUSE Reviewed; 456 AA.
AC Q8CI12;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Smoothelin-like protein 2;
GN Name=Smtnl2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-96; SER-98; SER-126; SER-131;
RP SER-250; SER-252; SER-265; THR-270; SER-274 AND SER-339, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- SIMILARITY: Belongs to the smoothelin family. {ECO:0000305}.
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DR EMBL; BC037993; AAH37993.1; -; mRNA.
DR CCDS; CCDS24985.1; -.
DR RefSeq; NP_808444.1; NM_177776.3.
DR AlphaFoldDB; Q8CI12; -.
DR SMR; Q8CI12; -.
DR BioGRID; 234901; 4.
DR STRING; 10090.ENSMUSP00000059043; -.
DR iPTMnet; Q8CI12; -.
DR PhosphoSitePlus; Q8CI12; -.
DR jPOST; Q8CI12; -.
DR MaxQB; Q8CI12; -.
DR PaxDb; Q8CI12; -.
DR PeptideAtlas; Q8CI12; -.
DR PRIDE; Q8CI12; -.
DR ProteomicsDB; 257527; -.
DR Antibodypedia; 11245; 75 antibodies from 21 providers.
DR DNASU; 276829; -.
DR Ensembl; ENSMUST00000050226; ENSMUSP00000059043; ENSMUSG00000045667.
DR GeneID; 276829; -.
DR KEGG; mmu:276829; -.
DR UCSC; uc007jyv.1; mouse.
DR CTD; 342527; -.
DR MGI; MGI:2442764; Smtnl2.
DR VEuPathDB; HostDB:ENSMUSG00000045667; -.
DR eggNOG; KOG4678; Eukaryota.
DR GeneTree; ENSGT00940000154495; -.
DR InParanoid; Q8CI12; -.
DR OMA; APHQGER; -.
DR OrthoDB; 168604at2759; -.
DR PhylomeDB; Q8CI12; -.
DR TreeFam; TF316716; -.
DR BioGRID-ORCS; 276829; 1 hit in 72 CRISPR screens.
DR PRO; PR:Q8CI12; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8CI12; protein.
DR Bgee; ENSMUSG00000045667; Expressed in sternocleidomastoid and 153 other tissues.
DR ExpressionAtlas; Q8CI12; baseline and differential.
DR Genevisible; Q8CI12; MM.
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:0008157; F:protein phosphatase 1 binding; IBA:GO_Central.
DR GO; GO:0005523; F:tropomyosin binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0045907; P:positive regulation of vasoconstriction; IBA:GO_Central.
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 Coiled coil; Phosphoprotein; Reference proteome.
FT CHAIN 1..456
FT /note="Smoothelin-like protein 2"
FT /id="PRO_0000317279"
FT DOMAIN 346..453
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 120..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 24..88
FT /evidence="ECO:0000255"
FT COMPBIAS 154..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..282
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 96
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 270
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 456 AA; 49523 MW; A7BE34B378C2FC05 CRC64;
MEPSPDAEEA HTVREALGRY EAALEGAVRA LHEDMQGLQR GVERRVAEAL RLAGPLARTV
AELQRDNQRL QAQLERLTRQ VEALGLATGV SPAPGTPSPP PAATVTDRAP RLGTARFSSH
ATFSLSGRSP SVEHDEASDL EVRRASNSCI LENGHQLDAG PANGSSEVQT SSAQEPPRPR
PVSLSLRMPH QPVTAVTRVS EKFSGETSAS ALSPTSAAIV GGFTPSPSEA ISPWTPSPTE
KSSSFTRSLS GSGYGAVTAG KRKDSPPLVT PPQSPPSSQP PAMTQAPRQG ERRRELVRSQ
TLPRTSGAQA RKALFEKWEQ DTASKGKGET RAKLKRSQSF GVASASSIKQ ILLEWCRSKT
VGYQHVDLQN FSSSWSDGMA FCALVHSFFP DAFDYNALSP TQRQKNFELA FTMAENLANC
ERLIEVEDMM VMGRKPDPMC VFTYVQSLYN HLRRFE
