SHRM1_MOUSE
ID SHRM1_MOUSE Reviewed; 823 AA.
AC Q5SX79; B1AQY5; B1AQY6; Q5SX83; Q99JP8;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Protein Shroom1;
GN Name=Shroom1;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103; THR-383 AND SER-385, AND
RP IDENTIFICATION BY 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-383 AND SER-385, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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 -!- FUNCTION: May be involved in the assembly of microtubule arrays during
CC cell elongation. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with F-actin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5SX79-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SX79-2; Sequence=VSP_024963;
CC -!- DOMAIN: The ASD1 domain mediates F-actin binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the shroom family. {ECO:0000305}.
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DR EMBL; AL596095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005761; AAH05761.1; -; mRNA.
DR EMBL; BC031598; AAH31598.1; -; mRNA.
DR CCDS; CCDS24680.2; -. [Q5SX79-1]
DR CCDS; CCDS70182.1; -. [Q5SX79-2]
DR RefSeq; NP_001277718.1; NM_001290789.1. [Q5SX79-2]
DR RefSeq; NP_082193.2; NM_027917.3. [Q5SX79-1]
DR AlphaFoldDB; Q5SX79; -.
DR SMR; Q5SX79; -.
DR BioGRID; 214917; 1.
DR STRING; 10090.ENSMUSP00000104641; -.
DR iPTMnet; Q5SX79; -.
DR PhosphoSitePlus; Q5SX79; -.
DR MaxQB; Q5SX79; -.
DR PaxDb; Q5SX79; -.
DR PRIDE; Q5SX79; -.
DR ProteomicsDB; 257160; -. [Q5SX79-1]
DR ProteomicsDB; 257161; -. [Q5SX79-2]
DR Antibodypedia; 64246; 54 antibodies from 21 providers.
DR DNASU; 71774; -.
DR Ensembl; ENSMUST00000018531; ENSMUSP00000018531; ENSMUSG00000018387. [Q5SX79-2]
DR Ensembl; ENSMUST00000109013; ENSMUSP00000104641; ENSMUSG00000018387. [Q5SX79-1]
DR GeneID; 71774; -.
DR KEGG; mmu:71774; -.
DR UCSC; uc007iwc.2; mouse. [Q5SX79-1]
DR UCSC; uc007iwd.2; mouse. [Q5SX79-2]
DR CTD; 134549; -.
DR MGI; MGI:1919024; Shroom1.
DR VEuPathDB; HostDB:ENSMUSG00000018387; -.
DR eggNOG; ENOG502SM3B; Eukaryota.
DR GeneTree; ENSGT00940000160656; -.
DR HOGENOM; CLU_016932_0_0_1; -.
DR InParanoid; Q5SX79; -.
DR OMA; EHPLHEH; -.
DR OrthoDB; 729991at2759; -.
DR PhylomeDB; Q5SX79; -.
DR TreeFam; TF335754; -.
DR BioGRID-ORCS; 71774; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Shroom1; mouse.
DR PRO; PR:Q5SX79; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SX79; protein.
DR Bgee; ENSMUSG00000018387; Expressed in ectoplacental cone and 70 other tissues.
DR ExpressionAtlas; Q5SX79; baseline and differential.
DR Genevisible; Q5SX79; MM.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0043296; C:apical junction complex; IBA:GO_Central.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0045159; F:myosin II binding; IDA:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IDA:UniProtKB.
DR InterPro; IPR014800; ASD1_dom.
DR InterPro; IPR014799; ASD2_dom.
DR InterPro; IPR027685; Shroom_fam.
DR PANTHER; PTHR15012; PTHR15012; 2.
DR Pfam; PF08688; ASD1; 1.
DR Pfam; PF08687; ASD2; 1.
DR PROSITE; PS51306; ASD1; 1.
DR PROSITE; PS51307; ASD2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Microtubule; Phosphoprotein; Reference proteome.
FT CHAIN 1..823
FT /note="Protein Shroom1"
FT /id="PRO_0000286062"
FT DOMAIN 145..233
FT /note="ASD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00637"
FT DOMAIN 517..796
FT /note="ASD2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00638"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q2M3G4"
FT MOD_RES 103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2M3G4"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2M3G4"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2M3G4"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2M3G4"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2M3G4"
FT MOD_RES 383
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 385
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 332..394
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024963"
SQ SEQUENCE 823 AA; 89951 MW; 1CD4FAEB0D7E86E2 CRC64;
MEALGTGRDR TSQASATESL DLRRLSTRAD SAYSSFSTAS GDPETRTPSP GTERLPYLDW
DYVRVVWGSQ SPTSKDAVLS TTQRPVQAVA GHSDPRSPEV QGSPGPLNRQ DTPLLYALAA
EAEATAHTAE PPSPPASRDA YRQRLQGAQR RVLRETSFQR KEFRMSLPGR LRPAVPTRLP
TAHVRSASSS QELGEEEPAR TAVPALAAAG RGRLSSQQRQ CCFSEPGKLH RVGWSGGPTG
EDLRKDYSTQ ELQRGMHAKS KGLLETQSLS STELNSGPAD LGNAHRPAGR SQSVSGEVMG
PCKGSERTVA TVQAVPQRAD IRRPLLHTKL SRSLTQKEVT GVCPGEALQT KPAGCGRRIS
ETSVSTPGPS LPEDDVFLRE AKTPSPQDSQ GLPTSTSYRQ YENDLSKKAG QIAVSAERPL
HETPGITGTE DCGQAVNGSV DLSRPTSIPE TTNDDIPTFD TNGTTDPSAA TEKKPLKPPP
VDVLRPSDSE TPGSPHHTSL TWGQFDSKTT WPSRHFEALV QELARLDPSL SRTLAAQPGP
EPPQGLLDGL FPVEEIRSAM RPALEEMGEK AAGASEEGSC GHHLTQDLQT SQEASRSENS
TPDPDQSSGQ EFPEGNSTQA KKVELARLLQ KMLQDLHAEQ ERLRGTAADW TQRNGALEAA
VSQACTPREL ERFRRFMTDL ERVLGLLLLL GSRLVRVNLA LARAGSNSDP DERASLLQRL
QLLQRQQEEA KELKEHVARR EQTLRQVLER ELPAEHLRSY CVLLASKARI LSQQRSLDDR
IRFLKDQLDT IWSDLSHHPL SPRLTWAPAI RPLNKQPFLA TLI
