SHRM4_MOUSE
ID SHRM4_MOUSE Reviewed; 1475 AA.
AC Q1W617; A2ADV9; B2RX74; Q69ZN9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Protein Shroom4;
GN Name=Shroom4; Synonyms=Kiaa1202;
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION
RP WITH F-ACTIN, FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=BALB/cJ, and C57BL/6J;
RX PubMed=17009331; DOI=10.1002/cm.20167;
RA Yoder M., Hildebrand J.D.;
RT "Shroom4 (Kiaa1202) is an actin-associated protein implicated in
RT cytoskeletal organization.";
RL Cell Motil. Cytoskeleton 64:49-63(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreatic islet;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [5]
RP NOMENCLATURE.
RX PubMed=16615870; DOI=10.1186/1471-2121-7-18;
RA Hagens O., Ballabio A., Kalscheuer V., Kraehenbuhl J.-P., Schiaffino M.V.,
RA Smith P., Staub O., Hildebrand J.D., Wallingford J.B.;
RT "A new standard nomenclature for proteins related to Apx and Shroom.";
RL BMC Cell Biol. 7:18-18(2006).
RN [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16249884; DOI=10.1007/s00439-005-0072-2;
RA Hagens O., Dubos A., Abidi F., Barbi G., Van Zutven L., Hoeltzenbein M.,
RA Tommerup N., Moraine C., Fryns J.-P., Chelly J., van Bokhoven H., Gecz J.,
RA Dollfus H., Ropers H.-H., Schwartz C.E., de Cassia Stocco Dos Santos R.,
RA Kalscheuer V., Hanauer A.;
RT "Disruptions of the novel KIAA1202 gene are associated with X-linked mental
RT retardation.";
RL Hum. Genet. 118:578-590(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412; SER-722 AND SER-1010,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, and Lung;
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: Probable regulator of cytoskeletal architecture that plays an
CC important role in development. May regulate cellular and cytoskeletal
CC architecture by modulating the spatial distribution of myosin II.
CC {ECO:0000269|PubMed:17009331}.
CC -!- SUBUNIT: Interacts directly with F-actin.
CC {ECO:0000269|PubMed:17009331}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17009331}. Note=Shows partial colocalization with
CC the cytoplasmic pool of F-actin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q1W617-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q1W617-2; Sequence=VSP_025291;
CC -!- TISSUE SPECIFICITY: Detected in most adult tissues examined. Expressed
CC in brain, lung, heart, liver, kidney, muscle and ovary. Expressed
CC throughout the brain, with high expression in the brain stem and
CC cerebellum and weaker expression in the hypothalamus, the hippocampus
CC and the olfactory bulb. Expressed in wide range of cell types during
CC developpment, including vascular endothelium and the polarized
CC epithelium of the neural tube and kidney. {ECO:0000269|PubMed:16249884,
CC ECO:0000269|PubMed:17009331}.
CC -!- DEVELOPMENTAL STAGE: Slight expression at 8.5 dpc, increasing till 11.5
CC dpc and remaining continuous thereafter, suggesting regulated
CC expression during development. {ECO:0000269|PubMed:16249884}.
CC -!- SIMILARITY: Belongs to the shroom family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32407.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ435686; ABD98016.1; -; mRNA.
DR EMBL; DQ435687; ABD98017.1; -; mRNA.
DR EMBL; AK173129; BAD32407.1; ALT_INIT; mRNA.
DR EMBL; AL671501; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC151022; AAI51023.1; -; mRNA.
DR CCDS; CCDS29959.1; -. [Q1W617-1]
DR CCDS; CCDS85744.1; -. [Q1W617-2]
DR RefSeq; NP_001035549.1; NM_001040459.2. [Q1W617-1]
DR RefSeq; NP_001300693.1; NM_001313764.1.
DR RefSeq; NP_001300694.1; NM_001313765.1. [Q1W617-2]
DR AlphaFoldDB; Q1W617; -.
DR SMR; Q1W617; -.
DR STRING; 10090.ENSMUSP00000100070; -.
DR iPTMnet; Q1W617; -.
DR PhosphoSitePlus; Q1W617; -.
DR jPOST; Q1W617; -.
DR MaxQB; Q1W617; -.
DR PaxDb; Q1W617; -.
DR PeptideAtlas; Q1W617; -.
DR PRIDE; Q1W617; -.
DR ProteomicsDB; 257226; -. [Q1W617-1]
DR ProteomicsDB; 257227; -. [Q1W617-2]
DR Antibodypedia; 532; 13 antibodies from 8 providers.
DR Ensembl; ENSMUST00000089520; ENSMUSP00000086949; ENSMUSG00000068270. [Q1W617-2]
DR Ensembl; ENSMUST00000103005; ENSMUSP00000100070; ENSMUSG00000068270. [Q1W617-1]
DR GeneID; 208431; -.
DR KEGG; mmu:208431; -.
DR UCSC; uc009sky.1; mouse. [Q1W617-1]
DR CTD; 57477; -.
DR MGI; MGI:2685570; Shroom4.
DR VEuPathDB; HostDB:ENSMUSG00000068270; -.
DR eggNOG; ENOG502QUU2; Eukaryota.
DR GeneTree; ENSGT00940000159479; -.
DR HOGENOM; CLU_003220_1_1_1; -.
DR InParanoid; Q1W617; -.
DR OMA; LHCSDFD; -.
DR OrthoDB; 29607at2759; -.
DR PhylomeDB; Q1W617; -.
DR TreeFam; TF333370; -.
DR BioGRID-ORCS; 208431; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Shroom4; mouse.
DR PRO; PR:Q1W617; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q1W617; protein.
DR Bgee; ENSMUSG00000068270; Expressed in placenta labyrinth and 178 other tissues.
DR ExpressionAtlas; Q1W617; baseline and differential.
DR Genevisible; Q1W617; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:MGI.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0009925; C:basal plasma membrane; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:HGNC.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:MGI.
DR GO; GO:0045159; F:myosin II binding; IDA:MGI.
DR GO; GO:0007015; P:actin filament organization; IDA:MGI.
DR GO; GO:0007420; P:brain development; ISO:MGI.
DR GO; GO:0050890; P:cognition; ISO:MGI.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR014799; ASD2_dom.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR027687; Shroom4.
DR InterPro; IPR027685; Shroom_fam.
DR PANTHER; PTHR15012; PTHR15012; 1.
DR PANTHER; PTHR15012:SF35; PTHR15012:SF35; 1.
DR Pfam; PF08687; ASD2; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS51307; ASD2; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Phosphoprotein; Reference proteome.
FT CHAIN 1..1475
FT /note="Protein Shroom4"
FT /id="PRO_0000287078"
FT DOMAIN 10..92
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1190..1469
FT /note="ASD2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00638"
FT REGION 151..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1022..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1380..1470
FT /evidence="ECO:0000255"
FT COMPBIAS 151..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..748
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 722
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1010
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..116
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_025291"
SQ SEQUENCE 1475 AA; 163238 MW; ACDB38FAB87F48B9 CRC64;
MESRPGSFQY VPVQLQGGAP WGFTLKGGLE HCEPLTVSKI EDGGKAALSQ KMRTGDELVN
INGTPLYGSR QEALILIKGS FRILKLIVRR RNTPVSRPHS WHVAKLLEGC PDVATTMHFP
SEAFSLSWHS GCNTSDVSVQ WCPLSRHCST EKSSSIGSME SLEQPGQPTY EGHLLPIDQN
MYPSQRDSAY SSFSASSNAS DCALSLKPEE PPSTDCVMPG PGPIKVTDDQ ANVSENSGSS
HSTSEDHVTS TSHASSYSDE GHHSGPAKMA RGPPEPPVRS DSLPASRAQL LNGEQHRASE
PVDSLPQKEK PGLETVLPPR SSNQFCCLSG QDQVTDEDHQ NCELSKPSES SQDDCEHLLI
EDSSKALDSP KAHDKGSNKE FGLLKEASAD LANTLNFGAI PHLRGTMEHR HSAPEQLLAS
HLQQVHLDSR GSKGMELPIG QDGHQWTVSP LHNNPKGKKS PSLPTGGTQD QTRKERKTTP
LDDKLMASVH QSQSDVLLGE VDGHPNRAGR ASSDLTSQQP SATCSSVQQT RDFLSAHKIV
DHTEASEEGD NEPKECGRLG GRRSGGPRGR SIQNRRRSER FATNLRNEIQ RRKAQLQKSK
GPLSQLCDTN EAVEETQEPP ESPPLSASNA SLLPSYKNVP SPGDKVFNKS MILRARSSEC
LSQASESSKA RGGVEGRMSP GQRSGQSSLA LNTWWKASDS STLDTEKANA HHGVCRGHWR
WSPEHNAQPQ VALSTEAPSN PDDSKELKTS TPQAGEEAVL MPFADRRKFF EESSKSLSTS
HLPGLTTHNN KPFIQRQKPI DQNFQSVSYR DLRCHPLDQS YHSADQSYHA ADQSYHSLSP
LQSETPTYPE CFATKGRDNS LCCKPVHHGD CDYHRTCSHP CSAQGTVRHD PCICCSGEIC
PALLKRNLLP KCHNCRCHHH QCIRCTGCCH GPQHSAHEDS SMAPGNAWKS RKAAIQEFPV
DKWKPITGNR KTSHSGREMA HSKAGFSLST PFRPCIENPA LDLSNYRAVS SLDILGDFKR
ASNKPEESSV YEDENSVASM PRPLRSRAFS ESHISLEPQN TQAWGKHQRE SFSKGSETQP
DTLGARKKVF PPPRPPPPNW EKYRLFRAAQ LQQQQQQQQQ QQQQQRCEEE EEKEQEEEGE
KEEDLPPQYF SSELTGSCAP NTEEQPQSLK MGHQEASRQG SQSLQEQEAF ALHPSNFVPP
VRGCTVPQPE KAQHPCYYGT HGLWRTTEQE ATVTPKQEFQ HFSPPKGASG IPTSYSAYYN
ISVAKAELLN KLKQQPEMAE AGLGEEGVDY ELAQKKIQLI ESISRKLSVL REAQRGLLDD
INANAALGEE VEANLKAVCK SNEFEKYHLF IGDLDKVVNL LLSLSGRLAR VENALNSIDS
ESNQEKLVLI EKKQQLTNQL ADAKELKEHV DGREKLVFGM VSRYLPQDQL QDYQHFVKMK
SALIIEQREL EEKIKLGEEQ LKCLKESLHL GPSNF
