SHRM3_MOUSE
ID SHRM3_MOUSE Reviewed; 1986 AA.
AC Q9QXN0; Q3TNX1; Q6ZPP9; Q99L16; Q9QXM9;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Protein Shroom3;
GN Name=Shroom3; Synonyms=Kiaa1481, Shrm;
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] (ISOFORMS 1 AND 2), DEVELOPMENTAL STAGE,
RP SUBCELLULAR LOCATION, INTERACTION WITH F-ACTIN, FUNCTION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=10589677; DOI=10.1016/s0092-8674(00)81537-8;
RA Hildebrand J.D., Soriano P.;
RT "Shroom, a PDZ domain-containing actin-binding protein, is required for
RT neural tube morphogenesis in mice.";
RL Cell 99:485-497(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PROTEIN SEQUENCE OF 123-145; 257-280; 283-300 AND 1107-1141, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 255-1986 (ISOFORM 3).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
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. 10:167-180(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1506-1986 (ISOFORM 1).
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 [6]
RP FUNCTION.
RX PubMed=14680628; DOI=10.1016/j.cub.2003.11.054;
RA Haigo S.L., Hildebrand J.D., Harland R.M., Wallingford J.B.;
RT "Shroom induces apical constriction and is required for hingepoint
RT formation during neural tube closure.";
RL Curr. Biol. 13:2125-2137(2003).
RN [7]
RP FUNCTION.
RX PubMed=16249236; DOI=10.1242/jcs.02626;
RA Hildebrand J.D.;
RT "Shroom regulates epithelial cell shape via the apical positioning of an
RT actomyosin network.";
RL J. Cell Sci. 118:5191-5203(2005).
RN [8]
RP FUNCTION.
RX PubMed=16684770; DOI=10.1074/jbc.m512463200;
RA Dietz M.L., Bernaciak T.M., Vendetti F., Kielec J.M., Hildebrand J.D.;
RT "Differential actin-dependent localization modulates the evolutionarily
RT conserved activity of Shroom family proteins.";
RL J. Biol. Chem. 281:20542-20554(2006).
RN [9]
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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212; SER-439; SER-443;
RP THR-909; SER-912; SER-1063; SER-1066 AND SER-1219, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-1350 AND SER-1354 (ISOFORM 3), PHOSPHORYLATION
RP [LARGE SCALE ANALYSIS] AT SER-1175 AND SER-1179 (ISOFORM 4), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, Spleen, 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).
RN [12]
RP FUNCTION, INTERACTION WITH ROCK1, SUBCELLULAR LOCATION, DOMAIN, AND
RP MUTAGENESIS OF 1772-LYS--LEU-1776; 1838-LEU--LEU-1841; 1840-SER--ALA-1846;
RP 1884-LEU--ARG-1891 AND 1921-LEU--LEU-1928.
RX PubMed=22493320; DOI=10.1091/mbc.e11-11-0937;
RA Mohan S., Rizaldy R., Das D., Bauer R.J., Heroux A., Trakselis M.A.,
RA Hildebrand J.D., VanDemark A.P.;
RT "Structure of Shroom domain 2 reveals a three-segmented coiled-coil
RT required for dimerization, Rock binding, and apical constriction.";
RL Mol. Biol. Cell 23:2131-2142(2012).
CC -!- FUNCTION: Controls cell shape changes in the neuroepithelium during
CC neural tube closure (PubMed:10589677, PubMed:14680628). Induces apical
CC constriction in epithelial cells by promoting the apical accumulation
CC of F-actin and myosin II, and probably by bundling stress fibers
CC (PubMed:14680628, PubMed:16249236, PubMed:16684770, PubMed:22493320).
CC Induces apicobasal cell elongation by redistributing gamma-tubulin and
CC directing the assembly of robust apicobasal microtubule arrays (By
CC similarity). {ECO:0000250|UniProtKB:Q27IV2,
CC ECO:0000269|PubMed:10589677, ECO:0000269|PubMed:14680628,
CC ECO:0000269|PubMed:16249236, ECO:0000269|PubMed:16684770,
CC ECO:0000269|PubMed:22493320}.
CC -!- SUBUNIT: Interacts with F-actin (PubMed:10589677). Interacts with ROCK1
CC (PubMed:22493320). {ECO:0000269|PubMed:10589677,
CC ECO:0000269|PubMed:22493320}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000269|PubMed:10589677}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:10589677}. Apical cell membrane
CC {ECO:0000269|PubMed:22493320}; Peripheral membrane protein
CC {ECO:0000305}. Note=Colocalizes with F-actin in stress fibers and
CC adherens junctions.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=L,a;
CC IsoId=Q9QXN0-1; Sequence=Displayed;
CC Name=2; Synonyms=S,b;
CC IsoId=Q9QXN0-2; Sequence=VSP_024969;
CC Name=3;
CC IsoId=Q9QXN0-3; Sequence=VSP_024970;
CC Name=4;
CC IsoId=Q9QXN0-4; Sequence=VSP_024969, VSP_024970;
CC -!- DEVELOPMENTAL STAGE: At 8.75 dpc, strongly expressed in the cranial
CC neuroepithelium, and also expressed in neural tube, paraxial mesoderm
CC and gut. At 10.5 dpc, expressed in neural tube, forebrain, somites,
CC ventral body wall, heart and gut. At 14.5 dpc, expression is restricted
CC to skeletal muscle, tips of the digits and forebrain.
CC {ECO:0000269|PubMed:10589677}.
CC -!- DOMAIN: The ASD1 domain mediates F-actin binding.
CC -!- DOMAIN: The ASD2 domain mediates the interaction with ROCK1 and is
CC required for apical constriction induction.
CC {ECO:0000269|PubMed:22493320}.
CC -!- DISRUPTION PHENOTYPE: Death at birth due to defects in neural tube
CC closure causing exencephaly, acrania, facial clefting and spina bifida.
CC {ECO:0000269|PubMed:10589677}.
CC -!- SIMILARITY: Belongs to the shroom family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF13269.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF13270.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF199421; AAF13269.1; ALT_FRAME; mRNA.
DR EMBL; AF199422; AAF13270.1; ALT_FRAME; mRNA.
DR EMBL; AK147493; BAE27948.1; -; mRNA.
DR EMBL; AK164918; BAE37966.1; -; mRNA.
DR EMBL; AK129371; BAC98181.1; -; mRNA.
DR EMBL; BC003909; AAH03909.1; -; mRNA.
DR CCDS; CCDS39154.1; -. [Q9QXN0-3]
DR CCDS; CCDS39155.1; -. [Q9QXN0-4]
DR RefSeq; NP_001071063.1; NM_001077595.2.
DR RefSeq; NP_001071064.1; NM_001077596.2.
DR RefSeq; NP_056571.2; NM_015756.2.
DR RefSeq; XP_006535031.1; XM_006534968.2.
DR AlphaFoldDB; Q9QXN0; -.
DR SMR; Q9QXN0; -.
DR BioGRID; 205229; 5.
DR IntAct; Q9QXN0; 1.
DR STRING; 10090.ENSMUSP00000108678; -.
DR iPTMnet; Q9QXN0; -.
DR PhosphoSitePlus; Q9QXN0; -.
DR MaxQB; Q9QXN0; -.
DR PaxDb; Q9QXN0; -.
DR PeptideAtlas; Q9QXN0; -.
DR PRIDE; Q9QXN0; -.
DR ProteomicsDB; 255419; -. [Q9QXN0-1]
DR ProteomicsDB; 255420; -. [Q9QXN0-2]
DR ProteomicsDB; 255421; -. [Q9QXN0-3]
DR ProteomicsDB; 255422; -. [Q9QXN0-4]
DR DNASU; 27428; -.
DR GeneID; 27428; -.
DR KEGG; mmu:27428; -.
DR CTD; 57619; -.
DR MGI; MGI:1351655; Shroom3.
DR eggNOG; ENOG502QUU2; Eukaryota.
DR InParanoid; Q9QXN0; -.
DR OrthoDB; 29607at2759; -.
DR PhylomeDB; Q9QXN0; -.
DR BioGRID-ORCS; 27428; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Shroom3; mouse.
DR PRO; PR:Q9QXN0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9QXN0; protein.
DR GO; GO:0005912; C:adherens junction; IDA:MGI.
DR GO; GO:0043296; C:apical junction complex; IDA:MGI.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IDA:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IGI:MGI.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0045176; P:apical protein localization; ISS:HGNC-UCL.
DR GO; GO:0000902; P:cell morphogenesis; ISS:HGNC-UCL.
DR GO; GO:0043482; P:cellular pigment accumulation; ISS:HGNC-UCL.
DR GO; GO:0002066; P:columnar/cuboidal epithelial cell development; IDA:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0007389; P:pattern specification process; IMP:MGI.
DR GO; GO:0008360; P:regulation of cell shape; IDA:MGI.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR014800; ASD1_dom.
DR InterPro; IPR014799; ASD2_dom.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR030494; Shrm3.
DR InterPro; IPR027685; Shroom_fam.
DR PANTHER; PTHR15012; PTHR15012; 1.
DR PANTHER; PTHR15012:SF33; PTHR15012:SF33; 1.
DR Pfam; PF08688; ASD1; 1.
DR Pfam; PF08687; ASD2; 1.
DR Pfam; PF00595; PDZ; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS51306; ASD1; 1.
DR PROSITE; PS51307; ASD2; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell junction; Cell membrane;
KW Cell shape; Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein;
KW Direct protein sequencing; Membrane; Microtubule; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1986
FT /note="Protein Shroom3"
FT /id="PRO_0000286067"
FT DOMAIN 24..109
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 927..1023
FT /note="ASD1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00637"
FT DOMAIN 1659..1947
FT /note="ASD2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00638"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1083..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1446..1654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1844..1890
FT /evidence="ECO:0000255"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1361..1399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1452..1480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1509..1543
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1582..1634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1637..1654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 888
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TF72"
FT MOD_RES 909
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 912
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 969
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TF72"
FT MOD_RES 1063
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1066
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..175
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10589677,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_024969"
FT VAR_SEQ 1354..1359
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_024970"
FT MUTAGEN 1772..1776
FT /note="KKAEL->AKARA: Does not affect binding to ROCK1."
FT MUTAGEN 1838..1841
FT /note="LLSL->AASA: Loss of dimerization, binding to ROCK1
FT and ability to trigger apical constriction in cells."
FT /evidence="ECO:0000269|PubMed:22493320"
FT MUTAGEN 1840..1846
FT /note="SLSGRLA->ALEADLE: Reduces binding to ROCK1 and
FT ability to trigger apical constriction in cells."
FT /evidence="ECO:0000269|PubMed:22493320"
FT MUTAGEN 1884..1891
FT /note="LKENLDRR->AAENLDDA: Loss of binding to ROCK1 and
FT ability to trigger apical constriction in cells."
FT /evidence="ECO:0000269|PubMed:22493320"
FT MUTAGEN 1921..1928
FT /note="LLIEQRKL->ALIEQAKA: Loss of dimerization, binding to
FT ROCK1 and ability to trigger apical constriction in cells."
FT /evidence="ECO:0000269|PubMed:22493320"
FT CONFLICT 409
FT /note="Q -> H (in Ref. 1; AAF13270/AAF13269)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="R -> K (in Ref. 1; AAF13270/AAF13269)"
FT /evidence="ECO:0000305"
FT CONFLICT 683
FT /note="Q -> P (in Ref. 4; BAC98181)"
FT /evidence="ECO:0000305"
FT CONFLICT 800
FT /note="Y -> N (in Ref. 1; AAF13270/AAF13269)"
FT /evidence="ECO:0000305"
FT CONFLICT 1078
FT /note="S -> N (in Ref. 1; AAF13270/AAF13269)"
FT /evidence="ECO:0000305"
FT CONFLICT 1239
FT /note="R -> K (in Ref. 1; AAF13270/AAF13269)"
FT /evidence="ECO:0000305"
FT CONFLICT 1293
FT /note="P -> H (in Ref. 1; AAF13270/AAF13269)"
FT /evidence="ECO:0000305"
FT CONFLICT 1318
FT /note="A -> S (in Ref. 4; BAC98181)"
FT /evidence="ECO:0000305"
FT CONFLICT 1397
FT /note="P -> L (in Ref. 1; AAF13270/AAF13269)"
FT /evidence="ECO:0000305"
FT CONFLICT 1407..1408
FT /note="GE -> EK (in Ref. 4; BAC98181)"
FT /evidence="ECO:0000305"
FT CONFLICT 1419
FT /note="R -> Q (in Ref. 4; BAC98181)"
FT /evidence="ECO:0000305"
FT CONFLICT 1423
FT /note="P -> L (in Ref. 4; BAC98181)"
FT /evidence="ECO:0000305"
FT CONFLICT 1457
FT /note="R -> L (in Ref. 4; BAC98181)"
FT /evidence="ECO:0000305"
FT CONFLICT 1770
FT /note="N -> Y (in Ref. 1; AAF13270/AAF13269)"
FT /evidence="ECO:0000305"
FT CONFLICT 1967
FT /note="A -> G (in Ref. 2; BAE27948/BAE37966)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9QXN0-3:1350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q9QXN0-3:1354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q9QXN0-4:1175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q9QXN0-4:1179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1986 AA; 214888 MW; 52C7A4AF6390D547 CRC64;
MKTPENLEEP SATPNPSRTP TERFVYLEAL LEGGAPWGFT LKGGLERGEP LIISKIEEGG
KADSVSSGLQ AGDEVIHINE VALSSPRREA VSLVKGSYKT LRLVVRRDVC AAPGHADPGT
SKSLSSELLT CSPQHRKATW SGGVKLRLKQ RCSEPATRPH SWHTTKFGET QPDVSMMQIS
QGTMGPPWHQ SYHSSSSTSD LSNYDHAYLR RSPDQCSSQG SMESLEPSGG YPPCHLLSPA
KSTSSIDQLG HLHNKRDSAY SSFSTSSSIF EYPPPGGSAR ERSGSMDVIS ARGGLLEGMR
QADIRYVKTV YDTRRGVSSE YEVNPSALLL QGRDAHASAD SQGCAKWHSI PRGKGTPSPS
WSQQCSGSLE TATDNLPQKA GAPLPPTRSD SYAAFRHRER PSSWSSLDQK RFCRPQTNSS
GSQKTPFAED QLHTVPERSP ENSPPVKSKH NYTQKAQPGQ PLLPTGIYPV PSPEPHFAQV
PQPSVSSNGT VYPALVKESG YTAAQGTCNK MATLDENGNQ NEASRPGFAF CQPLEHNSVT
PVEKRPEPTA KYIYKVHFSS VPENEDSSLK RHITPPHGHS PYPSERKNIH GGSRACSNHH
SLSSPQAQAL HVGDDRRPSR LSQPWEGDFQ EDHNANLRQK VEREGQGQGL SGNSGRTRSA
FSSLQNIPES LRRQSNVELG EAQEVHPGGR SKVEDPGRKA GASDIRGYLD RSVSYPRPEG
KMNAVDSVHS ADSRYEESPA PALPQTSGAS QRRLSSSSSA APQYRKPHCS VLEKVSRIEE
REQGRHRPLS VGSSAYGPGY RPGRTGPTPS TSSSDLDDPK AGSVHFSEST EHLRNGEQNP
PNGEAKQEEA SRPQCSHLIR RAPADGRGPP ARGGEPSRPE ARLLRSQSTF QLYSEAEREA
SWSEDRPGTP ESPLLDAPFS RAYRNSIKDA QSRVLGATSF RRRDLEPGTP ATSRPWRPRP
ASAHVGMRSP EAAVPSSSPH TPRERHSVTP AAPQAARRGP RRRLTVEQKK RSYSEPEKMN
EVGVSEEAEP TPCGPPRPAQ PRFSESTVAD RRRIFERDGK ACSTLSLSGP ELKQFQQSAL
ADYIQRKTGK RPTGAACTPE AGLRERAQSA YLQAGPAAPD GPGLASACSL SSLREPEALP
RKEHTHPSAA DGPQAPRDRS SSFASGRLVG ERRRWDPQVP RQLLSGANCE PRGVQRMDGA
PGGPPSWGMV AGKAGKSKSA EDLLERSDTL AVPVHVRSRS SPTSDKKGQD VLLREGSNFG
FVKDPCCLAG PGPRSLSCSD KGQNELALPL HHPTPCWNGS GCKATVASSA PPESSGAADH
LKQRRAPGPR PLSAGMHGHF PDARAASLSS PLPSPVPSAS PVPSSYRSQL AMDQQTGQQP
PSSPASAVTQ PTSPRSPELS SPAYGLGEGM WKRTSLPQRP PPPWVKWAHA VREDGLAEDT
LAPEFANLKH YRNQPSRPSS CSTSDPDTPG RISLRISESA LQPSPPPRGD YDDEVFMKDL
HPKVTSSPTF EALPPPPPPS PPSEEPLVNG TDDFPPPPPP QALCEVLLDG EASTEAGSGP
CRIPRVMVTR EGHVPGAAHS EGSQIMTATP PQTSAKGSEA ESNTPSSASA QPQLNGSPGK
QLCPSQTRNL TYEPVERTQD LGKKTHAEPQ KTSEDIRTEA LAKEIVHQDK SLADILDPDS
RMKTTMDLME GLFPGDASVL MDSGAKRKAL DITARRAGCE AKASDHKEAV SVLVNCPAYY
SVSAAKAELL NKIKDMPEEL QEEEGQEDVN EKKAELIGSL THKLESLQEA KGSLLTDIKL
NNALGEEVEA LISELCKPNE FDKYKMFIGD LDKVVNLLLS LSGRLARVEN VLRGLGEDAS
KEERSSLNEK RKVLAGQHED ARELKENLDR RERVVLDILA NYLSAEQLQD YQHFVKMKST
LLIEQRKLDD KIKLGQEQVR CLLESLPSDF RPKAGAISLP PALTGHATPG GTSVFGGVFP
TLTSPL
