ID   SHRM3_HUMAN             Reviewed;        1996 AA.
AC   Q8TF72; Q5QTQ3; Q6ZRW3; Q96IR9; Q9P247;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 2.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=Protein Shroom3;
DE   AltName: Full=Shroom-related protein;
DE            Short=hShrmL;
GN   Name=SHROOM3; Synonyms=KIAA1481, SHRML; ORFNames=MSTP013;
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 [MRNA] (ISOFORM 1), AND VARIANTS ALA-279; ALA-469 AND
RP   LEU-1290.
RA   Koide M., Iio A., Obata K., Inagaki M., Yokota M., Ono T., Tuan R.S.;
RT   "Molecular cloning of FKBP12-associated protein.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Spleen;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 617-1996 (ISOFORM 1), AND VARIANT
RP   LEU-1290.
RX   PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA   Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:143-150(2000).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1230-1996 (ISOFORM 1).
RC   TISSUE=Colon;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1799-1996 (ISOFORM 1).
RC   TISSUE=Aorta;
RA   Hui R.T., Liu Y.Q., Liu B., Zhao B., Meng X.M., Sheng H., Xu Y.Y.,
RA   Wang X.Y., Ye J., Song L., Gao Y., Wei Y.J., Zhang C.L., Zhang J.,
RA   Chai M.Q., Chen J.Z., Sun Y.H., Zhou X.L., Jiang Y.X., Zhao X.W., Liu S.,
RA   Cao H.Q., Zhao Y., Liu D.Q., Ding J.F., Liu L.S., Gao R.L., Wu Q.Y.,
RA   Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S.;
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [7]
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910 AND SER-913, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-439; SER-443; SER-910;
RP   SER-913 AND SER-1221, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-910 AND SER-970, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [13]
RP   INTERACTION WITH ROCK1.
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).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-816; SER-890; SER-910;
RP   SER-913; SER-1221 AND SER-1441, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1441, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- FUNCTION: Controls cell shape changes in the neuroepithelium during
CC       neural tube closure. Induces apical constriction in epithelial cells by
CC       promoting the apical accumulation of F-actin and myosin II, and
CC       probably by bundling stress fibers (By similarity). Induces apicobasal
CC       cell elongation by redistributing gamma-tubulin and directing the
CC       assembly of robust apicobasal microtubule arrays (By similarity).
CC       {ECO:0000250|UniProtKB:Q27IV2, ECO:0000250|UniProtKB:Q9QXN0}.
CC   -!- SUBUNIT: Interacts with F-actin (By similarity). Interacts with ROCK1
CC       (PubMed:22493320). {ECO:0000250|UniProtKB:Q9QXN0,
CC       ECO:0000269|PubMed:22493320}.
CC   -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC       {ECO:0000250|UniProtKB:Q9QXN0}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q9QXN0}. Apical cell membrane
CC       {ECO:0000250|UniProtKB:Q9QXN0}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9QXN0}. Note=Colocalizes with F-actin in stress
CC       fibers and adherens junctions. {ECO:0000250|UniProtKB:Q9QXN0}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8TF72-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8TF72-2; Sequence=VSP_024965, VSP_024966, VSP_024967,
CC                                  VSP_024968;
CC   -!- DOMAIN: The ASD1 domain mediates F-actin binding. {ECO:0000250}.
CC   -!- DOMAIN: The ASD2 domain mediates the interaction with ROCK1 and is
CC       required for apical constriction induction.
CC       {ECO:0000250|UniProtKB:Q9QXN0}.
CC   -!- SIMILARITY: Belongs to the shroom family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator. Met-2
CC       is more conserved than Met-1 among the orthologs. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAQ13515.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB84689.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB055660; BAB84689.1; ALT_INIT; mRNA.
DR   EMBL; AK127929; BAC87195.1; -; mRNA.
DR   EMBL; AC096743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC107051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC107072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC112249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC121158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB040914; BAA96005.1; -; mRNA.
DR   EMBL; BC007291; AAH07291.1; -; mRNA.
DR   EMBL; AF109367; AAQ13515.1; ALT_INIT; mRNA.
DR   CCDS; CCDS3579.2; -. [Q8TF72-1]
DR   RefSeq; NP_065910.3; NM_020859.3. [Q8TF72-1]
DR   PDB; 6FBB; X-ray; 1.30 A; P=1240-1244.
DR   PDB; 6FCP; X-ray; 1.45 A; P=1233-1247.
DR   PDBsum; 6FBB; -.
DR   PDBsum; 6FCP; -.
DR   AlphaFoldDB; Q8TF72; -.
DR   SMR; Q8TF72; -.
DR   BioGRID; 121665; 67.
DR   IntAct; Q8TF72; 31.
DR   MINT; Q8TF72; -.
DR   STRING; 9606.ENSP00000296043; -.
DR   iPTMnet; Q8TF72; -.
DR   PhosphoSitePlus; Q8TF72; -.
DR   SwissPalm; Q8TF72; -.
DR   BioMuta; SHROOM3; -.
DR   DMDM; 300669666; -.
DR   EPD; Q8TF72; -.
DR   jPOST; Q8TF72; -.
DR   MassIVE; Q8TF72; -.
DR   MaxQB; Q8TF72; -.
DR   PaxDb; 9606-ENSP00000296043; -.
DR   PeptideAtlas; Q8TF72; -.
DR   ProteomicsDB; 74572; -. [Q8TF72-1]
DR   ProteomicsDB; 74573; -. [Q8TF72-2]
DR   Pumba; Q8TF72; -.
DR   Antibodypedia; 62376; 71 antibodies from 20 providers.
DR   DNASU; 57619; -.
DR   Ensembl; ENST00000296043.7; ENSP00000296043.6; ENSG00000138771.16. [Q8TF72-1]
DR   GeneID; 57619; -.
DR   KEGG; hsa:57619; -.
DR   MANE-Select; ENST00000296043.7; ENSP00000296043.6; NM_020859.4; NP_065910.3.
DR   UCSC; uc011cbx.3; human. [Q8TF72-1]
DR   AGR; HGNC:30422; -.
DR   CTD; 57619; -.
DR   DisGeNET; 57619; -.
DR   GeneCards; SHROOM3; -.
DR   HGNC; HGNC:30422; SHROOM3.
DR   HPA; ENSG00000138771; Low tissue specificity.
DR   MIM; 604570; gene.
DR   neXtProt; NX_Q8TF72; -.
DR   OpenTargets; ENSG00000138771; -.
DR   PharmGKB; PA147357295; -.
DR   VEuPathDB; HostDB:ENSG00000138771; -.
DR   eggNOG; ENOG502QUU2; Eukaryota.
DR   GeneTree; ENSGT00940000157778; -.
DR   HOGENOM; CLU_002434_1_0_1; -.
DR   InParanoid; Q8TF72; -.
DR   OMA; TDPLGMQ; -.
DR   OrthoDB; 4120529at2759; -.
DR   PhylomeDB; Q8TF72; -.
DR   TreeFam; TF333370; -.
DR   PathwayCommons; Q8TF72; -.
DR   SignaLink; Q8TF72; -.
DR   BioGRID-ORCS; 57619; 9 hits in 1156 CRISPR screens.
DR   ChiTaRS; SHROOM3; human.
DR   GeneWiki; SHROOM3; -.
DR   GenomeRNAi; 57619; -.
DR   Pharos; Q8TF72; Tbio.
DR   PRO; PR:Q8TF72; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q8TF72; Protein.
DR   Bgee; ENSG00000138771; Expressed in ileal mucosa and 175 other cell types or tissues.
DR   ExpressionAtlas; Q8TF72; baseline and differential.
DR   GO; GO:0005912; C:adherens junction; ISS:HGNC-UCL.
DR   GO; GO:0043296; C:apical junction complex; ISS:UniProtKB.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:HGNC-UCL.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005856; C:cytoskeleton; ISS:HGNC-UCL.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
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:0007389; P:pattern specification process; ISS:HGNC-UCL.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 6.10.250.3120; -; 1.
DR   InterPro; IPR014800; ASD1_dom.
DR   InterPro; IPR014799; ASD2_dom.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR027685; Shroom_fam.
DR   PANTHER; PTHR15012; APICAL PROTEIN/SHROOM-RELATED; 1.
DR   PANTHER; PTHR15012:SF33; PROTEIN SHROOM3; 1.
DR   Pfam; PF08688; ASD1; 1.
DR   Pfam; PF08687; ASD2; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS51306; ASD1; 1.
DR   PROSITE; PS51307; ASD2; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   Genevisible; Q8TF72; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Alternative splicing; Cell junction;
KW   Cell membrane; Cell shape; Cytoplasm; Cytoskeleton; Developmental protein;
KW   Membrane; Microtubule; Phosphoprotein; Reference proteome.
FT   CHAIN           1..1996
FT                   /note="Protein Shroom3"
FT                   /id="PRO_0000286066"
FT   DOMAIN          25..110
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          928..1030
FT                   /note="ASD1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00637"
FT   DOMAIN          1669..1957
FT                   /note="ASD2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00638"
FT   REGION          150..173
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          437..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          568..629
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          673..772
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          788..1053
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1093..1115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1137..1223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1315..1573
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1627..1665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        360..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..461
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        810..825
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1007..1031
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1362..1376
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1453..1476
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1495..1513
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1520..1554
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1630..1646
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         213
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QXN0"
FT   MOD_RES         439
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         443
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         816
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         890
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         910
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18220336,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         913
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18220336,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT   MOD_RES         970
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         1069
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QXN0"
FT   MOD_RES         1072
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QXN0"
FT   MOD_RES         1221
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1441
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         1..125
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_024965"
FT   VAR_SEQ         126..153
FT                   /note="SPEHLTSGPQHRKAAWSGGVKLRLKHRR -> MAFYSTPEYDIQLARGLLSG
FT                   MFLFATRR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_024966"
FT   VAR_SEQ         277..311
FT                   /note="ISGRERSGSMDNTSARGGLLEGMRQADIRYVKTVY -> KRVKTRDLPGSQS
FT                   PGRAISRKTTMPTSGGGWREKA (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_024967"
FT   VAR_SEQ         312..1996
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_024968"
FT   VARIANT         147
FT                   /note="L -> H (in dbSNP:rs3821979)"
FT                   /id="VAR_032062"
FT   VARIANT         279
FT                   /note="G -> A (in dbSNP:rs344140)"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="VAR_032063"
FT   VARIANT         469
FT                   /note="P -> A (in dbSNP:rs344141)"
FT                   /evidence="ECO:0000269|Ref.1"
FT                   /id="VAR_032064"
FT   VARIANT         1290
FT                   /note="P -> L (in dbSNP:rs3733242)"
FT                   /evidence="ECO:0000269|PubMed:10819331, ECO:0000269|Ref.1"
FT                   /id="VAR_032065"
FT   CONFLICT        153
FT                   /note="R -> S (in Ref. 1; BAB84689)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1996 AA;  216857 MW;  735F6CD20FF64BC6 CRC64;
     MMRTTEDFHK PSATLNSNTA TKGRYIYLEA FLEGGAPWGF TLKGGLEHGE PLIISKVEEG
     GKADTLSSKL QAGDEVVHIN EVTLSSSRKE AVSLVKGSYK TLRLVVRRDV CTDPGHADTG
     ASNFVSPEHL TSGPQHRKAA WSGGVKLRLK HRRSEPAGRP HSWHTTKSGE KQPDASMMQI
     SQGMIGPPWH QSYHSSSSTS DLSNYDHAYL RRSPDQCSSQ GSMESLEPSG AYPPCHLSPA
     KSTGSIDQLS HFHNKRDSAY SSFSTSSSIL EYPHPGISGR ERSGSMDNTS ARGGLLEGMR
     QADIRYVKTV YDTRRGVSAE YEVNSSALLL QGREARASAN GQGYDKWSNI PRGKGVPPPS
     WSQQCPSSLE TATDNLPPKV GAPLPPARSD SYAAFRHRER PSSWSSLDQK RLCRPQANSL
     GSLKSPFIEE QLHTVLEKSP ENSPPVKPKH NYTQKAQPGQ PLLPTSIYPV PSLEPHFAQV
     PQPSVSSNGM LYPALAKESG YIAPQGACNK MATIDENGNQ NGSGRPGFAF CQPLEHDLLS
     PVEKKPEATA KYVPSKVHFC SVPENEEDAS LKRHLTPPQG NSPHSNERKS THSNKPSSHP
     HSLKCPQAQA WQAGEDKRSS RLSEPWEGDF QEDHNANLWR RLEREGLGQS LSGNFGKTKS
     AFSSLQNIPE SLRRHSSLEL GRGTQEGYPG GRPTCAVNTK AEDPGRKAAP DLGSHLDRQV
     SYPRPEGRTG ASASFNSTDP SPEEPPAPSH PHTSSLGRRG PGPGSASALQ GFQYGKPHCS
     VLEKVSKFEQ REQGSQRPSV GGSGFGHNYR PHRTVSTSST SGNDFEETKA HIRFSESAEP
     LGNGEQHFKN GELKLEEASR QPCGQQLSGG ASDSGRGPQR PDARLLRSQS TFQLSSEPER
     EPEWRDRPGS PESPLLDAPF SRAYRNSIKD AQSRVLGATS FRRRDLELGA PVASRSWRPR
     PSSAHVGLRS PEASASASPH TPRERHSVTP AEGDLARPVP PAARRGARRR LTPEQKKRSY
     SEPEKMNEVG IVEEAEPAPL GPQRNGMRFP ESSVADRRRL FERDGKACST LSLSGPELKQ
     FQQSALADYI QRKTGKRPTS AAGCSLQEPG PLRERAQSAY LQPGPAALEG SGLASASSLS
     SLREPSLQPR REATLLPATV AETQQAPRDR SSSFAGGRRL GERRRGDLLS GANGGTRGTQ
     RGDETPREPS SWGARAGKSM SAEDLLERSD VLAGPVHVRS RSSPATADKR QDVLLGQDSG
     FGLVKDPCYL AGPGSRSLSC SERGQEEMLP LFHHLTPRWG GSGCKAIGDS SVPSECPGTL
     DHQRQASRTP CPRPPLAGTQ GLVTDTRAAP LTPIGTPLPS AIPSGYCSQD GQTGRQPLPP
     YTPAMMHRSN GHTLTQPPGP RGCEGDGPEH GVEEGTRKRV SLPQWPPPSR AKWAHAARED
     SLPEESSAPD FANLKHYQKQ QSLPSLCSTS DPDTPLGAPS TPGRISLRIS ESVLRDSPPP
     HEDYEDEVFV RDPHPKATSS PTFEPLPPPP PPPPSQETPV YSMDDFPPPP PHTVCEAQLD
     SEDPEGPRPS FNKLSKVTIA RERHMPGAAH VVGSQTLASR LQTSIKGSEA ESTPPSFMSV
     HAQLAGSLGG QPAPIQTQSL SHDPVSGTQG LEKKVSPDPQ KSSEDIRTEA LAKEIVHQDK
     SLADILDPDS RLKTTMDLME GLFPRDVNLL KENSVKRKAI QRTVSSSGCE GKRNEDKEAV
     SMLVNCPAYY SVSAPKAELL NKIKEMPAEV NEEEEQADVN EKKAELIGSL THKLETLQEA
     KGSLLTDIKL NNALGEEVEA LISELCKPNE FDKYRMFIGD LDKVVNLLLS LSGRLARVEN
     VLSGLGEDAS NEERSSLYEK RKILAGQHED ARELKENLDR RERVVLGILA NYLSEEQLQD
     YQHFVKMKST LLIEQRKLDD KIKLGQEQVK CLLESLPSDF IPKAGALALP PNLTSEPIPA
     GGCTFSGIFP TLTSPL
//