ID   SHRM4_HUMAN             Reviewed;        1493 AA.
AC   Q9ULL8; A7E2X9; D6RFW0; Q96LA0;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 3.
DT   24-JAN-2024, entry version 155.
DE   RecName: Full=Protein Shroom4;
DE   AltName: Full=Second homolog of apical protein;
GN   Name=SHROOM4; Synonyms=KIAA1202, SHAP;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA   Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XV. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:337-345(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-839 (ISOFORM 2).
RC   TISSUE=Heart;
RA   Patzak D.;
RT   "5'-sequence of TATA-box dependent expression forms of the human SHAP
RT   gene.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
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   FUNCTION, AND SUBCELLULAR LOCATION.
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   [7]
RP   STRUCTURE BY NMR OF 6-93.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the PDZ domain from human Shroom family member 4.";
RL   Submitted (AUG-2007) to the PDB data bank.
RN   [8]
RP   VARIANT LEU-1089, CHROMOSOMAL TRANSLOCATION WITH FBXO25, SUBCELLULAR
RP   LOCATION, AND TISSUE SPECIFICITY.
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   [9]
RP   VARIANT PHE-1367.
RX   PubMed=24700572; DOI=10.1002/ajmg.a.36508;
RA   Barboza-Cerda M.C., Wong L.J., Martinez-de-Villarreal L.E., Zhang V.W.,
RA   Dector M.A.;
RT   "A novel EBP c.224T>A mutation supports the existence of a male-specific
RT   disorder independent of CDPX2.";
RL   Am. J. Med. Genet. A 164A:1642-1647(2014).
RN   [10]
RP   VARIANT SER-627.
RX   PubMed=26522270; DOI=10.1038/srep16022;
RA   Casey J.P., Stoeve S.I., McGorrian C., Galvin J., Blenski M., Dunne A.,
RA   Ennis S., Brett F., King M.D., Arnesen T., Lynch S.A.;
RT   "NAA10 mutation causing a novel intellectual disability syndrome with Long
RT   QT due to N-terminal acetyltransferase impairment.";
RL   Sci. Rep. 5:16022-16022(2015).
RN   [11]
RP   VARIANT TRP-146.
RX   PubMed=26740508; DOI=10.1136/jmedgenet-2015-103568;
RA   Lopes F., Barbosa M., Ameur A., Soares G., de Sa J., Dias A.I.,
RA   Oliveira G., Cabral P., Temudo T., Calado E., Cruz I.F., Vieira J.P.,
RA   Oliveira R., Esteves S., Sauer S., Jonasson I., Syvaenen A.C.,
RA   Gyllensten U., Pinto D., Maciel P.;
RT   "Identification of novel genetic causes of Rett syndrome-like phenotypes.";
RL   J. Med. Genet. 53:190-199(2016).
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 (By
CC       similarity). {ECO:0000250, ECO:0000269|PubMed:16684770}.
CC   -!- SUBUNIT: Interacts directly with F-actin. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:16249884, ECO:0000269|PubMed:16684770}. Note=Shows
CC       partial colocalization with the cytoplasmic pool of F-actin.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=SHAP-B;
CC         IsoId=Q9ULL8-1; Sequence=Displayed;
CC       Name=2; Synonyms=SHAP-A;
CC         IsoId=Q9ULL8-2; Sequence=VSP_025290;
CC   -!- TISSUE SPECIFICITY: Expressed in all fetal and adult tissues
CC       investigated. Expressed in adult heart, brain, placenta, lung, liver,
CC       skeletal muscle, kidney and pancreas. In brain regions detected in
CC       cerebellum, cerebral cortex, medulla, spinal cord, occipital pole,
CC       frontal lobe, temporal lobe and putamen. The expression is strongest in
CC       the medulla and weakest in the cerebral cortex.
CC       {ECO:0000269|PubMed:16249884}.
CC   -!- DISEASE: Note=A chromosomal aberration involving SHROOM4 is a cause of
CC       X-linked intellectual disability (XLID). Translocation
CC       t(X;8)(p11.22;p23.3) with FBXO25.
CC   -!- DISEASE: Note=A chromosomal aberration involving SHROOM4 is a cause of
CC       X-linked intellectual disability (XLID). Translocation t(X;19).
CC   -!- SIMILARITY: Belongs to the shroom family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA86516.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB033028; BAA86516.1; ALT_INIT; mRNA.
DR   EMBL; AL121865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL445491; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL359272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC151240; AAI51241.1; -; mRNA.
DR   EMBL; AY044234; AAK95579.1; -; mRNA.
DR   CCDS; CCDS35277.1; -. [Q9ULL8-1]
DR   RefSeq; NP_065768.2; NM_020717.3. [Q9ULL8-1]
DR   PDB; 2EDP; NMR; -; A=6-92.
DR   PDBsum; 2EDP; -.
DR   AlphaFoldDB; Q9ULL8; -.
DR   SMR; Q9ULL8; -.
DR   BioGRID; 121547; 3.
DR   IntAct; Q9ULL8; 1.
DR   STRING; 9606.ENSP00000365188; -.
DR   GlyGen; Q9ULL8; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9ULL8; -.
DR   PhosphoSitePlus; Q9ULL8; -.
DR   BioMuta; SHROOM4; -.
DR   DMDM; 313104187; -.
DR   EPD; Q9ULL8; -.
DR   jPOST; Q9ULL8; -.
DR   MassIVE; Q9ULL8; -.
DR   MaxQB; Q9ULL8; -.
DR   PaxDb; 9606-ENSP00000365188; -.
DR   PeptideAtlas; Q9ULL8; -.
DR   ProteomicsDB; 85073; -. [Q9ULL8-1]
DR   ProteomicsDB; 85074; -. [Q9ULL8-2]
DR   Antibodypedia; 532; 25 antibodies from 8 providers.
DR   DNASU; 57477; -.
DR   Ensembl; ENST00000289292.11; ENSP00000289292.7; ENSG00000158352.18. [Q9ULL8-1]
DR   Ensembl; ENST00000376020.9; ENSP00000365188.2; ENSG00000158352.18. [Q9ULL8-1]
DR   Ensembl; ENST00000460112.3; ENSP00000421450.1; ENSG00000158352.18. [Q9ULL8-2]
DR   GeneID; 57477; -.
DR   KEGG; hsa:57477; -.
DR   MANE-Select; ENST00000376020.9; ENSP00000365188.2; NM_020717.5; NP_065768.2.
DR   UCSC; uc004dpe.4; human. [Q9ULL8-1]
DR   AGR; HGNC:29215; -.
DR   CTD; 57477; -.
DR   DisGeNET; 57477; -.
DR   GeneCards; SHROOM4; -.
DR   HGNC; HGNC:29215; SHROOM4.
DR   HPA; ENSG00000158352; Low tissue specificity.
DR   MalaCards; SHROOM4; -.
DR   MIM; 300579; gene.
DR   neXtProt; NX_Q9ULL8; -.
DR   OpenTargets; ENSG00000158352; -.
DR   Orphanet; 85288; X-linked intellectual disability, Stocco Dos Santos type.
DR   PharmGKB; PA147357321; -.
DR   VEuPathDB; HostDB:ENSG00000158352; -.
DR   eggNOG; ENOG502QSTC; Eukaryota.
DR   GeneTree; ENSGT00940000159479; -.
DR   HOGENOM; CLU_003220_1_1_1; -.
DR   InParanoid; Q9ULL8; -.
DR   OMA; LHCSDFD; -.
DR   OrthoDB; 4120529at2759; -.
DR   PhylomeDB; Q9ULL8; -.
DR   TreeFam; TF333370; -.
DR   PathwayCommons; Q9ULL8; -.
DR   SignaLink; Q9ULL8; -.
DR   BioGRID-ORCS; 57477; 9 hits in 773 CRISPR screens.
DR   ChiTaRS; SHROOM4; human.
DR   EvolutionaryTrace; Q9ULL8; -.
DR   GenomeRNAi; 57477; -.
DR   Pharos; Q9ULL8; Tbio.
DR   PRO; PR:Q9ULL8; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; Q9ULL8; Protein.
DR   Bgee; ENSG00000158352; Expressed in buccal mucosa cell and 131 other cell types or tissues.
DR   GO; GO:0005884; C:actin filament; IDA:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0009925; C:basal plasma membrane; ISS:UniProtKB.
DR   GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR   GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR   GO; GO:0045159; F:myosin II binding; ISS:UniProtKB.
DR   GO; GO:0030036; P:actin cytoskeleton organization; NAS:UniProtKB.
DR   GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
DR   GO; GO:0007420; P:brain development; IDA:UniProtKB.
DR   GO; GO:0050890; P:cognition; IDA:UniProtKB.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 6.10.250.3120; -; 1.
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:SF35; PROTEIN SHROOM4; 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; PS51307; ASD2; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   Genevisible; Q9ULL8; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Alternative splicing;
KW   Chromosomal rearrangement; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Developmental protein; Intellectual disability; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..1493
FT                   /note="Protein Shroom4"
FT                   /id="PRO_0000287077"
FT   DOMAIN          10..92
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          1213..1492
FT                   /note="ASD2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00638"
FT   REGION          202..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          430..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          740..759
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          781..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1117..1170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1187..1206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1214..1236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1246..1265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1382..1488
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        230..262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        469..483
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        484..498
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..568
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..602
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..644
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..676
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        782..813
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1131..1161
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1189..1206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         411
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q1W617"
FT   MOD_RES         729
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q1W617"
FT   MOD_RES         1019
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q1W617"
FT   VAR_SEQ         1..116
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_025290"
FT   VARIANT         146
FT                   /note="R -> W (found in a patient with Rett syndrome-like
FT                   phenotype; uncertain significance; dbSNP:rs189694750)"
FT                   /evidence="ECO:0000269|PubMed:26740508"
FT                   /id="VAR_079036"
FT   VARIANT         627
FT                   /note="P -> S (in dbSNP:rs150861758)"
FT                   /evidence="ECO:0000269|PubMed:26522270"
FT                   /id="VAR_075207"
FT   VARIANT         722
FT                   /note="R -> H (in dbSNP:rs3761506)"
FT                   /id="VAR_057770"
FT   VARIANT         807
FT                   /note="I -> T (in dbSNP:rs3761505)"
FT                   /id="VAR_057771"
FT   VARIANT         970
FT                   /note="D -> G (in dbSNP:rs2281571)"
FT                   /id="VAR_032257"
FT   VARIANT         1089
FT                   /note="S -> L (found in a family with Stocco dos
FT                   Santos-type X-linked syndromic intellectual developmental
FT                   disorder; uncertain significance; dbSNP:rs121434620)"
FT                   /evidence="ECO:0000269|PubMed:16249884"
FT                   /id="VAR_032258"
FT   VARIANT         1367
FT                   /note="L -> F (in dbSNP:rs28362302)"
FT                   /evidence="ECO:0000269|PubMed:24700572"
FT                   /id="VAR_074639"
FT   CONFLICT        1129..1131
FT                   /note="KQQ -> QQQQKQQE (in Ref. 1; BAA86516 and 3;
FT                   AAI51241)"
FT                   /evidence="ECO:0000305"
FT   STRAND          9..14
FT                   /evidence="ECO:0007829|PDB:2EDP"
FT   STRAND          25..28
FT                   /evidence="ECO:0007829|PDB:2EDP"
FT   HELIX           29..31
FT                   /evidence="ECO:0007829|PDB:2EDP"
FT   STRAND          33..37
FT                   /evidence="ECO:0007829|PDB:2EDP"
FT   HELIX           45..49
FT                   /evidence="ECO:0007829|PDB:2EDP"
FT   STRAND          57..61
FT                   /evidence="ECO:0007829|PDB:2EDP"
FT   HELIX           71..78
FT                   /evidence="ECO:0007829|PDB:2EDP"
FT   STRAND          85..90
FT                   /evidence="ECO:0007829|PDB:2EDP"
SQ   SEQUENCE   1493 AA;  164857 MW;  40260DC12A24EAFF CRC64;
     MENRPGSFQY VPVQLQGGAP WGFTLKGGLE HCEPLTVSKI EDGGKAALSQ KMRTGDELVN
     INGTPLYGSR QEALILIKGS FRILKLIVRR RNAPVSRPHS WHVAKLLEGC PEAATTMHFP
     SEAFSLSWHS GCNTSDVCVQ WCPLSRHCST EKSSSIGSME SLEQPGQATY ESHLLPIDQN
     MYPNQRDSAY SSFSASSNAS DCALSLRPEE PASTDCIMQG PGPTKAPSGR PNVAETSGGS
     RRTNGGHLTP SSQMSSRPQE GYQSGPAKAV RGPPQPPVRR DSLQASRAQL LNGEQRRASE
     PVVPLPQKEK LSLEPVLPAR NPNRFCCLSG HDQVTSEGHQ NCEFSQPPES SQQGSEHLLM
     QASTKAVGSP KACDRASSVD SNPLNEASAE LAKASFGRPP HLIGPTGHRH SAPEQLLASH
     LQHVHLDTRG SKGMELPPVQ DGHQWTLSPL HSSHKGKKSP CPPTGGTHDQ SSKERKTRQV
     DDRSLVLGHQ SQSSPPHGEA DGHPSEKGFL DPNRTSRAAS ELANQQPSAS GSLVQQATDC
     SSTTKAASGT EAGEEGDSEP KECSRMGGRR SGGTRGRSIQ NRRKSERFAT NLRNEIQRRK
     AQLQKSKGPL SQLCDTKEPV EETQEPPESP PLTASNTSLL SSCKKPPSPR DKLFNKSMML
     RARSSECLSQ APESHESRTG LEGRISPGQR PGQSSLGLNT WWKAPDPSSS DPEKAHAHCG
     VRGGHWRWSP EHNSQPLVAA AMEGPSNPGD NKELKASTAQ AGEDAILLPF ADRRKFFEES
     SKSLSTSHLP GLTTHSNKTF TQRPKPIDQN FQPMSSSCRE LRRHPMDQSY HSADQPYHAT
     DQSYHSMSPL QSETPTYSEC FASKGLENSM CCKPLHCGDF DYHRTCSYSC SVQGALVHDP
     CIYCSGEICP ALLKRNMMPN CYNCRCHHHQ CIRCSVCYHN PQHSALEDSS LAPGNTWKPR
     KLTVQEFPGD KWNPITGNRK TSQSGREMAH SKTSFSWATP FHPCLENPAL DLSSYRAISS
     LDLLGDFKHA LKKSEETSVY EEGSSLASMP HPLRSRAFSE SHISLAPQST RAWGQHRREL
     FSKGDETQSD LLGARKKAFP PPRPPPPNWE KYRLFRAAQQ QKQQQQQQKQ QEEEEEEEEE
     EEEEEEEEEE EAEEEEEELP PQYFSSETSG SCALNPEEVL EQPQPLSFGH LEGSRQGSQS
     VPAEQESFAL HSSDFLPPIR GHLGSQPEQA QPPCYYGIGG LWRTSGQEAT ESAKQEFQHF
     SPPSGAPGIP TSYSAYYNIS VAKAELLNKL KDQPEMAEIG LGEEEVDHEL AQKKIQLIES
     ISRKLSVLRE AQRGLLEDIN ANSALGEEVE ANLKAVCKSN EFEKYHLFVG DLDKVVNLLL
     SLSGRLARVE NALNSIDSEA NQEKLVLIEK KQQLTGQLAD AKELKEHVDR REKLVFGMVS
     RYLPQDQLQD YQHFVKMKSA LIIEQRELEE KIKLGEEQLK CLRESLLLGP SNF
//