SHRM4_HUMAN
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 03-AUG-2022, entry version 148.
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 SDSX 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: Intellectual developmental disorder, X-linked, syndromic,
CC Stocco dos Santos type (SDSX) [MIM:300434]: A syndrome characterized by
CC severe intellectual disability with hyperactivity, aggressive behavior,
CC delayed or no speech, and seizures. Additional features include
CC congenital bilateral hip luxation, short stature, and kyphosis.
CC {ECO:0000269|PubMed:16249884}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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; 3.
DR STRING; 9606.ENSP00000365188; -.
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; Q9ULL8; -.
DR PeptideAtlas; Q9ULL8; -.
DR PRIDE; Q9ULL8; -.
DR ProteomicsDB; 85073; -. [Q9ULL8-1]
DR ProteomicsDB; 85074; -. [Q9ULL8-2]
DR Antibodypedia; 532; 13 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 CTD; 57477; -.
DR DisGeNET; 57477; -.
DR GeneCards; SHROOM4; -.
DR HGNC; HGNC:29215; SHROOM4.
DR HPA; ENSG00000158352; Tissue enhanced (brain).
DR MalaCards; SHROOM4; -.
DR MIM; 300434; phenotype.
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; 29607at2759; -.
DR PhylomeDB; Q9ULL8; -.
DR TreeFam; TF333370; -.
DR PathwayCommons; Q9ULL8; -.
DR SignaLink; Q9ULL8; -.
DR BioGRID-ORCS; 57477; 7 hits in 699 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 130 other tissues.
DR Genevisible; Q9ULL8; HS.
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 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 3D-structure; Actin-binding; Alternative splicing;
KW Chromosomal rearrangement; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Disease variant; Intellectual disability;
KW Phosphoprotein; 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; unknown pathological significance;
FT 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 (in SDSX; 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
