FRYL_HUMAN
ID FRYL_HUMAN Reviewed; 3013 AA.
AC O94915; O95640; Q8WTZ5; Q9NT40;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein furry homolog-like;
DE AltName: Full=ALL1-fused gene from chromosome 4p12 protein;
GN Name=FRYL; Synonyms=AF4P12, KIAA0826;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Urinary bladder;
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 [3]
RP PROTEIN SEQUENCE OF 2-30; 382-392; 401-418; 425-435; 453-464; 501-512;
RP 514-520; 575-583; 908-919; 1062-1070; 1191-1199; 1661-1668; 1752-1760;
RP 1780-1789; 1835-1851; 2253-2279; 2713-2738; 2881-2895 AND 2979-2987,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Prostatic carcinoma;
RA Bienvenut W.V., Gao M., Leug H.;
RL Submitted (JUN-2009) to UniProtKB.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1754-2548 (ISOFORM 1).
RA Lee P.L., Gelbart T., West C., Adams M., Blackstone R.;
RT "Identification of fifteen genes mapping to a region of chromosome 6p21.3
RT encompassing the microsatellite markers D6S306 and D6S1260.
RT characterization of three genes encoding zinc finger proteins.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1778-3013 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2853-3013 (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP FUNCTION, CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1, AND TISSUE
RP SPECIFICITY.
RX PubMed=16061630; DOI=10.1158/0008-5472.can-05-1325;
RA Hayette S., Cornillet-Lefebvre P., Tigaud I., Struski S., Forissier S.,
RA Berchet A., Doll D., Gillot L., Brahim W., Delabesse E., Magaud J.-P.,
RA Rimokh R.;
RT "AF4p12, a human homologue to the furry gene of Drosophila, as a novel MLL
RT fusion partner.";
RL Cancer Res. 65:6521-6525(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2272, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-844, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-844; THR-1959 AND SER-2272,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1914; SER-1935 AND SER-2272,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-844, 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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-844; SER-1941; SER-1945;
RP SER-1957; THR-1959; SER-1978 AND SER-2272, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2454 AND SER-2499, AND
RP IDENTIFICATION BY 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 [18]
RP VARIANT SER-890.
RX PubMed=21835304; DOI=10.1016/j.ajhg.2011.07.005;
RA Ozgul R.K., Siemiatkowska A.M., Yucel D., Myers C.A., Collin R.W.,
RA Zonneveld M.N., Beryozkin A., Banin E., Hoyng C.B., van den Born L.I.,
RA Bose R., Shen W., Sharon D., Cremers F.P., Klevering B.J.,
RA den Hollander A.I., Corbo J.C.;
RT "Exome sequencing and cis-regulatory mapping identify mutations in MAK, a
RT gene encoding a regulator of ciliary length, as a cause of retinitis
RT pigmentosa.";
RL Am. J. Hum. Genet. 89:253-264(2011).
CC -!- FUNCTION: Plays a key role in maintaining the integrity of polarized
CC cell extensions during morphogenesis, regulates the actin cytoskeleton
CC and plays a key role in patterning sensory neuron dendritic fields by
CC promoting avoidance between homologous dendrites as well as by limiting
CC dendritic branching (By similarity). May function as a transcriptional
CC activator. {ECO:0000250, ECO:0000269|PubMed:16061630}.
CC -!- INTERACTION:
CC O94915-2; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-12023420, EBI-748420;
CC O94915-2; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-12023420, EBI-14086479;
CC O94915-2; Q9BUL8: PDCD10; NbExp=3; IntAct=EBI-12023420, EBI-740195;
CC O94915-2; P0CG20: PRR35; NbExp=3; IntAct=EBI-12023420, EBI-11986293;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O94915-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O94915-2; Sequence=VSP_023038, VSP_023039;
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in colon,
CC placenta, brain and cells of lymphoid origin.
CC {ECO:0000269|PubMed:16061630}.
CC -!- DISEASE: Note=A chromosomal aberration involving FRYL is found in
CC treatment-related acute lymphoblastic leukemia (ALL). Translocation
CC t(4;11)(p12;q23) that forms a KMT2A/MLL1-FRYL fusion protein.
CC {ECO:0000269|PubMed:16061630}.
CC -!- SIMILARITY: Belongs to the furry protein family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/AF4q12ID42970ch4p12.html";
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DR EMBL; AC068037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021803; AAH21803.1; -; mRNA.
DR EMBL; U80082; AAD00351.1; -; mRNA.
DR EMBL; AB020633; BAA74849.1; -; mRNA.
DR EMBL; AL137546; CAB70804.1; -; mRNA.
DR CCDS; CCDS43227.1; -. [O94915-1]
DR PIR; T46389; T46389.
DR RefSeq; NP_055845.1; NM_015030.1. [O94915-1]
DR RefSeq; XP_016863535.1; XM_017008046.1. [O94915-1]
DR BioGRID; 130134; 55.
DR IntAct; O94915; 34.
DR MINT; O94915; -.
DR STRING; 9606.ENSP00000351113; -.
DR CarbonylDB; O94915; -.
DR GlyGen; O94915; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; O94915; -.
DR PhosphoSitePlus; O94915; -.
DR BioMuta; FRYL; -.
DR EPD; O94915; -.
DR jPOST; O94915; -.
DR MassIVE; O94915; -.
DR MaxQB; O94915; -.
DR PaxDb; O94915; -.
DR PeptideAtlas; O94915; -.
DR PRIDE; O94915; -.
DR ProteomicsDB; 50549; -. [O94915-1]
DR ProteomicsDB; 50550; -. [O94915-2]
DR Antibodypedia; 23821; 37 antibodies from 11 providers.
DR DNASU; 285527; -.
DR Ensembl; ENST00000358350.9; ENSP00000351113.4; ENSG00000075539.15. [O94915-1]
DR GeneID; 285527; -.
DR KEGG; hsa:285527; -.
DR MANE-Select; ENST00000358350.9; ENSP00000351113.4; NM_015030.2; NP_055845.1.
DR UCSC; uc003gyh.1; human. [O94915-1]
DR CTD; 285527; -.
DR DisGeNET; 285527; -.
DR GeneCards; FRYL; -.
DR HGNC; HGNC:29127; FRYL.
DR HPA; ENSG00000075539; Tissue enhanced (brain).
DR neXtProt; NX_O94915; -.
DR OpenTargets; ENSG00000075539; -.
DR PharmGKB; PA134967984; -.
DR VEuPathDB; HostDB:ENSG00000075539; -.
DR eggNOG; KOG1825; Eukaryota.
DR GeneTree; ENSGT00610000086058; -.
DR HOGENOM; CLU_000483_0_0_1; -.
DR InParanoid; O94915; -.
DR OMA; HAQQVTI; -.
DR OrthoDB; 11874at2759; -.
DR PhylomeDB; O94915; -.
DR TreeFam; TF313568; -.
DR PathwayCommons; O94915; -.
DR SignaLink; O94915; -.
DR BioGRID-ORCS; 285527; 44 hits in 1084 CRISPR screens.
DR ChiTaRS; FRYL; human.
DR GenomeRNAi; 285527; -.
DR Pharos; O94915; Tdark.
DR PRO; PR:O94915; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O94915; protein.
DR Bgee; ENSG00000075539; Expressed in corpus callosum and 205 other tissues.
DR ExpressionAtlas; O94915; baseline and differential.
DR Genevisible; O94915; HS.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0030427; C:site of polarized growth; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR025614; Cell_morpho_N.
DR InterPro; IPR025481; Cell_Morphogen_C.
DR InterPro; IPR045842; Fry_C.
DR InterPro; IPR039867; Furry/Tao3/Mor2.
DR InterPro; IPR029473; MOR2-PAG1_mid.
DR PANTHER; PTHR12295; PTHR12295; 1.
DR Pfam; PF19421; Fry_C; 1.
DR Pfam; PF14225; MOR2-PAG1_C; 1.
DR Pfam; PF14228; MOR2-PAG1_mid; 4.
DR Pfam; PF14222; MOR2-PAG1_N; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromosomal rearrangement;
KW Direct protein sequencing; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3"
FT CHAIN 2..3013
FT /note="Protein furry homolog-like"
FT /id="PRO_0000277619"
FT REGION 90..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1476..1498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2459..2492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2508..2567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2636..2660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1476..1492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2460..2484
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2527..2564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2636..2655
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 2302
FT /note="Breakpoint for insertion to form KMT2A/MLL1-AFF4
FT fusion protein"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.3"
FT MOD_RES 844
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1914
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1935
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1941
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1945
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1957
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1959
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1978
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2454
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 2499
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..2604
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023038"
FT VAR_SEQ 2822..2827
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023039"
FT VARIANT 890
FT /note="P -> S (in dbSNP:rs376571442)"
FT /evidence="ECO:0000269|PubMed:21835304"
FT /id="VAR_066994"
FT VARIANT 1878
FT /note="I -> V (in dbSNP:rs7670111)"
FT /id="VAR_053832"
SQ SEQUENCE 3013 AA; 339598 MW; DFD7FEC47792DA1E CRC64;
MSNITIDPDV KPGEYVIKSL FAEFAVQAEK KIEVVMAEPL EKLLSRSLQR GEDLQFDQLI
SSMSSVAEHC LPSLLRTLFD WYRRQNGTED ESYEYRPRSS TKSKGDEQQR ERDYLLERRD
LAVDFIFCLV LVEVLKQIPV HPVPDPLVHE VLNLAFKHFK HKEGYSGTNT GNVHIIADLY
AEVIGVLAQS KFQAVRKKFV TELKELRQKE QSPHVVQSVI SLIMGMKFFR VKMYPVEDFE
ASFQFMQECA QYFLEVKDKD IKHALAGLFV EILIPVAAAV KNEVNVPCLK NFVEMLYQTT
FELSSRKKHS LALYPLITCL LCVSQKQFFL NNWHIFLQNC LSHLKNKDPK MSRVALESLY
RLLWVYVIRI KCESNTVTQS RLMSIVSALF PKGSRSVVPR DTPLNIFVKI IQFIAQERLD
FAMKEIIFDL LSVGKSTKTF TINPERMNIG LRVFLVIADS LQQKDGEPPM PTTGVILPSG
NTLRVKKIFL NKTLTDEEAK VIGMSVYYPQ VRKALDSILR HLDKEVGRPM CMTSVQMSNK
EPEDMITGER KPKIDLFRTC IAAIPRLIPD GMSRTDLIEL LARLTIHMDE ELRALAFNTL
QALMLDFPDW REDVLSGFVY FIVREVTDVH PTLLDNAVKM LVQLINQWKQ AAQMHNKNQD
TQHGVANGAS HPPPLERSPY SNVFHVVEGF ALVILCSSRP ATRRLAVSVL REIRALFALL
EIPKGDDELA IDVMDRLSPS ILESFIHLTG ADQTTLLYCP SSIDLQTLAE WNSSPISHQF
DVISPSHIWI FAHVTQGQDP WIISLSSFLK QENLPKHCST AVSYAWMFAY TRLQLLSPQV
DINSPINAKK VNTTTSSDSY IGLWRNYLIL CCSAATSSSS TSAGSVRCSP PETLASTPDS
GYSIDSKIIG IPSPSSLFKH IVPMMRSESM EITESLVLGL GRTNPGAFRE LIEELHPIIK
EALERRPENM KRRRRRDILR VQLVRIFELL ADAGVISHSA SGGLDNETHF LNNTLLEYVD
LTRQLLEAEN EKDSDTLKDI RCHFSALVAN IIQNVPVHQR RSIFPQQSLR HSLFMLFSHW
AGPFSIMFTP LDRYSDRNMQ INRHQYCALK AMSAVLCCGP VADNVGLSSD GYLYKWLDNI
LDSLDKKVHQ LGCEAVTLLL ELNPDQSNLM YWAVDRCYTG SGRVAAGCFK AIANVFQNRD
YQCDTVMLLN LILFKAADSS RSIYEVAMQL LQILEPKMFR YAHKLEVQRT DGVLSQLSPL
PHLYSVSYYQ LSEELARAYP ELTLAIFSEI SQRIQTAHPA GRQVMLHYLL PWMNNIELVD
LKPLPTARRH DEDEDDSLKD RELMVTSRRW LRGEGWGSPQ ATAMVLNNLM YMTAKYGDEL
AWSEVENVWT TLADGWPKNL KIILHFLISI CGVNSEPSLL PYVKKVIVYL GRDKTMQLLE
ELVSELQLTD PVSSGVTHMD NPPYYRITSS YKIPSVTSGT TSSSNTMVAP TDGNPDNKPI
KENIEESYVH LDIYSGLNSH LNRQHHRLES RYSSSSGGSY EEEKSDSMPL YSNWRLKVME
HNQGEPLPFP PAGGCWSPLV DYVPETSSPG LPLHRCNIAV ILLTDLIIDH SVKVEWGSYL
HLLLHAIFIG FDHCHPEVYE HCKRLLLHLL IVMGPNSNIR TVASVLLRNK EFNEPRVLTV
KQVAHLDYNF TAGINDFIPD YQPSPMTDSG LSSSSTSSSI SLGNNSAAIS HLHTTILNEV
DISVEQDGKV KTLMEFITSR KRGPLWNHED VSAKNPSIKS AEQLTTFLKH VVSVFKQSSS
EGIHLEHHLS EVALQTALSC SSRHYAGRSF QIFRALKQPL TATTLSDVLS RLVETVGDPG
EDAQGFVIEL LLTLESAIDT LAETMKHYDL LSALSQTSYH DPIMGNKYAA NRKSTGQLNL
STSPINSSSY LGYNSNARSN SLRLSLIGDR RGDRRRSNTL DIMDGRINHS SSLARTRSLS
SLREKGMYDV QSTTEPTNLM ATIFWIAASL LESDYEYEYL LALRLLNKLL IHLPLDKSES
REKIENVQSK LKWTNFPGLQ QLFLKGFTSA STQEMTVHLL SKLISVSKHT LVDPSQLSGF
PLNILCLLPH LIQHFDSPTQ FCKETASRIA KVCAEEKCPT LVNLAHMMSL YSTHTYSRDC
SNWINVVCRY LHDSFSDTTF NLVTYLAELL EKGLSSMQQS LLQIIYSLLS HIDLSAAPAK
QFNLEIIKII GKYVQSPYWK EALNILKLVV SRSASLVVPS DIPKTYGGDT GSPEISFTKI
FNNVSKELPG KTLDFHFDIS ETPIIGNKYG DQHSAAGRNG KPKVIAVTRS TSSTSSGSNS
NALVPVSWKR PQLSQRRTRE KLMNVLSLCG PESGLPKNPS VVFSSNEDLE VGDQQTSLIS
TTEDINQEEE VAVEDNSSEQ QFGVFKDFDF LDVELEDAEG ESMDNFNWGV RRRSLDSIDK
GDTPSLQEYQ CSSSTPSLNL TNQEDTDESS EEEAALTASQ ILSRTQMLNS DSATDETIPD
HPDLLLQSED STGSITTEEV LQIRDETPTL EASLDNANSR LPEDTTSVLK EEHVTTFEDE
GSYIIQEQQE SLVCQGILDL EETEMPEPLA PESYPESVCE EDVTLALKEL DERCEEEEAD
FSGLSSQDEE EQDGFPEVQT SPLPSPFLSA IIAAFQPVAY DDEEEAWRCH VNQMLSDTDG
SSAVFTFHVF SRLFQTIQRK FGEITNEAVS FLGDSLQRIG TKFKSSLEVM MLCSECPTVF
VDAETLMSCG LLETLKFGVL ELQEHLDTYN VKREAAEQWL DDCKRTFGAK EDMYRINTDA
QQMEILAELE LCRRLYKLHF QLLLLFQAYC KLINQVNTIK NEAEVINMSE ELAQLESILK
EAESASENEE IDISKAAQTT IETAIHSLIE TLKNKEFISA VAQVKAFRSL WPSDIFGSCE
DDPVQTLLHI YFHHQTLGQT GSFAVIGSNL DMSEANYKLM ELNLEIRESL RMVQSYQLLA
QAKPMGNMVS TGF
