IQEC1_MOUSE
ID IQEC1_MOUSE Reviewed; 961 AA.
AC Q8R0S2; Q3TZC3; Q5DU15;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=IQ motif and SEC7 domain-containing protein 1;
GN Name=Iqsec1; Synonyms=Kiaa0763;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-217 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Inner ear;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 414-961.
RC TISSUE=Eye;
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 [LARGE SCALE MRNA] OF 432-961.
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-179, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104; SER-106; SER-179;
RP SER-247; SER-251; SER-510; SER-513 AND SER-923, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [10]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=20547133; DOI=10.1016/j.neuron.2010.05.003;
RA Scholz R., Berberich S., Rathgeber L., Kolleker A., Koehr G., Kornau H.C.;
RT "AMPA receptor signaling through BRAG2 and Arf6 critical for long-term
RT synaptic depression.";
RL Neuron 66:768-780(2010).
RN [11]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=31607425; DOI=10.1016/j.ajhg.2019.09.013;
RA Ansar M., Chung H.L., Al-Otaibi A., Elagabani M.N., Ravenscroft T.A.,
RA Paracha S.A., Scholz R., Abdel Magid T., Sarwar M.T., Shah S.F.,
RA Qaisar A.A., Makrythanasis P., Marcogliese P.C., Kamsteeg E.J.,
RA Falconnet E., Ranza E., Santoni F.A., Aldhalaan H., Al-Asmari A.,
RA Faqeih E.A., Ahmed J., Kornau H.C., Bellen H.J., Antonarakis S.E.;
RT "Bi-allelic Variants in IQSEC1 Cause Intellectual Disability, Developmental
RT Delay, and Short Stature.";
RL Am. J. Hum. Genet. 105:907-920(2019).
CC -!- FUNCTION: Guanine nucleotide exchange factor for ARF1 and ARF6. Guanine
CC nucleotide exchange factor activity is enhanced by lipid binding.
CC Accelerates GTP binding by ARFs of all three classes. Guanine
CC nucleotide exchange protein for ARF6, mediating internalization of
CC beta-1 integrin (By similarity). Involved in neuronal development
CC (PubMed:31607425). In neurons, plays a role in the control of vesicle
CC formation by endocytoc cargo. Upon long term depression, interacts with
CC GRIA2 and mediates the activation of ARF6 to internalize synaptic AMPAR
CC receptors (By similarity). {ECO:0000250|UniProtKB:A0A0G2JUG7,
CC ECO:0000250|UniProtKB:Q6DN90, ECO:0000269|PubMed:31607425}.
CC -!- SUBUNIT: Interacts with ARF1 and ARF6. Interacts with GRIA2; the
CC interaction is required for ARF6 activation.
CC {ECO:0000250|UniProtKB:A0A0G2JUG7, ECO:0000250|UniProtKB:Q6DN90}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6DN90}. Nucleus
CC {ECO:0000250|UniProtKB:Q6DN90}. Postsynaptic density
CC {ECO:0000269|PubMed:20547133}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle {ECO:0000269|PubMed:20547133}. Note=At steady state,
CC may be preferentially cytosolic. {ECO:0000250|UniProtKB:Q6DN90}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R0S2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R0S2-2; Sequence=VSP_019759;
CC -!- TISSUE SPECIFICITY: Expressed in hippocampus.
CC {ECO:0000269|PubMed:20547133}.
CC -!- DEVELOPMENTAL STAGE: Expression is first detected at postanatal day P7
CC and increases until P42 (at protein level).
CC {ECO:0000269|PubMed:20547133}.
CC -!- DOMAIN: The PH domain mediates interaction with lipid membranes that
CC contain phosphatidylinositol-4,5-bisphosphate, but does not bind
CC membranes that lack phosphatidylinositol-4,5-bisphosphate.
CC {ECO:0000250|UniProtKB:Q6DN90}.
CC -!- DISRUPTION PHENOTYPE: Mice with a conditional knockout in cortical
CC neurons exhibit an increased density of dendritic spines with an
CC immature morphology. {ECO:0000269|PubMed:31607425}.
CC -!- SIMILARITY: Belongs to the BRAG family. {ECO:0000305}.
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DR EMBL; AC121954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK157963; BAE34286.1; -; mRNA.
DR EMBL; BC026481; AAH26481.1; -; mRNA.
DR EMBL; AK220355; BAD90418.1; -; mRNA.
DR CCDS; CCDS51850.1; -. [Q8R0S2-1]
DR RefSeq; NP_001127855.1; NM_001134383.1. [Q8R0S2-1]
DR AlphaFoldDB; Q8R0S2; -.
DR SMR; Q8R0S2; -.
DR BioGRID; 231231; 31.
DR IntAct; Q8R0S2; 14.
DR MINT; Q8R0S2; -.
DR STRING; 10090.ENSMUSP00000140030; -.
DR iPTMnet; Q8R0S2; -.
DR PhosphoSitePlus; Q8R0S2; -.
DR EPD; Q8R0S2; -.
DR jPOST; Q8R0S2; -.
DR MaxQB; Q8R0S2; -.
DR PaxDb; Q8R0S2; -.
DR PeptideAtlas; Q8R0S2; -.
DR PRIDE; Q8R0S2; -.
DR ProteomicsDB; 269090; -. [Q8R0S2-1]
DR ProteomicsDB; 269091; -. [Q8R0S2-2]
DR Antibodypedia; 26313; 50 antibodies from 22 providers.
DR DNASU; 232227; -.
DR Ensembl; ENSMUST00000101153; ENSMUSP00000098712; ENSMUSG00000034312. [Q8R0S2-1]
DR GeneID; 232227; -.
DR KEGG; mmu:232227; -.
DR UCSC; uc009cxq.2; mouse. [Q8R0S2-1]
DR UCSC; uc033itn.1; mouse. [Q8R0S2-2]
DR CTD; 9922; -.
DR MGI; MGI:1196356; Iqsec1.
DR VEuPathDB; HostDB:ENSMUSG00000034312; -.
DR eggNOG; KOG0931; Eukaryota.
DR GeneTree; ENSGT00940000156915; -.
DR HOGENOM; CLU_004328_0_1_1; -.
DR InParanoid; Q8R0S2; -.
DR OrthoDB; 837077at2759; -.
DR PhylomeDB; Q8R0S2; -.
DR TreeFam; TF323811; -.
DR BioGRID-ORCS; 232227; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Iqsec1; mouse.
DR PRO; PR:Q8R0S2; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8R0S2; protein.
DR Bgee; ENSMUSG00000034312; Expressed in granulocyte and 244 other tissues.
DR ExpressionAtlas; Q8R0S2; baseline and differential.
DR Genevisible; Q8R0S2; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0008021; C:synaptic vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IPI:ARUK-UCL.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0060996; P:dendritic spine development; IMP:UniProtKB.
DR GO; GO:0120183; P:positive regulation of focal adhesion disassembly; IMP:ARUK-UCL.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0051549; P:positive regulation of keratinocyte migration; IMP:ARUK-UCL.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; IDA:SynGO.
DR CDD; cd13318; PH_IQSEC; 1.
DR CDD; cd00171; Sec7; 1.
DR Gene3D; 1.10.1000.11; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR030737; IQSEC1.
DR InterPro; IPR033742; IQSEC_PH.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR023394; Sec7_C_sf.
DR InterPro; IPR000904; Sec7_dom.
DR InterPro; IPR035999; Sec7_dom_sf.
DR PANTHER; PTHR10663:SF327; PTHR10663:SF327; 1.
DR Pfam; PF16453; IQ_SEC7_PH; 1.
DR Pfam; PF01369; Sec7; 1.
DR SMART; SM00222; Sec7; 1.
DR SUPFAM; SSF48425; SSF48425; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS50190; SEC7; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Guanine-nucleotide releasing factor; Lipid-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..961
FT /note="IQ motif and SEC7 domain-containing protein 1"
FT /id="PRO_0000245607"
FT DOMAIN 133..162
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 515..708
FT /note="SEC7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00189"
FT DOMAIN 772..864
FT /note="PH"
FT REGION 21..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 846..877
FT /evidence="ECO:0000255"
FT COMPBIAS 27..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 466..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DN90"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 890
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DN90"
FT MOD_RES 909
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q6DN90"
FT MOD_RES 922
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DN90"
FT MOD_RES 923
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..22
FT /note="MWCLHCNSERTQSLLELELDSG -> MKGDGGAVWGLMWKYCISVRTLS
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019759"
FT CONFLICT 759
FT /note="E -> Q (in Ref. 3; BAD90418)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 961 AA; 108015 MW; 44E9B61CE2445325 CRC64;
MWCLHCNSER TQSLLELELD SGVEGEAPSS ETGTSLDSPS AYHQGPLVPG SSLSPDHYEH
TSVGAYGLYA GPGPQQRTRR PRLQHSTSVL RKQAEEEAIK RSRSLSESYE LSSDLQDKQV
EMLERKYGGR LVTRHAARTI QTAFRQYQMN KNFERLRSSM SENRMSRRIV LSNMRMQFSF
EGPEKVHSSY FEGKQVSVTN DGSQLGALVP SECGDLSDPA LKSPAPSSDF ADAITELEDA
FSRQVKSLAE SIDDALNCRS LHSEEVPASD TARARDTEPK PGLHGMDHRK LDEMTASYSD
VTLYIDEEEL SPPLPLSQAG DRPSSTESDL RLRSGGAAQD YWALAHKEDK ADTDTSCRST
PSLERPEPRL RVEHLPLLTI EPPSDSSVEL SDRSDRSSLK RQSAYERSLG GQQGSPKHGP
HGGPPKGLPR EEPELRPRPP RPLESHLAIN GSANRQSKSE SDYSDGDNDS INSTSNSNDT
INCSSESSSR DSLREQTLSK QTYHKETRNS WDSPAFSNDV IRKRHYRIGL NLFNKKPEKG
IQYLIERGFV PDTPVGVAHF LLQRKGLSRQ MIGEFLGNRQ KQFNRDVLDC VVDEMDFSAM
ELDEALRKFQ AHIRVQGEAQ KVERLIEAFS QRYCVCNPGV VRQFRNPDTI FILAFAIILL
NTDMYSPNVK PERKMKLEDF VKNLRGVDDG EDIPRETLIG IYERIRKREL KTNEDHVSQV
QKVEKLIVGK KPIGSLHHGL GCVLSLPHRR LVCYCRLFEV PDPNKPQKLG LHQREIFLFN
DLLVVTKIFQ KKKNSVTYSF RQSFSLYGMQ VLLFENQYYP NGIRLTSAVP GADIKVLINF
NAPNPQDRKK FTDDLRESVA EVQEMEKHRI ESELEKQKGV VRPSMSQCSS LKKESGNGTL
SRACLDDSYA SGEGLKRSAL SSSLRDLSEA GKRGRRSSAG SLESNVEFQP FQPPQPPVLC
S
