DEN1B_MOUSE
ID DEN1B_MOUSE Reviewed; 766 AA.
AC Q3U1T9; B2RUR7; E9Q246; Q8CG96; Q9D5B9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 3.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=DENN domain-containing protein 1B {ECO:0000312|MGI:MGI:2447812};
DE AltName: Full=Connecdenn 2 {ECO:0000250|UniProtKB:Q6P3S1};
GN Name=Dennd1b {ECO:0000312|MGI:MGI:2447812};
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 MRNA] (ISOFORMS 2 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=Czech II; TISSUE=Brain, and Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-500; SER-516; SER-517;
RP SER-530; SER-533; SER-632 AND SER-633, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, 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 [5]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, INTERACTION WITH CD3E
RP AND RAB35, AND MUTAGENESIS OF GLY-246; LYS-482 AND 547-ASP--LEU-549.
RX PubMed=26774822; DOI=10.1016/j.cell.2015.11.052;
RA Yang C.W., Hojer C.D., Zhou M., Wu X., Wuster A., Lee W.P., Yaspan B.L.,
RA Chan A.C.;
RT "Regulation of T cell receptor signaling by DENND1B in TH2 cells and
RT allergic disease.";
RL Cell 164:141-155(2016).
CC -!- FUNCTION: Guanine nucleotide exchange factor (GEF) for RAB35 that acts
CC as a regulator of T-cell receptor (TCR) internalization in TH2 cells.
CC Acts by promoting the exchange of GDP to GTP, converting inactive GDP-
CC bound RAB35 into its active GTP-bound form. Plays a role in clathrin-
CC mediated endocytosis. Controls cytokine production in TH2 lymphocytes
CC by controlling the rate of TCR internalization and routing to
CC endosomes: acts by mediating clathrin-mediated endocytosis of TCR via
CC its interaction with the adapter protein complex 2 (AP-2) and GEF
CC activity. Dysregulation leads to impaired TCR down-modulation and
CC recycling, affecting cytokine production in TH2 cells.
CC {ECO:0000269|PubMed:26774822}.
CC -!- SUBUNIT: Interacts with RAB35 (PubMed:26774822). Interacts with
CC clathrin heavy chain/CLTC (By similarity). Interacts with components of
CC the adapter protein complex 2 (AP-2) AP2A2 and AP2B1 (By similarity).
CC Interacts with CD3E (PubMed:26774822). {ECO:0000250|UniProtKB:Q6P3S1,
CC ECO:0000269|PubMed:26774822}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q6P3S1}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000250|UniProtKB:Q6P3S1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=5;
CC IsoId=Q3U1T9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U1T9-2; Sequence=VSP_058173;
CC Name=3;
CC IsoId=Q3U1T9-3; Sequence=VSP_058174, VSP_058175;
CC Name=4;
CC IsoId=Q3U1T9-4; Sequence=VSP_058172;
CC Name=1;
CC IsoId=Q3U1T9-5; Sequence=VSP_058174, VSP_058176;
CC -!- TISSUE SPECIFICITY: Expressed in a subset of dendritic cells (DCs).
CC {ECO:0000269|PubMed:26774822}.
CC -!- DOMAIN: The FXDXF motif mediates interaction the AP-2 complex.
CC {ECO:0000269|PubMed:26774822}.
CC -!- DOMAIN: The clathrin box motif mediates interaction with clathrin.
CC {ECO:0000269|PubMed:26774822}.
CC -!- PTM: Phosphorylated on serine and/or threonine, possibly regulating the
CC guanine nucleotide exchange factor (GEF) activity.
CC {ECO:0000250|UniProtKB:Q6P3S1}.
CC -!- DISRUPTION PHENOTYPE: Mice are developmentally normal and fertile but
CC accumulate more splenic and lymph node CD4(+) and CD8(+)
CC effector/memory T-cells with age. TH2 cells display increased TCR-
CC mediated responses, due to delayed surface TCR down-modulation and
CC recycling, and increased production of cytokines. Mice have increased
CC antigen-induced allergic responses. {ECO:0000269|PubMed:26774822}.
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DR EMBL; AK015524; BAB29881.1; -; mRNA.
DR EMBL; AK155727; BAE33404.1; -; mRNA.
DR EMBL; AC138741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC042698; AAH42698.1; -; mRNA.
DR EMBL; BC141388; AAI41389.1; -; mRNA.
DR EMBL; BC141389; AAI41390.1; -; mRNA.
DR CCDS; CCDS35728.1; -. [Q3U1T9-2]
DR CCDS; CCDS48384.1; -. [Q3U1T9-1]
DR RefSeq; NP_001159973.1; NM_001166501.1. [Q3U1T9-1]
DR RefSeq; NP_851992.1; NM_181347.3. [Q3U1T9-2]
DR AlphaFoldDB; Q3U1T9; -.
DR SMR; Q3U1T9; -.
DR STRING; 10090.ENSMUSP00000092082; -.
DR iPTMnet; Q3U1T9; -.
DR PhosphoSitePlus; Q3U1T9; -.
DR EPD; Q3U1T9; -.
DR jPOST; Q3U1T9; -.
DR MaxQB; Q3U1T9; -.
DR PaxDb; Q3U1T9; -.
DR PRIDE; Q3U1T9; -.
DR ProteomicsDB; 279612; -. [Q3U1T9-1]
DR ProteomicsDB; 279613; -. [Q3U1T9-2]
DR ProteomicsDB; 279614; -. [Q3U1T9-3]
DR ProteomicsDB; 279615; -. [Q3U1T9-4]
DR ProteomicsDB; 279616; -. [Q3U1T9-5]
DR Antibodypedia; 34481; 152 antibodies from 19 providers.
DR DNASU; 329260; -.
DR Ensembl; ENSMUST00000094505; ENSMUSP00000092082; ENSMUSG00000056268. [Q3U1T9-2]
DR Ensembl; ENSMUST00000168527; ENSMUSP00000127580; ENSMUSG00000056268. [Q3U1T9-1]
DR Ensembl; ENSMUST00000200533; ENSMUSP00000142738; ENSMUSG00000056268. [Q3U1T9-3]
DR GeneID; 329260; -.
DR KEGG; mmu:329260; -.
DR UCSC; uc007cvy.2; mouse. [Q3U1T9-3]
DR UCSC; uc007cvz.2; mouse. [Q3U1T9-2]
DR UCSC; uc007cwb.2; mouse.
DR UCSC; uc011wtc.1; mouse. [Q3U1T9-4]
DR CTD; 163486; -.
DR MGI; MGI:2447812; Dennd1b.
DR VEuPathDB; HostDB:ENSMUSG00000056268; -.
DR eggNOG; KOG3569; Eukaryota.
DR GeneTree; ENSGT00940000155446; -.
DR InParanoid; Q3U1T9; -.
DR OMA; HRSNTMK; -.
DR OrthoDB; 189322at2759; -.
DR PhylomeDB; Q3U1T9; -.
DR TreeFam; TF343037; -.
DR Reactome; R-MMU-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR BioGRID-ORCS; 329260; 3 hits in 69 CRISPR screens.
DR ChiTaRS; Dennd1b; mouse.
DR PRO; PR:Q3U1T9; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q3U1T9; protein.
DR Bgee; ENSMUSG00000056268; Expressed in metanephric cortical collecting duct and 216 other tissues.
DR ExpressionAtlas; Q3U1T9; baseline and differential.
DR Genevisible; Q3U1T9; MM.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IMP:UniProtKB.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:UniProtKB.
DR GO; GO:2000553; P:positive regulation of T-helper 2 cell cytokine production; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0050776; P:regulation of immune response; IMP:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IMP:UniProtKB.
DR Gene3D; 3.40.50.11500; -; 1.
DR InterPro; IPR001194; cDENN_dom.
DR InterPro; IPR005112; dDENN_dom.
DR InterPro; IPR043153; DENN_C.
DR InterPro; IPR040032; DENND1A/B/C.
DR InterPro; IPR037516; Tripartite_DENN.
DR InterPro; IPR005113; uDENN_dom.
DR PANTHER; PTHR13196; PTHR13196; 1.
DR Pfam; PF03455; dDENN; 1.
DR Pfam; PF02141; DENN; 1.
DR Pfam; PF03456; uDENN; 1.
DR SMART; SM00801; dDENN; 1.
DR SMART; SM00799; DENN; 1.
DR SMART; SM00800; uDENN; 1.
DR PROSITE; PS50211; DENN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW Guanine-nucleotide releasing factor; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..766
FT /note="DENN domain-containing protein 1B"
FT /id="PRO_0000304675"
FT DOMAIN 14..143
FT /note="uDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 160..296
FT /note="cDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT DOMAIN 298..375
FT /note="dDENN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT REGION 472..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 378..382
FT /note="FXDXF motif"
FT /evidence="ECO:0000269|PubMed:26774822"
FT MOTIF 547..556
FT /note="Clathrin box"
FT /evidence="ECO:0000269|PubMed:26774822"
FT COMPBIAS 472..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 500
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..363
FT /note="MDRRTRENPERTFDLVLKVKCHASENEDPEVLWKFPEDFGDQEVLQSVPKFC
FT FPFDVERVSQNQVGQHFTFVLTDMESKQRFGFCRLTSGGRICLCILSYLPWFEVYYKLL
FT NTLADYLAKELEEDLNETLKSLYNHPVPKANTPVNLSVHSCFITPDITGLPTIPESRNL
FT TEYFVAVDVNNMLRLYASMLHERRIIITSSKLSTLTACLHGSAALLYPMYWQHIYIPVL
FT PPHLLDYCCAPMPYLIGIHSSLIERVKNKSLEDVVVLNVDTNTLESPFNDLSSLPSDVV
FT SALKNKLKKQSTATGDGVARAFLRAQAALFGSYRDALRYKPGEPITFCEESFVKHRSSV
FT MKQFLETAVNLQLFKQ -> MVLFISITCLYVFSSFSVRTSTCLIMFSCFSLRTCNSLA
FT VFSCISLSDLLKSFLMSSTIIMRYAFKSRSRFSASLKLRAHLITMFAWSFLHRILPM
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_058172"
FT VAR_SEQ 1..75
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_058173"
FT VAR_SEQ 149
FT /note="V -> VNQELFIASEQVLKDDPSLIP (in isoform 1 and isoform
FT 3)"
FT /id="VSP_058174"
FT VAR_SEQ 205..766
FT /note="LTACLHGSAALLYPMYWQHIYIPVLPPHLLDYCCAPMPYLIGIHSSLIERVK
FT NKSLEDVVVLNVDTNTLESPFNDLSSLPSDVVSALKNKLKKQSTATGDGVARAFLRAQA
FT ALFGSYRDALRYKPGEPITFCEESFVKHRSSVMKQFLETAVNLQLFKQFIDGRLAKLNA
FT GRGFSDIFEEEITSGGFCGGSPRSYQQWVYTVKKGGALFNTAVTKATPAVRTAYKFAKS
FT HARLGLKEVKSRLKHKDNEEEYGTCSGLVQYTPVYTLHNEKGENREKHKLSQTHLKRPH
FT KSLDGTLYDDDDDDDDIERASKISSEDGEETRAYFYESDDSVEAQVKAPYSGEMDLLGE
FT ILDTLSTHSSDQGKLAPAKSLDFFRSMDDIDYKPTNKSNAPSENNLALLCASGDQGEWN
FT LGQDDSALHGRQLPPSPRKRVSSGGLTESLFILKEESREKPLCADSVSGPTVVGKPAPT
FT SGLRSQPAAPEASQTERGRAEVKQTPGQAPLQSEDLSVPGPGSRQSTFVPWEKAGKEDT
FT KPSKDVGLLQEVVSLCHMSCDFQQDLNISEESRSGNQT -> VSPSHLRL (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_058175"
FT VAR_SEQ 394..766
FT /note="GSPRSYQQWVYTVKKGGALFNTAVTKATPAVRTAYKFAKSHARLGLKEVKSR
FT LKHKDNEEEYGTCSGLVQYTPVYTLHNEKGENREKHKLSQTHLKRPHKSLDGTLYDDDD
FT DDDDIERASKISSEDGEETRAYFYESDDSVEAQVKAPYSGEMDLLGEILDTLSTHSSDQ
FT GKLAPAKSLDFFRSMDDIDYKPTNKSNAPSENNLALLCASGDQGEWNLGQDDSALHGRQ
FT LPPSPRKRVSSGGLTESLFILKEESREKPLCADSVSGPTVVGKPAPTSGLRSQPAAPEA
FT SQTERGRAEVKQTPGQAPLQSEDLSVPGPGSRQSTFVPWEKAGKEDTKPSKDVGLLQEV
FT VSLCHMSCDFQQDLNISEESRSGNQT -> GKDSLESNYLDI (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_058176"
FT MUTAGEN 246
FT /note="G->D: Abolishes guanine nucleotide exchange factor
FT (GEF) activity and impaired TCR down-modulation and
FT recycling in TH2 cells."
FT /evidence="ECO:0000269|PubMed:26774822"
FT MUTAGEN 482
FT /note="K->A: Impaired interaction with the AP-2 complex and
FT impaired TCR down-modulation and recycling in TH2 cells;
FT when associated with 547-A--A-549."
FT /evidence="ECO:0000269|PubMed:26774822"
FT MUTAGEN 547..549
FT /note="DLL->AAA: Impaired interaction with the AP-2 complex
FT and impaired TCR down-modulation and recycling in TH2
FT cells; when associated with A-482."
FT /evidence="ECO:0000269|PubMed:26774822"
SQ SEQUENCE 766 AA; 85526 MW; 1CF3B3EEC8E5FB7F CRC64;
MDRRTRENPE RTFDLVLKVK CHASENEDPE VLWKFPEDFG DQEVLQSVPK FCFPFDVERV
SQNQVGQHFT FVLTDMESKQ RFGFCRLTSG GRICLCILSY LPWFEVYYKL LNTLADYLAK
ELEEDLNETL KSLYNHPVPK ANTPVNLSVH SCFITPDITG LPTIPESRNL TEYFVAVDVN
NMLRLYASML HERRIIITSS KLSTLTACLH GSAALLYPMY WQHIYIPVLP PHLLDYCCAP
MPYLIGIHSS LIERVKNKSL EDVVVLNVDT NTLESPFNDL SSLPSDVVSA LKNKLKKQST
ATGDGVARAF LRAQAALFGS YRDALRYKPG EPITFCEESF VKHRSSVMKQ FLETAVNLQL
FKQFIDGRLA KLNAGRGFSD IFEEEITSGG FCGGSPRSYQ QWVYTVKKGG ALFNTAVTKA
TPAVRTAYKF AKSHARLGLK EVKSRLKHKD NEEEYGTCSG LVQYTPVYTL HNEKGENREK
HKLSQTHLKR PHKSLDGTLY DDDDDDDDIE RASKISSEDG EETRAYFYES DDSVEAQVKA
PYSGEMDLLG EILDTLSTHS SDQGKLAPAK SLDFFRSMDD IDYKPTNKSN APSENNLALL
CASGDQGEWN LGQDDSALHG RQLPPSPRKR VSSGGLTESL FILKEESREK PLCADSVSGP
TVVGKPAPTS GLRSQPAAPE ASQTERGRAE VKQTPGQAPL QSEDLSVPGP GSRQSTFVPW
EKAGKEDTKP SKDVGLLQEV VSLCHMSCDF QQDLNISEES RSGNQT
