DC2I2_HUMAN
ID DC2I2_HUMAN Reviewed; 536 AA.
AC Q96EX3; Q5VXV4; Q9BV46;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Cytoplasmic dynein 2 intermediate chain 2;
DE AltName: Full=Dynein 2 intermediate chain 2;
DE AltName: Full=WD repeat-containing protein 34;
GN Name=DYNC2I2 {ECO:0000312|HGNC:HGNC:28296}; Synonyms=WDR34;
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=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Lung;
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 FUNCTION, INTERACTION WITH MAP3K7; TAB2; TAB3 AND TRAF6, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19521662; DOI=10.1007/s00018-009-0059-6;
RA Gao D., Wang R., Li B., Yang Y., Zhai Z., Chen D.Y.;
RT "WDR34 is a novel TAK1-associated suppressor of the IL-1R/TLR3/TLR4-induced
RT NF-kappaB activation pathway.";
RL Cell. Mol. Life Sci. 66:2573-2584(2009).
RN [4]
RP FUNCTION, AND VARIANTS SRTD11 VAL-341; MET-354; GLN-447 AND TRP-447.
RX PubMed=24183449; DOI=10.1016/j.ajhg.2013.10.007;
RA Huber C., Wu S., Kim A.S., Sigaudy S., Sarukhanov A., Serre V., Baujat G.,
RA Le Quan Sang K.H., Rimoin D.L., Cohn D.H., Munnich A., Krakow D.,
RA Cormier-Daire V.;
RT "WDR34 mutations that cause short-rib polydactyly syndrome type III/severe
RT asphyxiating thoracic dysplasia reveal a role for the NF-kappaB pathway in
RT cilia.";
RL Am. J. Hum. Genet. 93:926-931(2013).
RN [5]
RP VARIANTS SRTD11 PHE-148; LEU-390; SER-393; ILE-410; ARG-436 AND TRP-447,
RP AND VARIANTS VAL-22 AND CYS-206.
RX PubMed=24183451; DOI=10.1016/j.ajhg.2013.10.003;
RA Schmidts M., Vodopiutz J., Christou-Savina S., Cortes C.R.,
RA McInerney-Leo A.M., Emes R.D., Arts H.H., Tuysuz B., D'Silva J., Leo P.J.,
RA Giles T.C., Oud M.M., Harris J.A., Koopmans M., Marshall M., Elcioglu N.,
RA Kuechler A., Bockenhauer D., Moore A.T., Wilson L.C., Janecke A.R.,
RA Hurles M.E., Emmet W., Gardiner B., Streubel B., Dopita B., Zankl A.,
RA Kayserili H., Scambler P.J., Brown M.A., Beales P.L., Wicking C.,
RA Duncan E.L., Mitchison H.M.;
RT "Mutations in the gene encoding IFT dynein complex component WDR34 cause
RT Jeune asphyxiating thoracic dystrophy.";
RL Am. J. Hum. Genet. 93:932-944(2013).
RN [6]
RP IDENTIFICATION IN THE CYTOPLASMIC DYNEIN 2 COMPLEX, SUBCELLULAR LOCATION,
RP AND FUNCTION.
RX PubMed=25205765; DOI=10.1242/jcs.159038;
RA Asante D., Stevenson N.L., Stephens D.J.;
RT "Subunit composition of the human cytoplasmic dynein-2 complex.";
RL J. Cell Sci. 127:4774-4787(2014).
RN [7]
RP VARIANT SRTD11 TRP-182.
RX PubMed=29241935; DOI=10.1016/j.tjog.2017.10.033;
RA You S.H., Lee Y.S., Lee C.P., Lin C.P., Lin C.Y., Tsai C.L., Chang Y.L.,
RA Cheng P.J., Wang T.H., Chang S.D.;
RT "Identification of a c.544C>T mutation in WDR34 as a deleterious recessive
RT allele of short rib-polydactyly syndrome.";
RL Taiwan. J. Obstet. Gynecol. 56:857-862(2017).
RN [8]
RP INTERACTION WITH DYNC2I1, AND FUNCTION.
RX PubMed=29742051; DOI=10.1091/mbc.e18-03-0173;
RA Hamada Y., Tsurumi Y., Nozaki S., Katoh Y., Nakayama K.;
RT "Interaction of WDR60 intermediate chain with TCTEX1D2 light chain of the
RT dynein-2 complex is crucial for ciliary protein trafficking.";
RL Mol. Biol. Cell 29:1628-1639(2018).
RN [9]
RP FUNCTION.
RX PubMed=30320547; DOI=10.7554/elife.39655;
RA Vuolo L., Stevenson N.L., Heesom K.J., Stephens D.J.;
RT "Dynein-2 intermediate chains play crucial but distinct roles in primary
RT cilia formation and function.";
RL Elife 7:0-0(2018).
RN [10]
RP SUBUNIT, FUNCTION, AND INTERACTION WITH DYNLL2 AND DYNLRB1.
RX PubMed=30649997; DOI=10.1091/mbc.e18-10-0678;
RA Tsurumi Y., Hamada Y., Katoh Y., Nakayama K.;
RT "Interactions of the dynein-2 intermediate chain WDR34 with the light
RT chains are required for ciliary retrograde protein trafficking.";
RL Mol. Biol. Cell 30:658-670(2019).
RN [11] {ECO:0007744|PDB:6RLB, ECO:0007744|PDB:6SC2}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) OF THE DYNEIN-2 COMPLEX.
RX PubMed=31451806; DOI=10.1038/s41594-019-0286-y;
RA Toropova K., Zalyte R., Mukhopadhyay A.G., Mladenov M., Carter A.P.,
RA Roberts A.J.;
RT "Structure of the dynein-2 complex and its assembly with intraflagellar
RT transport trains.";
RL Nat. Struct. Mol. Biol. 26:823-829(2019).
CC -!- FUNCTION: Acts as one of several non-catalytic accessory components of
CC the cytoplasmic dynein 2 complex (dynein-2 complex), a motor protein
CC complex that drives the movement of cargos along microtubules within
CC cilia and flagella in concert with the intraflagellar transport (IFT)
CC system (PubMed:25205765, PubMed:29742051). DYNC2I2 plays a major role
CC in retrograde ciliary protein trafficking and in ciliogenesis
CC (PubMed:30649997, PubMed:29742051, PubMed:30320547). Required also to
CC maintain a functional transition zone (PubMed:30320547).
CC {ECO:0000269|PubMed:25205765, ECO:0000269|PubMed:29742051,
CC ECO:0000269|PubMed:30320547, ECO:0000269|PubMed:30649997}.
CC -!- FUNCTION: Acts as a negative regulator of the Toll-like and IL-1R
CC receptor signaling pathways. Inhibits the MAP3K7-induced NF-kappa-B
CC activation pathway. Inhibits MAP3K7 phosphorylation at 'Thr-184' and
CC 'Thr-187' upon Il-1 beta stimulation. {ECO:0000269|PubMed:19521662,
CC ECO:0000269|PubMed:24183449}.
CC -!- SUBUNIT: The cytoplasmic dynein 2 complex consists of two catalytic
CC heavy chains (HCs) and a number of non-catalytic subunits presented by
CC intermediate chains (ICs), light intermediate chains (LICs) and light
CC chains (LCs). Among them, a heavy chain (DYNC2H1), two intermediate
CC chains (DYNC2I2 and DYNC2I1), a light intermediate chain (DYNC2LI1),
CC and a light chain (DYNLT2B) are unique to the cytoplasmic dynein
CC complex 2, but a subset of the light chains are also shared by dynein-1
CC and dynein-2 complexes (PubMed:25205765, PubMed:31451806). Interacts
CC with DYNC2I1; their C-terminal domains each bind a copy of the heavy
CC chain, and their extended N-terminal regions are held together by an
CC array of light chain dimers (PubMed:29742051, PubMed:31451806).
CC Interacts with DYNLL2; this interaction is essential for dynein-2-
CC mediated retrograde trafficking of ciliary proteins (PubMed:30649997).
CC Interacts with DYNLRB1; this interaction is essential for dynein-2-
CC mediated retrograde trafficking of ciliary proteins (PubMed:30649997).
CC Interacts (via the WD domains) with MAP3K7 and TAB3. Interacts (via WD
CC domains) with TAB2 (via C-terminus). Interacts (via WD domains) with
CC TRAF6 (via TRAF-type domains) (PubMed:19521662).
CC {ECO:0000269|PubMed:19521662, ECO:0000269|PubMed:25205765,
CC ECO:0000269|PubMed:29742051, ECO:0000269|PubMed:30649997,
CC ECO:0000269|PubMed:31451806}.
CC -!- INTERACTION:
CC Q96EX3; P38432: COIL; NbExp=3; IntAct=EBI-2556091, EBI-945751;
CC Q96EX3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2556091, EBI-16439278;
CC Q96EX3; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-2556091, EBI-2130429;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19521662,
CC ECO:0000269|PubMed:25205765}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:19521662, ECO:0000269|PubMed:25205765}.
CC Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:19521662}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:25205765}. Cell projection, cilium
CC {ECO:0000269|PubMed:25205765}. Cell projection, filopodium
CC {ECO:0000250|UniProtKB:Q5U4F6}. Note=Concentrates around the centrioles
CC and basal bodies also showing axonemal staining.
CC {ECO:0000250|UniProtKB:Q5U4F6}.
CC -!- TISSUE SPECIFICITY: Expressed in several cell lines (at protein level).
CC {ECO:0000269|PubMed:19521662}.
CC -!- DISEASE: Short-rib thoracic dysplasia 11 with or without polydactyly
CC (SRTD11) [MIM:615633]: A form of short-rib thoracic dysplasia, a group
CC of autosomal recessive ciliopathies that are characterized by a
CC constricted thoracic cage, short ribs, shortened tubular bones, and a
CC 'trident' appearance of the acetabular roof. Polydactyly is variably
CC present. Non-skeletal involvement can include cleft lip/palate as well
CC as anomalies of major organs such as the brain, eye, heart, kidneys,
CC liver, pancreas, intestines, and genitalia. Some forms of the disease
CC are lethal in the neonatal period due to respiratory insufficiency
CC secondary to a severely restricted thoracic cage, whereas others are
CC compatible with life. Disease spectrum encompasses Ellis-van Creveld
CC syndrome, asphyxiating thoracic dystrophy (Jeune syndrome), Mainzer-
CC Saldino syndrome, and short rib-polydactyly syndrome.
CC {ECO:0000269|PubMed:24183449, ECO:0000269|PubMed:24183451,
CC ECO:0000269|PubMed:29241935}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the dynein light intermediate chain family.
CC {ECO:0000305}.
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DR EMBL; AL356481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001614; AAH01614.3; -; mRNA.
DR EMBL; BC011874; AAH11874.2; -; mRNA.
DR CCDS; CCDS6906.2; -.
DR RefSeq; NP_443076.2; NM_052844.3.
DR PDB; 6RLB; EM; 4.50 A; D=1-536.
DR PDB; 6SC2; EM; 3.90 A; D=1-536.
DR PDBsum; 6RLB; -.
DR PDBsum; 6SC2; -.
DR AlphaFoldDB; Q96EX3; -.
DR SMR; Q96EX3; -.
DR BioGRID; 124640; 52.
DR CORUM; Q96EX3; -.
DR IntAct; Q96EX3; 26.
DR MINT; Q96EX3; -.
DR STRING; 9606.ENSP00000361800; -.
DR iPTMnet; Q96EX3; -.
DR PhosphoSitePlus; Q96EX3; -.
DR BioMuta; WDR34; -.
DR DMDM; 88985038; -.
DR EPD; Q96EX3; -.
DR jPOST; Q96EX3; -.
DR MassIVE; Q96EX3; -.
DR MaxQB; Q96EX3; -.
DR PaxDb; Q96EX3; -.
DR PeptideAtlas; Q96EX3; -.
DR PRIDE; Q96EX3; -.
DR ProteomicsDB; 76465; -.
DR Antibodypedia; 31223; 120 antibodies from 18 providers.
DR DNASU; 89891; -.
DR Ensembl; ENST00000372715.7; ENSP00000361800.2; ENSG00000119333.12.
DR GeneID; 89891; -.
DR KEGG; hsa:89891; -.
DR MANE-Select; ENST00000372715.7; ENSP00000361800.2; NM_052844.4; NP_443076.2.
DR UCSC; uc004bvq.2; human.
DR CTD; 89891; -.
DR DisGeNET; 89891; -.
DR GeneCards; DYNC2I2; -.
DR HGNC; HGNC:28296; DYNC2I2.
DR HPA; ENSG00000119333; Low tissue specificity.
DR MalaCards; DYNC2I2; -.
DR MIM; 613363; gene.
DR MIM; 615633; phenotype.
DR neXtProt; NX_Q96EX3; -.
DR OpenTargets; ENSG00000119333; -.
DR Orphanet; 474; Jeune syndrome.
DR Orphanet; 93271; Short rib-polydactyly syndrome, Verma-Naumoff type.
DR VEuPathDB; HostDB:ENSG00000119333; -.
DR eggNOG; KOG1587; Eukaryota.
DR GeneTree; ENSGT00940000158483; -.
DR HOGENOM; CLU_031167_1_0_1; -.
DR InParanoid; Q96EX3; -.
DR OMA; KKYLFCV; -.
DR OrthoDB; 1453532at2759; -.
DR PhylomeDB; Q96EX3; -.
DR TreeFam; TF300553; -.
DR PathwayCommons; Q96EX3; -.
DR Reactome; R-HSA-5620924; Intraflagellar transport.
DR SignaLink; Q96EX3; -.
DR BioGRID-ORCS; 89891; 12 hits in 1084 CRISPR screens.
DR ChiTaRS; WDR34; human.
DR GenomeRNAi; 89891; -.
DR Pharos; Q96EX3; Tbio.
DR PRO; PR:Q96EX3; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q96EX3; protein.
DR Bgee; ENSG00000119333; Expressed in right uterine tube and 164 other tissues.
DR ExpressionAtlas; Q96EX3; baseline and differential.
DR Genevisible; Q96EX3; HS.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0097014; C:ciliary plasm; IBA:GO_Central.
DR GO; GO:0097542; C:ciliary tip; TAS:Reactome.
DR GO; GO:0005929; C:cilium; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0045504; F:dynein heavy chain binding; IBA:GO_Central.
DR GO; GO:0045503; F:dynein light chain binding; IPI:GO_Central.
DR GO; GO:0060271; P:cilium assembly; IGI:GO_Central.
DR GO; GO:0035721; P:intraciliary retrograde transport; IMP:UniProtKB.
DR GO; GO:0042073; P:intraciliary transport; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 2.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Ciliopathy; Cytoplasm; Cytoskeleton;
KW Disease variant; Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..536
FT /note="Cytoplasmic dynein 2 intermediate chain 2"
FT /id="PRO_0000051383"
FT REPEAT 215..255
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 264..308
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 390..430
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 433..473
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 480..520
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REGION 80..93
FT /note="DYNLL2 binding"
FT /evidence="ECO:0000269|PubMed:30649997"
FT REGION 106..131
FT /note="DYNLRB1 binding"
FT /evidence="ECO:0000269|PubMed:30649997"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U4F6"
FT VARIANT 22
FT /note="A -> V (in dbSNP:rs201715229)"
FT /evidence="ECO:0000269|PubMed:24183451"
FT /id="VAR_070962"
FT VARIANT 148
FT /note="C -> F (in SRTD11)"
FT /evidence="ECO:0000269|PubMed:24183451"
FT /id="VAR_070963"
FT VARIANT 182
FT /note="R -> W (in SRTD11)"
FT /evidence="ECO:0000269|PubMed:29241935"
FT /id="VAR_083840"
FT VARIANT 206
FT /note="R -> C (in dbSNP:rs148543026)"
FT /evidence="ECO:0000269|PubMed:24183451"
FT /id="VAR_070964"
FT VARIANT 341
FT /note="A -> V (in SRTD11; dbSNP:rs587777091)"
FT /evidence="ECO:0000269|PubMed:24183449"
FT /id="VAR_070965"
FT VARIANT 354
FT /note="T -> M (in SRTD11; dbSNP:rs587777092)"
FT /evidence="ECO:0000269|PubMed:24183449"
FT /id="VAR_070966"
FT VARIANT 390
FT /note="P -> L (in SRTD11)"
FT /evidence="ECO:0000269|PubMed:24183451"
FT /id="VAR_070967"
FT VARIANT 393
FT /note="G -> S (in SRTD11; dbSNP:rs587777096)"
FT /evidence="ECO:0000269|PubMed:24183451"
FT /id="VAR_070968"
FT VARIANT 410
FT /note="S -> I (in SRTD11)"
FT /evidence="ECO:0000269|PubMed:24183451"
FT /id="VAR_070969"
FT VARIANT 436
FT /note="K -> R (in SRTD11; dbSNP:rs587777098)"
FT /evidence="ECO:0000269|PubMed:24183451"
FT /id="VAR_070970"
FT VARIANT 447
FT /note="R -> Q (in SRTD11; dbSNP:rs587777094)"
FT /evidence="ECO:0000269|PubMed:24183449"
FT /id="VAR_070971"
FT VARIANT 447
FT /note="R -> W (in SRTD11; dbSNP:rs587777093)"
FT /evidence="ECO:0000269|PubMed:24183449,
FT ECO:0000269|PubMed:24183451"
FT /id="VAR_070972"
FT CONFLICT 60
FT /note="W -> G (in Ref. 2; AAH11874/AAH01614)"
FT /evidence="ECO:0000305"
FT CONFLICT 356
FT /note="G -> S (in Ref. 2; AAH01614)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 536 AA; 57801 MW; D23C2E0055120A4C CRC64;
MATRAQPGPL SQAGSAGVAA LATVGVASGP GPGRPGPLQD ETLGVASVPS QWRAVQGIRW
ETKSCQTASI ATASASAQAR NHVDAQVQTE APVPVSVQPP SQYDIPRLAA FLRRVEAMVI
RELNKNWQSH AFDGFEVNWT EQQQMVSCLY TLGYPPAQAQ GLHVTSISWN STGSVVACAY
GRLDHGDWST LKSFVCAWNL DRRDLRPQQP SAVVEVPSAV LCLAFHPTQP SHVAGGLYSG
EVLVWDLSRL EDPLLWRTGL TDDTHTDPVS QVVWLPEPGH SHRFQVLSVA TDGKVLLWQG
IGVGQLQLTE GFALVMQQLP RSTKLKKHPR GETEVGATAV AFSSFDPRLF ILGTEGGFPL
KCSLAAGEAA LTRMPSSVPL RAPAQFTFSP HGGPIYSVSC SPFHRNLFLS AGTDGHVHLY
SMLQAPPLTS LQLSLKYLFA VRWSPVRPLV FAAASGKGDV QLFDLQKSSQ KPTVLIKQTQ
DESPVYCLEF NSQQTQLLAA GDAQGTVKVW QLSTEFTEQG PREAEDLDCL AAEVAA
