RIPK4_HUMAN
ID RIPK4_HUMAN Reviewed; 832 AA.
AC P57078; Q96KH0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Receptor-interacting serine/threonine-protein kinase 4;
DE EC=2.7.11.1;
DE AltName: Full=Ankyrin repeat domain-containing protein 3;
DE AltName: Full=PKC-delta-interacting protein kinase;
GN Name=RIPK4; Synonyms=ANKRD3, DIK;
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 [MRNA] (ISOFORM 2).
RC TISSUE=Fetal kidney, and Fetal lung;
RA Shimizu N., Kudoh J., Shibuya K.;
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [3]
RP PROTEOLYTIC CLEAVAGE AT ASP-388 AND ASP-426, INTERACTION WITH TRAF1; TRAF2;
RP TRAF3 AND TRAF5, AND FUNCTION.
RX PubMed=12446564; DOI=10.1093/embo-reports/kvf236;
RA Meylan E., Martinon F., Thome M., Gschwendt M., Tschopp J.;
RT "RIP4 (DIK/PKK), a novel member of the RIP kinase family, activates NF-
RT kappa B and is processed during apoptosis.";
RL EMBO Rep. 3:1201-1208(2002).
RN [4]
RP UBIQUITINATION AT LYS-51 AND LYS-145, UBIQUITINATION BY BIRC2/C-IAP1 AND
RP BIRC3/C-IAP2, AND INTERACTION WITH BIRC2/C-IAP1; BIRC3/C-IAP2 AND
RP XIAP/BIRC4.
RX PubMed=21931591; DOI=10.1371/journal.pone.0022356;
RA Bertrand M.J., Lippens S., Staes A., Gilbert B., Roelandt R., De Medts J.,
RA Gevaert K., Declercq W., Vandenabeele P.;
RT "cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin
RT chains to receptor interacting proteins kinases 1 to 4 (RIP1-4).";
RL PLoS ONE 6:E22356-E22356(2011).
RN [5]
RP FUNCTION, AND VARIANT BPS ASN-81.
RX PubMed=22197488; DOI=10.1016/j.ajhg.2011.11.013;
RA Mitchell K., O'Sullivan J., Missero C., Blair E., Richardson R.,
RA Anderson B., Antonini D., Murray J.C., Shanske A.L., Schutte B.C.,
RA Romano R.A., Sinha S., Bhaskar S.S., Black G.C., Dixon J., Dixon M.J.;
RT "Exome sequence identifies RIPK4 as the Bartsocas-Papas syndrome locus.";
RL Am. J. Hum. Genet. 90:69-75(2012).
RN [6]
RP VARIANTS [LARGE SCALE ANALYSIS] ASN-462; MET-463; TYR-562; HIS-669 AND
RP SER-749.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [7]
RP VARIANTS BPS ASN-121 AND ILE-184, AND CHARACTERIZATION OF VARIANTS BPS
RP ASN-121 AND ILE-184.
RX PubMed=22197489; DOI=10.1016/j.ajhg.2011.11.014;
RA Kalay E., Sezgin O., Chellappa V., Mutlu M., Morsy H., Kayserili H.,
RA Kreiger E., Cansu A., Toraman B., Abdalla E.M., Aslan Y., Pillai S.,
RA Akarsu N.A.;
RT "Mutations in RIPK4 cause the autosomal-recessive form of popliteal
RT pterygium syndrome.";
RL Am. J. Hum. Genet. 90:76-85(2012).
RN [8]
RP INVOLVEMENT IN CHANDS, AND VARIANT CHANDS ASP-163.
RX PubMed=23610050; DOI=10.1002/ajmg.a.35913;
RA Gripp K.W., Ennis S., Napoli J.;
RT "Exome analysis in clinical practice: expanding the phenotype of Bartsocas-
RT Papas syndrome.";
RL Am. J. Med. Genet. A 161A:1058-1063(2013).
RN [9]
RP INVOLVEMENT IN CHANDS, VARIANT CHANDS LYS-284, AND TISSUE SPECIFICITY.
RX PubMed=26129644; DOI=10.1002/ajmg.a.37233;
RA Gollasch B., Basmanav F.B., Nanda A., Fritz G., Mahmoudi H., Thiele H.,
RA Wehner M., Wolf S., Altmueller J., Nuernberg P., Frank J., Betz R.C.;
RT "Identification of a novel mutation in RIPK4 in a kindred with phenotypic
RT features of Bartsocas-Papas and CHAND syndromes.";
RL Am. J. Med. Genet. A 167A:2555-2562(2015).
RN [10]
RP VARIANTS BPS LEU-189; PRO-496 AND HIS-666.
RX PubMed=25691407; DOI=10.1002/ajmg.a.36896;
RA Leslie E.J., O'Sullivan J., Cunningham M.L., Singh A., Goudy S.L.,
RA Ababneh F., Alsubaie L., Ch'ng G.S., van der Laar I.M., Hoogeboom A.J.,
RA Dunnwald M., Kapoor S., Jiramongkolchai P., Standley J., Manak J.R.,
RA Murray J.C., Dixon M.J.;
RT "Expanding the genetic and phenotypic spectrum of popliteal pterygium
RT disorders.";
RL Am. J. Med. Genet. A 167A:545-552(2015).
CC -!- FUNCTION: Involved in stratified epithelial development. It is a direct
CC transcriptional target of TP63. Plays a role in NF-kappa-B activation.
CC {ECO:0000269|PubMed:12446564, ECO:0000269|PubMed:22197488}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with PRKCB (By similarity). Interacts with TRAF1,
CC TRAF2, TRAF3 and TRAF5. Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and
CC XIAP/BIRC4. {ECO:0000250, ECO:0000269|PubMed:12446564,
CC ECO:0000269|PubMed:21931591}.
CC -!- INTERACTION:
CC P57078; Q13490: BIRC2; NbExp=3; IntAct=EBI-4422308, EBI-514538;
CC P57078; Q13489: BIRC3; NbExp=3; IntAct=EBI-4422308, EBI-517709;
CC P57078; O14641: DVL2; NbExp=4; IntAct=EBI-4422308, EBI-740850;
CC P57078; Q9NWT6: HIF1AN; NbExp=4; IntAct=EBI-4422308, EBI-745632;
CC P57078; P98170: XIAP; NbExp=2; IntAct=EBI-4422308, EBI-517127;
CC P57078-2; Q9Y4H4: GPSM3; NbExp=3; IntAct=EBI-12854608, EBI-347538;
CC P57078-2; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-12854608, EBI-11959123;
CC P57078-2; B2RUY7: VWC2L; NbExp=3; IntAct=EBI-12854608, EBI-11747707;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P57078-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P57078-2; Sequence=VSP_004862;
CC -!- TISSUE SPECIFICITY: Expressed in hair follicles and skin.
CC {ECO:0000269|PubMed:26129644}.
CC -!- PTM: May be phosphorylated by MAP3K2 and MAP3K3. {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved by during Fas-induced apoptosis. Cleavage
CC at Asp-388 and Asp-426. {ECO:0000269|PubMed:12446564}.
CC -!- PTM: Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by
CC BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-B.
CC {ECO:0000269|PubMed:21931591}.
CC -!- DISEASE: Bartsocas-Papas syndrome (BPS) [MIM:263650]: An autosomal
CC recessive disorder characterized by multiple popliteal pterygia leading
CC to severe arthrogryposis, ankyloblepharon filiforme adnatum, filiform
CC bands between the jaws, synostosis of the carpal/tarsal and phalangeal
CC bones in the hands and feet, digital hypoplasia/aplasia, complete soft-
CC tissue syndactyly, lack of nails, lack of scalp hair, eyebrows and
CC eyelashes, blepharophimosis, cleft lip and/or palate, and hypoplastic
CC external genitalia. Early lethality is common, although survival into
CC childhood and beyond has been reported. {ECO:0000269|PubMed:22197488,
CC ECO:0000269|PubMed:22197489, ECO:0000269|PubMed:25691407}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: CHAND syndrome (CHANDS) [MIM:214350]: An autosomal recessive
CC syndrome characterized by ankyloblepharon, sparse, curly and woolly
CC hair, nail dysplasia, and oral frenula. {ECO:0000269|PubMed:23610050,
CC ECO:0000269|PubMed:26129644}. Note=The disease may be caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AB047783; BAB56136.1; -; mRNA.
DR EMBL; AP001743; BAA95526.1; -; Genomic_DNA.
DR CCDS; CCDS13675.1; -. [P57078-2]
DR AlphaFoldDB; P57078; -.
DR SMR; P57078; -.
DR DIP; DIP-40722N; -.
DR IntAct; P57078; 379.
DR STRING; 9606.ENSP00000332454; -.
DR BindingDB; P57078; -.
DR ChEMBL; CHEMBL6083; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; P57078; -.
DR iPTMnet; P57078; -.
DR PhosphoSitePlus; P57078; -.
DR BioMuta; RIPK4; -.
DR DMDM; 10719883; -.
DR EPD; P57078; -.
DR jPOST; P57078; -.
DR MassIVE; P57078; -.
DR MaxQB; P57078; -.
DR PeptideAtlas; P57078; -.
DR PRIDE; P57078; -.
DR ProteomicsDB; 56989; -. [P57078-1]
DR ProteomicsDB; 56990; -. [P57078-2]
DR Antibodypedia; 9243; 307 antibodies from 27 providers.
DR Ensembl; ENST00000332512.8; ENSP00000332454.3; ENSG00000183421.12. [P57078-2]
DR Ensembl; ENST00000352483.3; ENSP00000330161.2; ENSG00000183421.12. [P57078-1]
DR MANE-Select; ENST00000332512.8; ENSP00000332454.3; NM_020639.3; NP_065690.2. [P57078-2]
DR UCSC; uc002yzn.2; human. [P57078-1]
DR GeneCards; RIPK4; -.
DR HGNC; HGNC:496; RIPK4.
DR HPA; ENSG00000183421; Tissue enhanced (esophagus).
DR MalaCards; RIPK4; -.
DR MIM; 214350; phenotype.
DR MIM; 263650; phenotype.
DR MIM; 605706; gene.
DR neXtProt; NX_P57078; -.
DR OpenTargets; ENSG00000183421; -.
DR Orphanet; 1234; Bartsocas-Papas syndrome.
DR Orphanet; 1401; CHAND syndrome.
DR VEuPathDB; HostDB:ENSG00000183421; -.
DR eggNOG; KOG0192; Eukaryota.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000159908; -.
DR HOGENOM; CLU_015188_0_0_1; -.
DR InParanoid; P57078; -.
DR OMA; HSKENTC; -.
DR PhylomeDB; P57078; -.
DR TreeFam; TF106506; -.
DR PathwayCommons; P57078; -.
DR SignaLink; P57078; -.
DR ChiTaRS; RIPK4; human.
DR Pharos; P57078; Tchem.
DR PRO; PR:P57078; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P57078; protein.
DR Bgee; ENSG00000183421; Expressed in esophagus squamous epithelium and 128 other tissues.
DR Genevisible; P57078; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF12796; Ank_2; 4.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 10.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 9.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; ATP-binding; Cytoplasm; Disease variant;
KW Ectodermal dysplasia; Isopeptide bond; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase; Ubl conjugation.
FT CHAIN 1..832
FT /note="Receptor-interacting serine/threonine-protein kinase
FT 4"
FT /id="PRO_0000086613"
FT DOMAIN 22..286
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 485..514
FT /note="ANK 1"
FT REPEAT 518..547
FT /note="ANK 2"
FT REPEAT 551..580
FT /note="ANK 3"
FT REPEAT 584..613
FT /note="ANK 4"
FT REPEAT 617..647
FT /note="ANK 5"
FT REPEAT 651..680
FT /note="ANK 6"
FT REPEAT 684..713
FT /note="ANK 7"
FT REPEAT 717..746
FT /note="ANK 8"
FT REPEAT 750..780
FT /note="ANK 9"
FT REPEAT 782..811
FT /note="ANK 10"
FT REGION 325..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 28..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT SITE 388..389
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:12446564"
FT SITE 426..427
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:12446564"
FT CROSSLNK 51
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:21931591"
FT CROSSLNK 145
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:21931591"
FT VAR_SEQ 278..325
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_004862"
FT VARIANT 12
FT /note="A -> G (in dbSNP:rs6586239)"
FT /id="VAR_030160"
FT VARIANT 81
FT /note="I -> N (in BPS; dbSNP:rs387906922)"
FT /evidence="ECO:0000269|PubMed:22197488"
FT /id="VAR_067331"
FT VARIANT 121
FT /note="I -> N (in BPS; loss of function;
FT dbSNP:rs387906923)"
FT /evidence="ECO:0000269|PubMed:22197489"
FT /id="VAR_067332"
FT VARIANT 163
FT /note="G -> D (in CHANDS; unknown pathological
FT significance; dbSNP:rs764278537)"
FT /evidence="ECO:0000269|PubMed:23610050"
FT /id="VAR_081473"
FT VARIANT 177
FT /note="S -> N (in dbSNP:rs12482626)"
FT /id="VAR_030161"
FT VARIANT 184
FT /note="T -> I (in BPS; loss of function)"
FT /evidence="ECO:0000269|PubMed:22197489"
FT /id="VAR_067333"
FT VARIANT 189
FT /note="P -> L (in BPS; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:25691407"
FT /id="VAR_085697"
FT VARIANT 284
FT /note="E -> K (in CHANDS; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:26129644"
FT /id="VAR_081474"
FT VARIANT 462
FT /note="I -> N (in dbSNP:rs55809511)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041050"
FT VARIANT 463
FT /note="V -> M (in dbSNP:rs55645753)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041051"
FT VARIANT 496
FT /note="A -> P (in BPS; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:25691407"
FT /id="VAR_085698"
FT VARIANT 562
FT /note="N -> Y (in dbSNP:rs55829311)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041052"
FT VARIANT 666
FT /note="R -> H (in BPS; unknown pathological significance;
FT dbSNP:rs763794698)"
FT /evidence="ECO:0000269|PubMed:25691407"
FT /id="VAR_085699"
FT VARIANT 669
FT /note="R -> H (in dbSNP:rs56056485)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041053"
FT VARIANT 749
FT /note="P -> S (in dbSNP:rs35537517)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041054"
FT CONFLICT 714
FT /note="M -> V (in Ref. 1; BAB56136)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 832 AA; 91611 MW; 5D8FFFD5F04F7ECB CRC64;
MEGDGGTPWA LALLRTFDAG EFTGWEKVGS GGFGQVYKVR HVHWKTWLAI KCSPSLHVDD
RERMELLEEA KKMEMAKFRY ILPVYGICRE PVGLVMEYME TGSLEKLLAS EPLPWDLRFR
IIHETAVGMN FLHCMAPPLL HLDLKPANIL LDAHYHVKIS DFGLAKCNGL SHSHDLSMDG
LFGTIAYLPP ERIREKSRLF DTKHDVYSFA IVIWGVLTQK KPFADEKNIL HIMVKVVKGH
RPELPPVCRA RPRACSHLIR LMQRCWQGDP RVRPTFQGNG LNGELIRQVL AALLPVTGRW
RSPGEGFRLE SEVIIRVTCP LSSPQEITSE TEDLCEKPDD EVKETAHDLD VKSPPEPRSE
VVPARLKRAS APTFDNDYSL SELLSQLDSG VSQAVEGPEE LSRSSSESKL PSSGSGKRLS
GVSSVDSAFS SRGSLSLSFE REPSTSDLGT TDVQKKKLVD AIVSGDTSKL MKILQPQDVD
LALDSGASLL HLAVEAGQEE CAKWLLLNNA NPNLSNRRGS TPLHMAVERR VRGVVELLLA
RKISVNAKDE DQWTALHFAA QNGDESSTRL LLEKNASVNE VDFEGRTPMH VACQHGQENI
VRILLRRGVD VSLQGKDAWL PLHYAAWQGH LPIVKLLAKQ PGVSVNAQTL DGRTPLHLAA
QRGHYRVARI LIDLCSDVNV CSLLAQTPLH VAAETGHTST ARLLLHRGAG KEAMTSDGYT
ALHLAARNGH LATVKLLVEE KADVLARGPL NQTALHLAAA HGHSEVVEEL VSADVIDLFD
EQGLSALHLA AQGRHAQTVE TLLRHGAHIN LQSLKFQGGH GPAATLLRRS KT
