ULK4_HUMAN
ID ULK4_HUMAN Reviewed; 1275 AA.
AC Q96C45; A6NF15; B3KSE5; B4E2M4; Q8IW79; Q9NWV6; Q9UF96;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Serine/threonine-protein kinase ULK4;
DE EC=2.7.11.1;
DE AltName: Full=Unc-51-like kinase 4;
GN Name=ULK4;
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 MRNA], AND VARIANTS GLY-348; ARG-569;
RP ALA-640 AND THR-715.
RC TISSUE=Kidney proximal tubule, Testis, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-580 AND 985-1275.
RC TISSUE=Brain, and Lymph;
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 953-1275.
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 [5]
RP 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 [6]
RP INVOLVEMENT IN SCHIZOPHRENIA, FUNCTION, TISSUE SPECIFICITY, AND INDUCTION
RP BY RETINOIC ACID.
RX PubMed=24284070; DOI=10.1242/jcs.137604;
RA Lang B., Pu J., Hunter I., Liu M., Martin-Granados C., Reilly T.J.,
RA Gao G.D., Guan Z.L., Li W.D., Shi Y.Y., He G., He L., Stefansson H.,
RA St Clair D., Blackwood D.H., McCaig C.D., Shen S.;
RT "Recurrent deletions of ULK4 in schizophrenia: a gene crucial for
RT neuritogenesis and neuronal motility.";
RL J. Cell Sci. 127:630-640(2014).
RN [7]
RP VARIANTS [LARGE SCALE ANALYSIS] ALA-18; ARG-39; LYS-139; ASN-223; GLY-348;
RP MET-415 AND PRO-417.
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).
CC -!- FUNCTION: May be involved in the remodeling of cytoskeletal components,
CC such as alpha-tubulin, and in this way regulates neurite branching and
CC elongation, as well as cell motility. {ECO:0000269|PubMed:24284070}.
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 -!- TISSUE SPECIFICITY: Expressed in the brain, mainly in postmitotic
CC neurons, including GABAergic neurons, but not in astrocytes (at protein
CC level). {ECO:0000269|PubMed:24284070}.
CC -!- INDUCTION: Up-regulated during neuronal differentiation of
CC neuroblastoma cells treated with all-trans or 9-cis retinoic acid.
CC {ECO:0000269|PubMed:24284070}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- DISEASE: Note=Various anomalies in ULK4 gene have been reported for
CC several cases of schizophrenia, schizophrenia plus bipolar disorder and
CC autism. ULK4 gene has been proposed to be a rare susceptibility risk
CC factor for a range of psychiatric diseases including schizophrenia.
CC {ECO:0000269|PubMed:24284070}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. APG1/unc-51/ULK1 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91270.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAG52707.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK000581; BAA91270.1; ALT_FRAME; mRNA.
DR EMBL; AK093396; BAG52707.1; ALT_INIT; mRNA.
DR EMBL; AK304341; BAG65186.1; -; mRNA.
DR EMBL; AC104305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014794; AAH14794.1; -; mRNA.
DR EMBL; BC040739; AAH40739.1; -; mRNA.
DR EMBL; AL133104; CAB61411.1; -; mRNA.
DR CCDS; CCDS43071.1; -.
DR PIR; T42683; T42683.
DR RefSeq; NP_060356.2; NM_017886.3.
DR PDB; 6TSZ; X-ray; 1.90 A; U=2-288.
DR PDB; 6U5L; X-ray; 1.75 A; A=1-285.
DR PDBsum; 6TSZ; -.
DR PDBsum; 6U5L; -.
DR AlphaFoldDB; Q96C45; -.
DR SMR; Q96C45; -.
DR BioGRID; 120321; 8.
DR IntAct; Q96C45; 19.
DR STRING; 9606.ENSP00000301831; -.
DR iPTMnet; Q96C45; -.
DR PhosphoSitePlus; Q96C45; -.
DR BioMuta; ULK4; -.
DR DMDM; 118574241; -.
DR EPD; Q96C45; -.
DR jPOST; Q96C45; -.
DR MassIVE; Q96C45; -.
DR PaxDb; Q96C45; -.
DR PeptideAtlas; Q96C45; -.
DR PRIDE; Q96C45; -.
DR ProteomicsDB; 76159; -.
DR Antibodypedia; 6576; 112 antibodies from 28 providers.
DR DNASU; 54986; -.
DR Ensembl; ENST00000301831.9; ENSP00000301831.4; ENSG00000168038.11.
DR GeneID; 54986; -.
DR KEGG; hsa:54986; -.
DR MANE-Select; ENST00000301831.9; ENSP00000301831.4; NM_017886.4; NP_060356.2.
DR UCSC; uc003ckv.5; human.
DR CTD; 54986; -.
DR DisGeNET; 54986; -.
DR GeneCards; ULK4; -.
DR HGNC; HGNC:15784; ULK4.
DR HPA; ENSG00000168038; Tissue enhanced (testis).
DR MIM; 617010; gene.
DR neXtProt; NX_Q96C45; -.
DR OpenTargets; ENSG00000168038; -.
DR PharmGKB; PA134978836; -.
DR VEuPathDB; HostDB:ENSG00000168038; -.
DR eggNOG; KOG0597; Eukaryota.
DR GeneTree; ENSGT00940000156541; -.
DR HOGENOM; CLU_002110_0_0_1; -.
DR InParanoid; Q96C45; -.
DR OMA; NWYETNN; -.
DR OrthoDB; 219167at2759; -.
DR PhylomeDB; Q96C45; -.
DR TreeFam; TF332678; -.
DR PathwayCommons; Q96C45; -.
DR SignaLink; Q96C45; -.
DR BioGRID-ORCS; 54986; 13 hits in 1112 CRISPR screens.
DR ChiTaRS; ULK4; human.
DR GenomeRNAi; 54986; -.
DR Pharos; Q96C45; Tbio.
DR PRO; PR:Q96C45; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q96C45; protein.
DR Bgee; ENSG00000168038; Expressed in decidua and 137 other tissues.
DR ExpressionAtlas; Q96C45; baseline and differential.
DR Genevisible; Q96C45; HS.
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:0000226; P:microtubule cytoskeleton organization; IMP:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0046328; P:regulation of JNK cascade; IMP:MGI.
DR GO; GO:0043408; P:regulation of MAPK cascade; IMP:MGI.
DR GO; GO:2001222; P:regulation of neuron migration; IMP:MGI.
DR GO; GO:0010975; P:regulation of neuron projection development; IMP:MGI.
DR GO; GO:1900744; P:regulation of p38MAPK cascade; IMP:MGI.
DR GO; GO:0090036; P:regulation of protein kinase C signaling; IMP:MGI.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR045906; ULK4.
DR PANTHER; PTHR46240; PTHR46240; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Repeat; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1275
FT /note="Serine/threonine-protein kinase ULK4"
FT /id="PRO_0000260154"
FT DOMAIN 4..280
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REPEAT 842..880
FT /note="HEAT 1"
FT REPEAT 926..964
FT /note="HEAT 2"
FT REPEAT 1025..1063
FT /note="HEAT 3"
FT REPEAT 1151..1189
FT /note="HEAT 4"
FT REPEAT 1213..1253
FT /note="HEAT 5"
FT REGION 299..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 18
FT /note="V -> A (in dbSNP:rs34538622)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041286"
FT VARIANT 39
FT /note="K -> R (in dbSNP:rs2272007)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041287"
FT VARIANT 139
FT /note="N -> K (in dbSNP:rs35833603)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041288"
FT VARIANT 223
FT /note="S -> N (in dbSNP:rs55840267)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041289"
FT VARIANT 224
FT /note="I -> V (in dbSNP:rs1716975)"
FT /id="VAR_051679"
FT VARIANT 348
FT /note="S -> G (in dbSNP:rs35263917)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:17344846"
FT /id="VAR_041290"
FT VARIANT 415
FT /note="T -> M (in dbSNP:rs371185820)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041291"
FT VARIANT 417
FT /note="S -> P (in dbSNP:rs75907560)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041292"
FT VARIANT 542
FT /note="A -> T (in dbSNP:rs1052501)"
FT /id="VAR_029005"
FT VARIANT 569
FT /note="K -> R (in dbSNP:rs3774372)"
FT /id="VAR_029006"
FT VARIANT 603
FT /note="L -> S (in dbSNP:rs17063572)"
FT /id="VAR_029007"
FT VARIANT 640
FT /note="S -> A (in dbSNP:rs4973986)"
FT /id="VAR_029008"
FT VARIANT 715
FT /note="A -> T (in dbSNP:rs17215589)"
FT /id="VAR_029009"
FT VARIANT 1260
FT /note="S -> N (in dbSNP:rs12488691)"
FT /id="VAR_059772"
FT VARIANT 1261
FT /note="A -> V (in dbSNP:rs6769117)"
FT /id="VAR_051680"
FT CONFLICT 388
FT /note="K -> E (in Ref. 1; BAA91270)"
FT /evidence="ECO:0000305"
FT CONFLICT 553..580
FT /note="AIVLLTELIRENFRNSKLKQCLLPTLGE -> TTSSIGIGILNCLVQHSTPV
FT PRQCLVYV (in Ref. 3; AAH14794)"
FT /evidence="ECO:0000305"
FT CONFLICT 732
FT /note="G -> V (in Ref. 1; BAA91270)"
FT /evidence="ECO:0000305"
FT CONFLICT 1024
FT /note="R -> S (in Ref. 3; AAH40739)"
FT /evidence="ECO:0000305"
FT HELIX 1..3
FT /evidence="ECO:0007829|PDB:6U5L"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:6U5L"
FT STRAND 16..23
FT /evidence="ECO:0007829|PDB:6U5L"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:6U5L"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:6U5L"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:6U5L"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:6U5L"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:6U5L"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:6U5L"
FT HELIX 95..114
FT /evidence="ECO:0007829|PDB:6U5L"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:6U5L"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:6U5L"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:6U5L"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:6U5L"
FT HELIX 150..160
FT /evidence="ECO:0007829|PDB:6U5L"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:6U5L"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:6TSZ"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:6U5L"
FT HELIX 198..214
FT /evidence="ECO:0007829|PDB:6U5L"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:6U5L"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:6U5L"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:6U5L"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:6U5L"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:6U5L"
FT TURN 281..284
FT /evidence="ECO:0007829|PDB:6U5L"
SQ SEQUENCE 1275 AA; 142442 MW; D3DB6795CEB1DC76 CRC64;
MENFILYEEI GRGSKTVVYK GRRKGTINFV AILCTDKCKR PEITNWVRLT REIKHKNIVT
FHEWYETSNH LWLVVELCTG GSLKTVIAQD ENLPEDVVRE FGIDLISGLH HLHKLGILFC
DISPRKILLE GPGTLKFSNF CLAKVEGENL EEFFALVAAE EGGGDNGENV LKKSMKSRVK
GSPVYTAPEV VRGADFSISS DLWSLGCLLY EMFSGKPPFF SESISELTEK ILCEDPLPPI
PKDSSRPKAS SDFINLLDGL LQRDPQKRLT WTRLLQHSFW KKAFAGADQE SSVEDLSLSR
NTMECSGPQD SKELLQNSQS RQAKGHKSGQ PLGHSFRLEN PTEFRPKSTL EGQLNESMFL
LSSRPTPRTS TAVEVSPGED MTHCSPQKTS PLTKITSGHL SQQDLESQMR ELIYTDSDLV
VTPIIDNPKI MKQPPVKFDA KILHLPTYSV DKLLFLKDQD WNDFLQQVCS QIDSTEKSMG
ASRAKLNLLC YLCVVAGHQE VATRLLHSPL FQLLIQHLRI APNWDIRAKV AHVIGLLASH
TAELQENTPV VEAIVLLTEL IRENFRNSKL KQCLLPTLGE LIYLVATQEE KKKNPRECWA
VPLAAYTVLM RCLREGEERV VNHMAAKIIE NVCTTFSAQS QGFITGEIGP ILWYLFRHST
ADSLRITAVS ALCRITRHSP TAFQNVIEKV GLNSVINSLA SAICKVQQYM LTLFAAMLSC
GIHLQRLIQE KGFVSTIIRL LDSPSTCIRA KAFLVLLYIL IYNREMLLLS CQARLVMYIE
RDSRKTTPGK EQQSGNEYLS KCLDLLICHI VQELPRILGD ILNSLANVSG RKHPSTVQVK
QLKLCLPLMP VVLHLVTSQV FRPQVVTEEF LFSYGTILSH IKSVDSGETN IDGAIGLTAS
EEFIKITLSA FEAIIQYPIL LKDYRSTVVD YILPPLVSLV QSQNVEWRLF SLRLLSETTS
LLVNQEFGDG KEKASVDSDS NLLALIRDVL LPQYEHILLE PDPVPAYALK LLVAMTEHNP
TFTRLVEESK LIPLIFEVTL EHQESILGNT MQSVIALLSN LVACKDSNME LLYEQGLVSH
ICNLLTETAT LCLDVDNKNN NEMAAPLLFS LLDILHSMLT YTSGIVRLAL QAQKSGSGED
PQAAEDLLLL NRPLTDLISL LIPLLPNEDP EIFDVSSKCL SILVQLYGGE NPDSLSPENV
EIFAHLLTSK EDPKEQKLLL RILRRMITSN EKHLESLKNA GSLLRALERL APGSGSFADS
AVAPLALEIL QAVGH
