TEX14_HUMAN
ID TEX14_HUMAN Reviewed; 1497 AA.
AC Q8IWB6; A6NH19; Q7RTP3; Q8ND97; Q9BXT9;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Inactive serine/threonine-protein kinase TEX14;
DE AltName: Full=Protein kinase-like protein SgK307;
DE AltName: Full=Sugen kinase 307;
DE AltName: Full=Testis-expressed sequence 14;
DE AltName: Full=Testis-expressed sequence 14 protein;
GN Name=TEX14; Synonyms=SGK307;
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] (ISOFORM 3).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [MRNA] OF 480-1497 (ISOFORM 3), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11279525; DOI=10.1038/86927;
RA Wang P.J., McCarrey J.R., Yang F., Page D.C.;
RT "An abundance of X-linked genes expressed in spermatogonia.";
RL Nat. Genet. 27:422-426(2001).
RN [5]
RP IDENTIFICATION, AND ALTERNATIVE SPLICING (ISOFORM 2).
RX PubMed=12711554; DOI=10.1016/s1567-133x(03)00036-x;
RA Wu M.-H., Rajkovic A., Burns K.H., Yan W., Lin Y.-N., Matzuk M.M.;
RT "Sequence and expression of testis-expressed gene 14 (Tex14): a gene
RT encoding a protein kinase preferentially expressed during
RT spermatogenesis.";
RL Gene Expr. Patterns 3:231-236(2003).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CEP55.
RX PubMed=20176808; DOI=10.1128/mcb.01392-09;
RA Iwamori T., Iwamori N., Ma L., Edson M.A., Greenbaum M.P., Matzuk M.M.;
RT "TEX14 interacts with CEP55 to block cell abscission.";
RL Mol. Cell. Biol. 30:2280-2292(2010).
RN [7]
RP PHOSPHORYLATION, AND MUTAGENESIS OF 614-SER--THR-618 AND 726-SER--THR-728.
RX PubMed=22405274; DOI=10.1016/j.molcel.2012.01.013;
RA Mondal G., Ohashi A., Yang L., Rowley M., Couch F.J.;
RT "Tex14, a plk1-regulated protein, is required for kinetochore-microtubule
RT attachment and regulation of the spindle assembly checkpoint.";
RL Mol. Cell 45:680-695(2012).
RN [8]
RP INVOLVEMENT IN SPGF23, AND TISSUE SPECIFICITY.
RX PubMed=28206990; DOI=10.1038/gim.2016.225;
RA Gershoni M., Hauser R., Yogev L., Lehavi O., Azem F., Yavetz H.,
RA Pietrokovski S., Kleiman S.E.;
RT "A familial study of azoospermic men identifies three novel causative
RT mutations in three new human azoospermia genes.";
RL Genet. Med. 19:998-1006(2017).
RN [9]
RP VARIANTS [LARGE SCALE ANALYSIS] GLY-88; GLU-321; CYS-443 AND MET-559.
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: Required both for the formation of intercellular bridges
CC during meiosis and for kinetochore-microtubule attachment during
CC mitosis. Intercellular bridges are evolutionarily conserved structures
CC that connect differentiating germ cells and are required for
CC spermatogenesis and male fertility. Acts by promoting the conversion of
CC midbodies into intercellular bridges via its interaction with CEP55:
CC interaction with CEP55 inhibits the interaction between CEP55 and
CC PDCD6IP/ALIX and TSG101, blocking cell abscission and leading to
CC transform midbodies into intercellular bridges. Also plays a role
CC during mitosis: recruited to kinetochores by PLK1 during early mitosis
CC and regulates the maturation of the outer kinetochores and microtubule
CC attachment. Has no protein kinase activity in vitro (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with KIF23 and RBM44. Interacts with CEP55;
CC inhibiting interaction between CEP55 and PDCD6IP/ALIX and TSG101 (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8IWB6; Q53EZ4: CEP55; NbExp=5; IntAct=EBI-6674697, EBI-747776;
CC Q8IWB6; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-6674697, EBI-742054;
CC Q8IWB6; Q9UBR4-2: LHX3; NbExp=5; IntAct=EBI-6674697, EBI-12039345;
CC Q8IWB6; P61968: LMO4; NbExp=3; IntAct=EBI-6674697, EBI-2798728;
CC Q8IWB6; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-6674697, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Midbody {ECO:0000250}.
CC Chromosome, centromere, kinetochore {ECO:0000250}. Note=Detected in the
CC intercellular bridges that connect male germ cell daughter cells after
CC cell division. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IWB6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IWB6-2; Sequence=VSP_019868;
CC Name=3;
CC IsoId=Q8IWB6-3; Sequence=VSP_019868, VSP_019869;
CC -!- TISSUE SPECIFICITY: Expression restricted to testis.
CC {ECO:0000269|PubMed:11279525, ECO:0000269|PubMed:28206990}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive.
CC -!- DOMAIN: The GPPX3Y motif mediates interaction with CEP55.
CC -!- PTM: Phosphorylated on Thr residues by CDK1 during early phases of
CC mitosis, promoting the interaction with PLK1 and recruitment to
CC kinetochores. Phosphorylated on Ser-437 by PLK1 during late
CC prometaphase promotes the rapid depletion from kinetochores and its
CC subsequent degradation by the APC/C complex.
CC {ECO:0000269|PubMed:22405274}.
CC -!- DISEASE: Spermatogenic failure 23 (SPGF23) [MIM:617707]: An infertility
CC disorder caused by spermatogenesis defects that result in non-
CC obstructive azoospermia. {ECO:0000269|PubMed:28206990}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
CC -!- CAUTION: Ser-376 is present instead of the conserved Asp which is
CC expected to be an active site residue. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK31980.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL834143; CAD38856.2; -; mRNA.
DR EMBL; AC005666; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040526; AAH40526.1; -; mRNA.
DR EMBL; AF285601; AAK31980.1; ALT_INIT; mRNA.
DR EMBL; BK000998; DAA01359.1; -; mRNA.
DR CCDS; CCDS32692.1; -. [Q8IWB6-3]
DR CCDS; CCDS32693.1; -. [Q8IWB6-2]
DR CCDS; CCDS56042.1; -. [Q8IWB6-1]
DR RefSeq; NP_001188386.1; NM_001201457.1. [Q8IWB6-1]
DR RefSeq; NP_112562.3; NM_031272.4. [Q8IWB6-3]
DR RefSeq; NP_938207.2; NM_198393.3. [Q8IWB6-2]
DR PDB; 3WUT; X-ray; 2.30 A; C/F/I/L=792-804.
DR PDB; 3WUU; X-ray; 2.90 A; C/F/I/L=791-805.
DR PDBsum; 3WUT; -.
DR PDBsum; 3WUU; -.
DR AlphaFoldDB; Q8IWB6; -.
DR SMR; Q8IWB6; -.
DR BioGRID; 121089; 8.
DR ELM; Q8IWB6; -.
DR IntAct; Q8IWB6; 29.
DR STRING; 9606.ENSP00000240361; -.
DR TCDB; 8.A.23.1.18; the basigin (basigin) family.
DR iPTMnet; Q8IWB6; -.
DR PhosphoSitePlus; Q8IWB6; -.
DR BioMuta; TEX14; -.
DR DMDM; 110816441; -.
DR MassIVE; Q8IWB6; -.
DR PaxDb; Q8IWB6; -.
DR PeptideAtlas; Q8IWB6; -.
DR PRIDE; Q8IWB6; -.
DR ProteomicsDB; 70835; -. [Q8IWB6-1]
DR ProteomicsDB; 70836; -. [Q8IWB6-2]
DR ProteomicsDB; 70837; -. [Q8IWB6-3]
DR Antibodypedia; 31015; 89 antibodies from 25 providers.
DR DNASU; 56155; -.
DR Ensembl; ENST00000240361.12; ENSP00000240361.8; ENSG00000121101.16. [Q8IWB6-1]
DR Ensembl; ENST00000349033.10; ENSP00000268910.8; ENSG00000121101.16. [Q8IWB6-3]
DR Ensembl; ENST00000389934.7; ENSP00000374584.3; ENSG00000121101.16. [Q8IWB6-2]
DR GeneID; 56155; -.
DR KEGG; hsa:56155; -.
DR MANE-Select; ENST00000349033.10; ENSP00000268910.8; NM_031272.5; NP_112562.3. [Q8IWB6-3]
DR UCSC; uc002iwr.3; human. [Q8IWB6-1]
DR CTD; 56155; -.
DR DisGeNET; 56155; -.
DR GeneCards; TEX14; -.
DR HGNC; HGNC:11737; TEX14.
DR HPA; ENSG00000121101; Tissue enriched (testis).
DR MalaCards; TEX14; -.
DR MIM; 605792; gene.
DR MIM; 617707; phenotype.
DR neXtProt; NX_Q8IWB6; -.
DR OpenTargets; ENSG00000121101; -.
DR Orphanet; 399805; Male infertility with azoospermia or oligozoospermia due to single gene mutation.
DR PharmGKB; PA36454; -.
DR VEuPathDB; HostDB:ENSG00000121101; -.
DR eggNOG; ENOG502QSZN; Eukaryota.
DR GeneTree; ENSGT00390000015123; -.
DR HOGENOM; CLU_004733_0_0_1; -.
DR InParanoid; Q8IWB6; -.
DR OMA; LCFQFYL; -.
DR OrthoDB; 92703at2759; -.
DR PhylomeDB; Q8IWB6; -.
DR TreeFam; TF328704; -.
DR PathwayCommons; Q8IWB6; -.
DR SignaLink; Q8IWB6; -.
DR BioGRID-ORCS; 56155; 9 hits in 1093 CRISPR screens.
DR ChiTaRS; TEX14; human.
DR GenomeRNAi; 56155; -.
DR Pharos; Q8IWB6; Tbio.
DR PRO; PR:Q8IWB6; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8IWB6; protein.
DR Bgee; ENSG00000121101; Expressed in right testis and 95 other tissues.
DR ExpressionAtlas; Q8IWB6; baseline and differential.
DR Genevisible; Q8IWB6; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; ISS:UniProtKB.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0043063; P:intercellular bridge organization; ISS:UniProtKB.
DR GO; GO:0007140; P:male meiotic nuclear division; ISS:UniProtKB.
DR GO; GO:0051306; P:mitotic sister chromatid separation; ISS:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0032466; P:negative regulation of cytokinesis; IEA:Ensembl.
DR GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR Gene3D; 1.25.40.20; -; 1.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR039339; Tex14.
DR PANTHER; PTHR23060; PTHR23060; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat; ATP-binding; Cell cycle;
KW Cell division; Centromere; Chromosome; Cytoplasm; Kinetochore; Mitosis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1497
FT /note="Inactive serine/threonine-protein kinase TEX14"
FT /id="PRO_0000246995"
FT REPEAT 27..54
FT /note="ANK 1"
FT REPEAT 55..84
FT /note="ANK 2"
FT REPEAT 88..117
FT /note="ANK 3"
FT DOMAIN 227..518
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 848..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1144..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1348..1470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 795..801
FT /note="GPPX3Y"
FT MOTIF 852..860
FT /note="D-box"
FT COMPBIAS 987..1020
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1348..1365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1367..1470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 233..241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1M5M3"
FT MOD_RES 437
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q7M6U3"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1M5M3"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F1M5M3"
FT MOD_RES 1106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7M6U3"
FT MOD_RES 1404
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7M6U3"
FT MOD_RES 1459
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7M6U3"
FT MOD_RES 1496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7M6U3"
FT VAR_SEQ 213..218
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11279525,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_019868"
FT VAR_SEQ 1064..1103
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11279525,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_019869"
FT VARIANT 88
FT /note="D -> G (in dbSNP:rs56292204)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041388"
FT VARIANT 321
FT /note="K -> E (in a gastric adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041389"
FT VARIANT 443
FT /note="S -> C"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041390"
FT VARIANT 559
FT /note="I -> M"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041391"
FT MUTAGEN 614..618
FT /note="SSPST->AAPAA: In PBD-1; reduced ability to interact
FT with PLK1."
FT /evidence="ECO:0000269|PubMed:22405274"
FT MUTAGEN 726..728
FT /note="STT->AAA: In PBD-5; reduced ability to interact with
FT PLK1."
FT /evidence="ECO:0000269|PubMed:22405274"
FT CONFLICT 1326
FT /note="H -> R (in Ref. 4; AAK31980)"
FT /evidence="ECO:0000305"
FT CONFLICT 1387
FT /note="L -> P (in Ref. 1; CAD38856)"
FT /evidence="ECO:0000305"
FT STRAND 797..800
FT /evidence="ECO:0007829|PDB:3WUT"
SQ SEQUENCE 1497 AA; 167901 MW; D7DC446A1A18FC4D CRC64;
MSRAVRLPVP CPVQLGTLRN DSLEAQLHEY VKQGNYVKVK KILKKGIYVD AVNSLGQTAL
FVAALLGLRK FVDVLVDYGS DPNHRCFDGS TPVHAAAFSG NQWILSKLLD AGGDLRLHDE
RGQNPKTWAL TAGKERSTQI VEFMQRCASH MQAIIQGFSY DLLKKIDSPQ RLVYSPSWCG
GLVQGNPNGS PNRLLKAGVI SAQNIYSFGF GKAMPWFQFY LTGATQMAYL GSLPVIGEKE
VIQADDEPTF SFFSGPYMVM TNLVWNGSRV TVKELNLPTH PHCSRLRLAD LLIAEQEHSS
KLRHPYLLQL MAVCLSQDLE KTRLVYERIT IGTLFSVLHE RRSQFPVLHM EVIVHLLLQI
SDALRYLHFQ GFIHRSLSSY AVHIISPGEA RLTNLEYMLE SEDRGVQRDL TRVPLPTQLY
NWAAPEVILQ KAATVKSDIY SFSMIMQEIL TDDIPWKGLD GSVVKKAVVS GNYLEADVRL
PKPYYDIVKS GIHVKQKDRT MNLQDIRYIL KNDLKDFTGA QRTQPTESPR VQRYGLHPDV
NVYLGLTSEH PRETPDMEII ELKEMGSQPH SPRVHSLFTE GTLDPQAPDP CLMARETQNQ
DAPCPAPFMA EEASSPSTGQ PSLCSFEINE IYSGCLILED DIEEPPGAAS SLEADGPNQV
DELKSMEEEL DKMEREACCF GSEDESSSKA ETEYSFDDWD WQNGSLSSLS LPESTREAKS
NLNNMSTTEE YLISKCVLDL KIMQTIMHEN DDRLRNIEQI LDEVEMKQKE QEERMSLWAT
SREFTNAYKL PLAVGPPSLN YIPPVLQLSG GQKPDTSGNY PTLPRFPRML PTLCDPGKQN
TDEQFQCTQG AKDSLETSRI QNTSSQGRPR ESTAQAKATQ FNSALFTLSS HRQGPSASPS
CHWDSTRMSV EPVSSEIYNA ESRNKDDGKV HLKWKMEVKE MAKKAATGQL TVPPWHPQSS
LTLESEAENE PDALLQPPIR SPENTDWQRV IEYHRENDEP RGNGKFDKTG NNDCDSDQHG
RQPRLGSFTS IRHPSPRQKE QPEHSEAFQA SSDTLVAVEK SYSHQSMQST CSPESSEDIT
DEFLTPDGEY FYSSTAQENL ALETSSPIEE DFEGIQGAFA QPQVSGEEKF QMRKILGKNA
EILPRSQFQP VRSTEDEQEE TSKESPKELK EKDISLTDIQ DLSSISYEPD SSFKEASCKT
PKINHAPTSV STPLSPGSVS SAASQYKDCL ESITFQVKTE FASCWNSQEF IQTLSDDFIS
VRERAKKLDS LLTSSETPPS RLTGLKRLSS FIGAGSPSLV KACDSSPPHA TQRRSLPKVE
AFSQHHIDEL PPPSQELLDD IELLKQQQGS STVLHENTAS DGGGTANDQR HLEEQETDSK
KEDSSMLLSK ETEDLGEDTE RAHSTLDEDL ERWLQPPEES VELQDLPKGS ERETNIKDQK
VGEEKRKRED SITPERRKSE GVLGTSEEDE LKSCFWKRLG WSESSRIIVL DQSDLSD
