CE104_HUMAN
ID CE104_HUMAN Reviewed; 925 AA.
AC O60308; A0A024R4G3; Q5JSQ3; Q5SR24; Q5SR25; Q6PKF5; Q86W32; Q86X14;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Centrosomal protein of 104 kDa;
DE Short=Cep104;
GN Name=CEP104; Synonyms=KIAA0562;
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 1).
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [2]
RP SEQUENCE REVISION TO N-TERMINUS.
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Kidney, Skin, and 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21399614; DOI=10.1038/emboj.2011.63;
RA Jakobsen L., Vanselow K., Skogs M., Toyoda Y., Lundberg E., Poser I.,
RA Falkenby L.G., Bennetzen M., Westendorf J., Nigg E.A., Uhlen M.,
RA Hyman A.A., Andersen J.S.;
RT "Novel asymmetrically localizing components of human centrosomes identified
RT by complementary proteomics methods.";
RL EMBO J. 30:1520-1535(2011).
RN [7]
RP INTERACTION WITH CCP110 AND CEP97.
RX PubMed=22885064; DOI=10.1016/j.cub.2012.07.047;
RA Jiang K., Toedt G., Montenegro Gouveia S., Davey N.E., Hua S.,
RA van der Vaart B., Grigoriev I., Larsen J., Pedersen L.B., Bezstarosti K.,
RA Lince-Faria M., Demmers J., Steinmetz M.O., Gibson T.J., Akhmanova A.;
RT "A proteome-wide screen for mammalian SxIP motif-containing microtubule
RT plus-end tracking proteins.";
RL Curr. Biol. 22:1800-1807(2012).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23970417; DOI=10.1242/jcs.133439;
RA Satish Tammana T.V., Tammana D., Diener D.R., Rosenbaum J.;
RT "Centrosomal protein CEP104 (Chlamydomonas FAP256) moves to the ciliary tip
RT during ciliary assembly.";
RL J. Cell Sci. 126:5018-5029(2013).
RN [9]
RP INVOLVEMENT IN JBTS25.
RX PubMed=26477546; DOI=10.1016/j.ajhg.2015.09.009;
RG Care4Rare Canada Consortium;
RA Srour M., Hamdan F.F., McKnight D., Davis E., Mandel H.,
RA Schwartzentruber J., Martin B., Patry L., Nassif C., Dionne-Laporte A.,
RA Ospina L.H., Lemyre E., Massicotte C., Laframboise R., Maranda B.,
RA Labuda D., Decarie J.C., Rypens F., Goldsher D., Fallet-Bianco C.,
RA Soucy J.F., Laberge A.M., Maftei C., Boycott K., Brais B., Boucher R.M.,
RA Rouleau G.A., Katsanis N., Majewski J., Elpeleg O., Kukolich M.K.,
RA Shalev S., Michaud J.L.;
RT "Joubert Syndrome in French Canadians and Identification of Mutations in
RT CEP104.";
RL Am. J. Hum. Genet. 97:744-753(2015).
RN [10]
RP INTERACTION WITH ARMC9; TOGARAM1; CCDC66 AND CSPP1.
RX PubMed=32453716; DOI=10.1172/jci131656;
RG University of Washington Center for Mendelian Genomics;
RG Genomics England Research Consortium;
RA Latour B.L., Van De Weghe J.C., Rusterholz T.D., Letteboer S.J., Gomez A.,
RA Shaheen R., Gesemann M., Karamzade A., Asadollahi M., Barroso-Gil M.,
RA Chitre M., Grout M.E., van Reeuwijk J., van Beersum S.E., Miller C.V.,
RA Dempsey J.C., Morsy H., Bamshad M.J., Nickerson D.A., Neuhauss S.C.,
RA Boldt K., Ueffing M., Keramatipour M., Sayer J.A., Alkuraya F.S.,
RA Bachmann-Gagescu R., Roepman R., Doherty D.;
RT "Dysfunction of the ciliary ARMC9/TOGARAM1 protein module causes Joubert
RT syndrome.";
RL J. Clin. Invest. 130:4423-4439(2020).
CC -!- FUNCTION: Required for ciliogenesis and for structural integrity at the
CC ciliary tip. {ECO:0000269|PubMed:23970417}.
CC -!- SUBUNIT: Interacts with CCP110 and CEP97. Interacts with ARMC9,
CC TOGARAM1, CCDC66 and CSPP1 (PubMed:32453716).
CC {ECO:0000269|PubMed:22885064, ECO:0000269|PubMed:32453716}.
CC -!- INTERACTION:
CC O60308; Q15637: SF1; NbExp=4; IntAct=EBI-2685240, EBI-744603;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:23970417}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:21399614,
CC ECO:0000269|PubMed:23970417}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:23970417}. Cytoplasm,
CC cytoskeleton, spindle pole. Note=In interphase non-ciliated cells,
CC localizes to the distal ends of both the mother and daughter
CC centrioles. In ciliated cells, present at the distal end of the
CC daughter centriole, but not on the mother centriole, and at the tip of
CC primary cilium. Localization at the ciliary tip is also observed in
CC motile cilia. Throughout S phase, associated with both mother and
CC daughter centrioles in each centrosome. During metaphase and telophase,
CC present at both spindle poles. {ECO:0000269|PubMed:23970417}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O60308-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60308-2; Sequence=VSP_014364, VSP_014365;
CC Name=3;
CC IsoId=O60308-3; Sequence=VSP_014366, VSP_014367;
CC -!- DISEASE: Joubert syndrome 25 (JBTS25) [MIM:616781]: A form of Joubert
CC syndrome, a disorder presenting with cerebellar ataxia, oculomotor
CC apraxia, hypotonia, neonatal breathing abnormalities and psychomotor
CC delay. Neuroradiologically, it is characterized by cerebellar vermian
CC hypoplasia/aplasia, thickened and reoriented superior cerebellar
CC peduncles, and an abnormally large interpeduncular fossa, giving the
CC appearance of a molar tooth on transaxial slices (molar tooth sign).
CC Additional variable features include retinal dystrophy, renal disease,
CC liver fibrosis, and polydactyly. JBTS25 clinical manifestations appear
CC to be confined to the neurologic system. JBTS25 inheritance is
CC autosomal recessive. {ECO:0000269|PubMed:26477546}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH01640.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAA25488.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB011134; BAA25488.2; ALT_INIT; mRNA.
DR EMBL; AL365330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL691523; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471130; EAW71483.1; -; Genomic_DNA.
DR EMBL; CH471130; EAW71484.1; -; Genomic_DNA.
DR EMBL; BC001640; AAH01640.1; ALT_SEQ; mRNA.
DR EMBL; BC047450; AAH47450.1; -; mRNA.
DR EMBL; BC050721; AAH50721.1; -; mRNA.
DR CCDS; CCDS30571.1; -. [O60308-1]
DR PIR; T00334; T00334.
DR RefSeq; NP_055519.1; NM_014704.3. [O60308-1]
DR PDB; 5LPH; X-ray; 2.25 A; A/B=392-676.
DR PDB; 5LPI; X-ray; 1.80 A; A/B/C/D=746-875.
DR PDBsum; 5LPH; -.
DR PDBsum; 5LPI; -.
DR AlphaFoldDB; O60308; -.
DR SMR; O60308; -.
DR BioGRID; 115080; 85.
DR IntAct; O60308; 79.
DR MINT; O60308; -.
DR STRING; 9606.ENSP00000367476; -.
DR GlyGen; O60308; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60308; -.
DR PhosphoSitePlus; O60308; -.
DR BioMuta; CEP104; -.
DR EPD; O60308; -.
DR jPOST; O60308; -.
DR MassIVE; O60308; -.
DR MaxQB; O60308; -.
DR PaxDb; O60308; -.
DR PeptideAtlas; O60308; -.
DR PRIDE; O60308; -.
DR ProteomicsDB; 49335; -. [O60308-1]
DR ProteomicsDB; 49336; -. [O60308-2]
DR ProteomicsDB; 49337; -. [O60308-3]
DR Antibodypedia; 26970; 102 antibodies from 16 providers.
DR DNASU; 9731; -.
DR Ensembl; ENST00000378223.3; ENSP00000367468.3; ENSG00000116198.14. [O60308-2]
DR Ensembl; ENST00000378230.8; ENSP00000367476.3; ENSG00000116198.14. [O60308-1]
DR Ensembl; ENST00000494653.5; ENSP00000501736.1; ENSG00000116198.14. [O60308-3]
DR Ensembl; ENST00000674558.1; ENSP00000501829.1; ENSG00000116198.14. [O60308-1]
DR Ensembl; ENST00000674623.1; ENSP00000501733.1; ENSG00000116198.14. [O60308-1]
DR GeneID; 9731; -.
DR KEGG; hsa:9731; -.
DR MANE-Select; ENST00000378230.8; ENSP00000367476.3; NM_014704.4; NP_055519.1.
DR UCSC; uc001aky.3; human. [O60308-1]
DR CTD; 9731; -.
DR DisGeNET; 9731; -.
DR GeneCards; CEP104; -.
DR GeneReviews; CEP104; -.
DR HGNC; HGNC:24866; CEP104.
DR HPA; ENSG00000116198; Low tissue specificity.
DR MalaCards; CEP104; -.
DR MIM; 616690; gene.
DR MIM; 616781; phenotype.
DR neXtProt; NX_O60308; -.
DR OpenTargets; ENSG00000116198; -.
DR Orphanet; 475; Joubert syndrome.
DR PharmGKB; PA144596418; -.
DR VEuPathDB; HostDB:ENSG00000116198; -.
DR eggNOG; KOG4825; Eukaryota.
DR GeneTree; ENSGT00390000013405; -.
DR HOGENOM; CLU_003200_0_0_1; -.
DR InParanoid; O60308; -.
DR OMA; VQGNDYN; -.
DR OrthoDB; 242784at2759; -.
DR PhylomeDB; O60308; -.
DR TreeFam; TF323766; -.
DR PathwayCommons; O60308; -.
DR SignaLink; O60308; -.
DR BioGRID-ORCS; 9731; 22 hits in 1077 CRISPR screens.
DR ChiTaRS; CEP104; human.
DR GenomeRNAi; 9731; -.
DR Pharos; O60308; Tbio.
DR PRO; PR:O60308; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O60308; protein.
DR Bgee; ENSG00000116198; Expressed in secondary oocyte and 198 other tissues.
DR ExpressionAtlas; O60308; baseline and differential.
DR Genevisible; O60308; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0016595; F:glutamate binding; IEA:Ensembl.
DR GO; GO:0016594; F:glycine binding; IEA:Ensembl.
DR GO; GO:0016596; F:thienylcyclohexylpiperidine binding; IEA:Ensembl.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR034085; TOG.
DR SMART; SM01349; TOG; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell projection; Ciliopathy;
KW Coiled coil; Cytoplasm; Cytoskeleton; Joubert syndrome; Reference proteome;
KW Repeat.
FT CHAIN 1..925
FT /note="Centrosomal protein of 104 kDa"
FT /id="PRO_0000050763"
FT REPEAT 529..567
FT /note="HEAT 1"
FT REPEAT 604..640
FT /note="HEAT 2"
FT REGION 883..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 209..289
FT /evidence="ECO:0000255"
FT COILED 677..725
FT /evidence="ECO:0000255"
FT COMPBIAS 911..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 189..244
FT /note="RKSDYISPLDDLAFDMYQDPEVAQIIRKLDERKREAVQKERYDYAKKLKQAI
FT ADLQ -> SSVRTGGESTFGELKGPAVPSSVTLSVLGTSLGQWFPCHLPAVDDNEGTPF
FT QRCLV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014364"
FT VAR_SEQ 245..925
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014365"
FT VAR_SEQ 554
FT /note="E -> V (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014366"
FT VAR_SEQ 555..925
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014367"
FT VARIANT 414
FT /note="L -> I (in dbSNP:rs2275824)"
FT /id="VAR_034036"
FT VARIANT 686
FT /note="A -> V (in dbSNP:rs2275831)"
FT /id="VAR_020042"
FT CONFLICT 51
FT /note="V -> L (in Ref. 5; AAH01640)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="Y -> F (in Ref. 5; AAH47450)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="P -> S (in Ref. 5; AAH47450)"
FT /evidence="ECO:0000305"
FT HELIX 422..427
FT /evidence="ECO:0007829|PDB:5LPH"
FT HELIX 429..435
FT /evidence="ECO:0007829|PDB:5LPH"
FT HELIX 437..444
FT /evidence="ECO:0007829|PDB:5LPH"
FT HELIX 448..464
FT /evidence="ECO:0007829|PDB:5LPH"
FT HELIX 471..488
FT /evidence="ECO:0007829|PDB:5LPH"
FT HELIX 494..509
FT /evidence="ECO:0007829|PDB:5LPH"
FT HELIX 511..514
FT /evidence="ECO:0007829|PDB:5LPH"
FT HELIX 519..535
FT /evidence="ECO:0007829|PDB:5LPH"
FT HELIX 536..538
FT /evidence="ECO:0007829|PDB:5LPH"
FT HELIX 542..557
FT /evidence="ECO:0007829|PDB:5LPH"
FT HELIX 559..562
FT /evidence="ECO:0007829|PDB:5LPH"
FT TURN 563..565
FT /evidence="ECO:0007829|PDB:5LPH"
FT HELIX 566..571
FT /evidence="ECO:0007829|PDB:5LPH"
FT HELIX 581..598
FT /evidence="ECO:0007829|PDB:5LPH"
FT STRAND 600..604
FT /evidence="ECO:0007829|PDB:5LPH"
FT HELIX 607..617
FT /evidence="ECO:0007829|PDB:5LPH"
FT HELIX 623..640
FT /evidence="ECO:0007829|PDB:5LPH"
FT HELIX 641..647
FT /evidence="ECO:0007829|PDB:5LPH"
FT HELIX 655..657
FT /evidence="ECO:0007829|PDB:5LPH"
FT HELIX 659..671
FT /evidence="ECO:0007829|PDB:5LPH"
FT TURN 747..750
FT /evidence="ECO:0007829|PDB:5LPI"
FT STRAND 751..753
FT /evidence="ECO:0007829|PDB:5LPI"
FT TURN 755..757
FT /evidence="ECO:0007829|PDB:5LPI"
FT HELIX 768..775
FT /evidence="ECO:0007829|PDB:5LPI"
FT STRAND 780..782
FT /evidence="ECO:0007829|PDB:5LPI"
FT TURN 784..786
FT /evidence="ECO:0007829|PDB:5LPI"
FT STRAND 789..791
FT /evidence="ECO:0007829|PDB:5LPI"
FT HELIX 792..794
FT /evidence="ECO:0007829|PDB:5LPI"
FT HELIX 795..801
FT /evidence="ECO:0007829|PDB:5LPI"
FT HELIX 806..808
FT /evidence="ECO:0007829|PDB:5LPI"
FT STRAND 809..811
FT /evidence="ECO:0007829|PDB:5LPI"
FT TURN 813..815
FT /evidence="ECO:0007829|PDB:5LPI"
FT STRAND 818..820
FT /evidence="ECO:0007829|PDB:5LPI"
FT HELIX 821..823
FT /evidence="ECO:0007829|PDB:5LPI"
FT HELIX 824..830
FT /evidence="ECO:0007829|PDB:5LPI"
FT TURN 839..841
FT /evidence="ECO:0007829|PDB:5LPI"
FT TURN 846..848
FT /evidence="ECO:0007829|PDB:5LPI"
FT HELIX 856..864
FT /evidence="ECO:0007829|PDB:5LPI"
SQ SEQUENCE 925 AA; 104448 MW; 6B2BBD5068136887 CRC64;
MPHKIGFVVV SSSGHEDGFS ARELMIHAPT VSGWRSPRFC QFPQEIVLQM VERCRIRKLQ
LLAHQYMISS KIEFYISESL PEYFAPYQAE RFRRLGYVSL CDNEKTGCKA RELKSVYVDA
VGQFLKLIFH QNHVNKYNIY NQVALVAINI IGDPADFSDE SNTASREKLI DHYLGHNSED
PALEGTYARK SDYISPLDDL AFDMYQDPEV AQIIRKLDER KREAVQKERY DYAKKLKQAI
ADLQKVGERL GRYEVEKRCA VEKEDYDLAK EKKQQMEQYR AEVYEQLELH SLLDAELMRR
PFDLPLQPLA RSGSPCHQKP MPSLPQLEER GTENQFAEPF LQEKPSSYSL TISPQHSAVD
PLLPATDPHP KINAESLPYD ERPLPAIRKH YGEAVVEPEM SNADISDARR GGMLGEPEPL
TEKALREASS AIDVLGETLV AEAYCKTWSY REDALLALSK KLMEMPVGTP KEDLKNTLRA
SVFLVRRAIK DIVTSVFQAS LKLLKMIITQ YIPKHKLSKL ETAHCVERTI PVLLTRTGDS
SARLRVTAAN FIQEMALFKE VKSLQIIPSY LVQPLKANSS VHLAMSQMGL LARLLKDLGT
GSSGFTIDNV MKFSVSALEH RVYEVRETAV RIILDMYRQH QASILEYLPP DDSNTRRNIL
YKTIFEGFAK IDGRATDAEM RARRKAATEE AEKQKKEEIK ALQGQLAALK EIQAEVQEKE
SDAVKPKNQD IQGGKAAPAE ALGIPDEHYL DNLCIFCGER SESFTEEGLD LHYWKHCLML
TRCDHCKQVV EISSLTEHLL TECDKKDGFG KCYRCSEAVF KEELPRHIKH KDCNPAKPEK
LANRCPLCHE NFSPGEEAWK AHLMGPAGCT MNLRKTHILQ KAPALQPGKS SAVAASGPLG
SKAGSKIPTP KGGLSKSSSR TYAKR
