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GCP6_HUMAN
ID   GCP6_HUMAN              Reviewed;        1819 AA.
AC   Q96RT7; Q5JZ80; Q6PJ40; Q86YE9; Q9BY91; Q9UGX3; Q9UGX4;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 3.
DT   03-AUG-2022, entry version 176.
DE   RecName: Full=Gamma-tubulin complex component 6;
DE            Short=GCP-6;
GN   Name=TUBGCP6; Synonyms=GCP6, KIAA1669;
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 1), FUNCTION, SUBUNIT, SUBCELLULAR
RP   LOCATION, AND VARIANTS SER-567 AND ALA-1377.
RX   PubMed=11694571; DOI=10.1091/mbc.12.11.3340;
RA   Murphy S.M., Preble A.M., Patel U.K., O'Connell K.L., Dias D.P., Moritz M.,
RA   Agard D., Stults J.T., Stearns T.;
RT   "GCP5 and GCP6: two new members of the human gamma-tubulin complex.";
RL   Mol. Biol. Cell 12:3340-3352(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-1819 (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=11258795; DOI=10.1093/dnares/8.1.1;
RA   Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.;
RT   "Identification of novel transcribed sequences on human chromosome 22 by
RT   expressed sequence tag mapping.";
RL   DNA Res. 8:1-9(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 811-1819 (ISOFORM 1), NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1315-1819 (ISOFORM 3), AND VARIANT LEU-1621.
RC   TISSUE=Brain, and Kidney;
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT   "Proteomic characterization of the human centrosome by protein correlation
RT   profiling.";
RL   Nature 426:570-574(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [7]
RP   INVOLVEMENT IN MCCRP1.
RX   PubMed=22279524; DOI=10.1371/journal.pone.0028936;
RA   Puffenberger E.G., Jinks R.N., Sougnez C., Cibulskis K., Willert R.A.,
RA   Achilly N.P., Cassidy R.P., Fiorentini C.J., Heiken K.F., Lawrence J.J.,
RA   Mahoney M.H., Miller C.J., Nair D.T., Politi K.A., Worcester K.N.,
RA   Setton R.A., Dipiazza R., Sherman E.A., Eastman J.T., Francklyn C.,
RA   Robey-Bond S., Rider N.L., Gabriel S., Morton D.H., Strauss K.A.;
RT   "Genetic mapping and exome sequencing identify variants associated with
RT   five novel diseases.";
RL   PLoS ONE 7:E28936-E28936(2012).
CC   -!- FUNCTION: Gamma-tubulin complex is necessary for microtubule nucleation
CC       at the centrosome. {ECO:0000269|PubMed:11694571}.
CC   -!- SUBUNIT: Gamma-tubulin complex is composed of gamma-tubulin, TUBGCP2,
CC       TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6. {ECO:0000269|PubMed:11694571}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC       center, centrosome {ECO:0000269|PubMed:11694571,
CC       ECO:0000269|PubMed:14654843}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q96RT7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96RT7-2; Sequence=VSP_001624;
CC       Name=3;
CC         IsoId=Q96RT7-3; Sequence=VSP_017208, VSP_017209;
CC   -!- DISEASE: Microcephaly and chorioretinopathy, autosomal recessive, 1
CC       (MCCRP1) [MIM:251270]: A syndrome characterized by microcephaly,
CC       cognitive impairment, underdeveloped retina and choroid, and epilepsy
CC       in some patients. The more anterior parts of the retina, near the
CC       periphery and pars plana, have a grayish hue and diminutive vasculature
CC       similar to retinopathy of prematurity. Visual impairment becomes
CC       evident during the first year of life. {ECO:0000269|PubMed:22279524}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- SIMILARITY: Belongs to the TUBGCP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH42165.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAB33339.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; AF272887; AAK82968.1; -; mRNA.
DR   EMBL; AL022328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB051456; BAB33339.1; ALT_SEQ; mRNA.
DR   EMBL; BC023573; AAH23573.1; -; mRNA.
DR   EMBL; BC042165; AAH42165.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS14087.1; -. [Q96RT7-1]
DR   RefSeq; NP_065194.2; NM_020461.3. [Q96RT7-1]
DR   PDB; 6M33; X-ray; 3.29 A; A=1-119.
DR   PDB; 6V6C; EM; 4.50 A; L=1-1819.
DR   PDB; 6V6S; EM; 4.30 A; L=1-1819.
DR   PDB; 6X0U; EM; 3.60 A; D=1-1819.
DR   PDB; 7AS4; EM; 4.13 A; 4/L=1-1819.
DR   PDB; 7QJ0; EM; 5.32 A; L=1-1819.
DR   PDB; 7QJ1; EM; 7.00 A; L=1-1819.
DR   PDB; 7QJ2; EM; 8.60 A; L=1-1819.
DR   PDB; 7QJ3; EM; 7.60 A; L=1-1819.
DR   PDB; 7QJ4; EM; 9.00 A; L=1-1819.
DR   PDB; 7QJ5; EM; 8.70 A; L/c=1-1819.
DR   PDB; 7QJ6; EM; 7.80 A; L/c=1-1819.
DR   PDB; 7QJ7; EM; 8.70 A; L/c=1-1819.
DR   PDB; 7QJ8; EM; 8.70 A; L/c=1-1819.
DR   PDB; 7QJ9; EM; 8.10 A; L/c=1-1819.
DR   PDB; 7QJA; EM; 9.20 A; L/c=1-1819.
DR   PDB; 7QJB; EM; 9.20 A; L/c=1-1819.
DR   PDB; 7QJC; EM; 16.10 A; L/c=1-1819.
DR   PDB; 7QJD; EM; 7.10 A; L/c=1-1819.
DR   PDB; 7QJE; EM; 7.80 A; L=1-1819.
DR   PDBsum; 6M33; -.
DR   PDBsum; 6V6C; -.
DR   PDBsum; 6V6S; -.
DR   PDBsum; 6X0U; -.
DR   PDBsum; 7AS4; -.
DR   PDBsum; 7QJ0; -.
DR   PDBsum; 7QJ1; -.
DR   PDBsum; 7QJ2; -.
DR   PDBsum; 7QJ3; -.
DR   PDBsum; 7QJ4; -.
DR   PDBsum; 7QJ5; -.
DR   PDBsum; 7QJ6; -.
DR   PDBsum; 7QJ7; -.
DR   PDBsum; 7QJ8; -.
DR   PDBsum; 7QJ9; -.
DR   PDBsum; 7QJA; -.
DR   PDBsum; 7QJB; -.
DR   PDBsum; 7QJC; -.
DR   PDBsum; 7QJD; -.
DR   PDBsum; 7QJE; -.
DR   AlphaFoldDB; Q96RT7; -.
DR   SMR; Q96RT7; -.
DR   BioGRID; 124505; 75.
DR   CORUM; Q96RT7; -.
DR   IntAct; Q96RT7; 34.
DR   MINT; Q96RT7; -.
DR   STRING; 9606.ENSP00000248846; -.
DR   GlyGen; Q96RT7; 1 site.
DR   iPTMnet; Q96RT7; -.
DR   PhosphoSitePlus; Q96RT7; -.
DR   BioMuta; TUBGCP6; -.
DR   DMDM; 143811395; -.
DR   EPD; Q96RT7; -.
DR   jPOST; Q96RT7; -.
DR   MassIVE; Q96RT7; -.
DR   MaxQB; Q96RT7; -.
DR   PaxDb; Q96RT7; -.
DR   PeptideAtlas; Q96RT7; -.
DR   PRIDE; Q96RT7; -.
DR   ProteomicsDB; 78029; -. [Q96RT7-1]
DR   ProteomicsDB; 78030; -. [Q96RT7-2]
DR   ProteomicsDB; 78031; -. [Q96RT7-3]
DR   Antibodypedia; 52528; 123 antibodies from 24 providers.
DR   Ensembl; ENST00000248846.10; ENSP00000248846.5; ENSG00000128159.12. [Q96RT7-1]
DR   GeneID; 85378; -.
DR   KEGG; hsa:85378; -.
DR   MANE-Select; ENST00000248846.10; ENSP00000248846.5; NM_020461.4; NP_065194.3.
DR   UCSC; uc003bkb.2; human. [Q96RT7-1]
DR   CTD; 85378; -.
DR   DisGeNET; 85378; -.
DR   GeneCards; TUBGCP6; -.
DR   HGNC; HGNC:18127; TUBGCP6.
DR   HPA; ENSG00000128159; Low tissue specificity.
DR   MalaCards; TUBGCP6; -.
DR   MIM; 251270; phenotype.
DR   MIM; 610053; gene.
DR   neXtProt; NX_Q96RT7; -.
DR   OpenTargets; ENSG00000128159; -.
DR   Orphanet; 2518; Autosomal recessive chorioretinopathy-microcephaly syndrome.
DR   PharmGKB; PA38507; -.
DR   VEuPathDB; HostDB:ENSG00000128159; -.
DR   eggNOG; KOG2000; Eukaryota.
DR   GeneTree; ENSGT00940000157810; -.
DR   HOGENOM; CLU_002518_0_0_1; -.
DR   InParanoid; Q96RT7; -.
DR   OMA; HIRVGEN; -.
DR   OrthoDB; 110079at2759; -.
DR   PhylomeDB; Q96RT7; -.
DR   TreeFam; TF106321; -.
DR   PathwayCommons; Q96RT7; -.
DR   Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR   Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR   SignaLink; Q96RT7; -.
DR   SIGNOR; Q96RT7; -.
DR   BioGRID-ORCS; 85378; 683 hits in 1079 CRISPR screens.
DR   ChiTaRS; TUBGCP6; human.
DR   GeneWiki; TUBGCP6; -.
DR   GenomeRNAi; 85378; -.
DR   Pharos; Q96RT7; Tbio.
DR   PRO; PR:Q96RT7; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; Q96RT7; protein.
DR   Bgee; ENSG00000128159; Expressed in right hemisphere of cerebellum and 111 other tissues.
DR   ExpressionAtlas; Q96RT7; baseline and differential.
DR   Genevisible; Q96RT7; HS.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0000923; C:equatorial microtubule organizing center; IBA:GO_Central.
DR   GO; GO:0000930; C:gamma-tubulin complex; IBA:GO_Central.
DR   GO; GO:0000931; C:gamma-tubulin large complex; IDA:UniProtKB.
DR   GO; GO:0008275; C:gamma-tubulin small complex; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0000922; C:spindle pole; IEA:InterPro.
DR   GO; GO:0043015; F:gamma-tubulin binding; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR   GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR   GO; GO:0007020; P:microtubule nucleation; IDA:UniProtKB.
DR   GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0051225; P:spindle assembly; IBA:GO_Central.
DR   Gene3D; 1.20.120.1900; -; 1.
DR   InterPro; IPR007259; GCP.
DR   InterPro; IPR045818; GCP6_N.
DR   InterPro; IPR040457; GCP_C.
DR   InterPro; IPR042241; GCP_C_sf.
DR   InterPro; IPR041470; GCP_N.
DR   PANTHER; PTHR19302; PTHR19302; 1.
DR   Pfam; PF19340; GCP6_N; 1.
DR   Pfam; PF04130; GCP_C_terminal; 1.
DR   Pfam; PF17681; GCP_N_terminal; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cytoplasm; Cytoskeleton; Microtubule;
KW   Reference proteome; Repeat.
FT   CHAIN           1..1819
FT                   /note="Gamma-tubulin complex component 6"
FT                   /id="PRO_0000078131"
FT   REPEAT          1027..1053
FT                   /note="1"
FT   REPEAT          1054..1080
FT                   /note="2"
FT   REPEAT          1081..1107
FT                   /note="3"
FT   REPEAT          1108..1134
FT                   /note="4"
FT   REPEAT          1135..1161
FT                   /note="5"
FT   REPEAT          1162..1188
FT                   /note="6"
FT   REPEAT          1189..1215
FT                   /note="7"
FT   REPEAT          1216..1242
FT                   /note="8"
FT   REPEAT          1243..1269
FT                   /note="9"
FT   REGION          810..889
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          929..951
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1000..1023
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1027..1269
FT                   /note="9 X 27 AA tandem repeats"
FT   REGION          1271..1412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1296..1311
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1327..1361
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1380..1396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1652..1662
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_017208"
FT   VAR_SEQ         1724..1757
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:11258795"
FT                   /id="VSP_001624"
FT   VAR_SEQ         1724..1729
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_017209"
FT   VARIANT         104
FT                   /note="L -> P (in dbSNP:rs8137873)"
FT                   /id="VAR_055852"
FT   VARIANT         567
FT                   /note="L -> S (in dbSNP:rs4838865)"
FT                   /evidence="ECO:0000269|PubMed:11694571"
FT                   /id="VAR_031594"
FT   VARIANT         624
FT                   /note="I -> M (in dbSNP:rs35573482)"
FT                   /id="VAR_055853"
FT   VARIANT         884
FT                   /note="A -> V (in dbSNP:rs34455105)"
FT                   /id="VAR_055854"
FT   VARIANT         1232
FT                   /note="V -> M (in dbSNP:rs17248287)"
FT                   /id="VAR_055855"
FT   VARIANT         1364
FT                   /note="S -> C (in dbSNP:rs5771107)"
FT                   /id="VAR_055856"
FT   VARIANT         1377
FT                   /note="T -> A (in dbSNP:rs11703226)"
FT                   /evidence="ECO:0000269|PubMed:11694571"
FT                   /id="VAR_055857"
FT   VARIANT         1621
FT                   /note="V -> L (in dbSNP:rs4838864)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_055858"
FT   HELIX           4..14
FT                   /evidence="ECO:0007829|PDB:6M33"
FT   HELIX           29..48
FT                   /evidence="ECO:0007829|PDB:6M33"
FT   HELIX           67..79
FT                   /evidence="ECO:0007829|PDB:6M33"
FT   HELIX           83..97
FT                   /evidence="ECO:0007829|PDB:6M33"
FT   HELIX           108..116
FT                   /evidence="ECO:0007829|PDB:6M33"
SQ   SEQUENCE   1819 AA;  200498 MW;  265F89F318996157 CRC64;
     MASITQLFDD LCEALLPAAK THLGQRSVNR KRAKRSLKKV AYNALFTNLF QDETQQLQPD
     MSKLPARNKI LMLSFDLRVG GLGPKADRLE ELVEELEAAP CCPLLEVGSV LDLLVQLAGS
     GPPQVLPRKR DYFLNNKHVG RNVPYSGYDC DDLSVFEMDV QSLISREECL CHSMIQETLQ
     VMEAAPGTGL PTVGLFSFGD PCGDRFERDT RVSLFGALVH SRTYDMDVRL GLPPVPDNAD
     LSGLAIKVPP SVDQWEDEGF QSASNLTPDS QSEPSVTPDV DLWEAALTYE ASKRRCWERV
     GCPPGHREEP YLTEAGRDAF DKFCRLHQGE LQLLAGGVLQ APQPVLVKEC ELVKDVLNVL
     IGVVSATFSL CQPAQAFVVK RGVHVSGASP ESISSLLSEV AEYGTCYTRL SHFSLQPVLD
     SLYSKGLVFQ AFTSGLRRYL QYYRACVLST PPTLSLLTIG FLFKKLGRQL RYLAELCGVG
     AVLPGTCGGG PRAAFPTGVK LLSYLYQEAL HNCSNEHYPV LLSLLKTSCE PYTRFIHDWV
     YSGVFRDAYG EFMIQVNHEY LSFRDKLYWT HGYVLISKEV EDCVPVFLKH IAHDIYVCGK
     TINLLKLCCP RHYLCWSDVP VPRISVIFSL EELKEIEKDC AVYVGRMERV ARHSSVSKEE
     KELRMEIAKQ ELIAHAREAA SRVLSALSDR QMSERMALDA RKREQFQRLK EQFVKDQERR
     QAARQEELDD DFSYARELRD RERRLKSLEE ELERKARQAL VDHYSKLSAE AARREQKALW
     RIQRHRLESA RLRFLLEDEK HIQEMLKAVS EAHQPQEPPD VLLSVHPQVT SPGPEHPEGG
     QGCDSGSAEQ HSPAWDGWNR PGLLTPQPLK PLAVGAGGRG LQQAEGARPF SDSLSIGDFL
     PVGPGAEPSV QTGMVPLLEV ALQTINLDLP PSAPGEAPAA ASTQPSRPQE YDFSTVLRPA
     VATSPAPGPL QAAECSLGSS GLQLWEDSCG KMDACGSASR ETLLPSHPPR RAALEEGSSQ
     PTERLFGQVS GGGLPTGDYA SEIAPTRPRW NTHGHVSDAS IRVGENVSDV APTQPRWNTH
     GHVSNASISL GESVSDVAPT RPRWNIHGHV SNASIRVGEN VSDVAPTRPR WNTHGHVSNA
     SIRVGENVSD VAPTRPRWNT HGHVSDASIS LGESVSDMAP ARPRWNTHGH VSDASISLGE
     SVSDMAPTRP RWNTHGHVSD TSIRVGENVS DVAPIRSRCN THGHVSDASI SLGEPVSDVV
     STRPRWNTHV PIPPPHMVLG ALSPEAEPNT PRPQQSPPGH TSQSALSLGA QSTVLDCGPR
     LPVEVGPSLS SPSSGCGEGS ISVGENVSDV APTQPWWPNT PGDSVSEELG PGRSGDTEDL
     SPNWPLNSQE DTAAQSSPGR GEEAEASAAE AQGGEQAYLA GLAGQYHLER YPDSYESMSE
     PPIAHLLRPV LPRAFAFPVD PQVQSAADET AVQLSELLTL PVLMKRSITA PLAAHISLVN
     KAAVDYFFVE LHLEAHYEAL RHFLLMEDGE FAQSLSDLLF EKLGAGQTPG ELLNPLVLNS
     VLSKALQCSL HGDTPHASNL SLALKYLPEV FAPNAPDVLS CLELRYKVDW PLNIVITEGC
     VSKYSGVFSF LLQLKLMMWA LKDVCFHLKR TALLSHMAGS VQFRQLQLFK HEMQHFVKVI
     QGYIANQILH VTWCEFRARL ATVGDLEEIQ RAHAEYLHKA VFRGLLTEKA APVMNVIHSI
     FSLVLKFRSQ LISQAWGPPG GPRGAEHPNF ALMQQSYNTF KYYSHFLFKV VTKLVNRGYQ
     PHLEDFLLRI NFNNYYQDA
 
 
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