CNTRB_HUMAN
ID CNTRB_HUMAN Reviewed; 903 AA.
AC Q8N137; A6NHQ1; Q331K3; Q69YV7; Q8NCB8; Q8WXV3; Q96CQ7; Q9C060;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Centrobin;
DE AltName: Full=Centrosomal BRCA2-interacting protein;
DE AltName: Full=LYST-interacting protein 8;
GN Name=CNTROB; Synonyms=LIP8; ORFNames=PP1221;
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] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16275750; DOI=10.1083/jcb.200506185;
RA Zou C., Li J., Bai Y., Gunning W.T., Wazer D.E., Band V., Gao Q.;
RT "Centrobin: a novel daughter centriole-associated protein that is required
RT for centriole duplication.";
RL J. Cell Biol. 171:437-445(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 147-903 (ISOFORM 4).
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 100-903 (ISOFORM 3).
RC TISSUE=Brain, and Skin;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 369-903 (ISOFORM 5), AND VARIANT
RP GLN-578.
RC TISSUE=Teratocarcinoma;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 524-646, INTERACTION WITH LYST, AND VARIANT
RP GLN-578.
RX PubMed=11984006; DOI=10.1007/bf03402003;
RA Tchernev V.T., Mansfield T.A., Giot L., Kumar A.M., Nandabalan K., Li Y.,
RA Mishra V.S., Detter J.C., Rothberg J.M., Wallace M.R., Southwick F.S.,
RA Kingsmore S.F.;
RT "The Chediak-Higashi protein interacts with SNARE complex and signal
RT transduction proteins.";
RL Mol. Med. 8:56-64(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND SER-790, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Required for centriole duplication. Inhibition of centriole
CC duplication leading to defects in cytokinesis.
CC {ECO:0000269|PubMed:16275750}.
CC -!- SUBUNIT: Interacts with LYST. {ECO:0000269|PubMed:11984006}.
CC -!- INTERACTION:
CC Q8N137; Q13057-2: COASY; NbExp=3; IntAct=EBI-947360, EBI-10227704;
CC Q8N137; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-947360, EBI-5453285;
CC Q8N137; Q68J44: DUSP29; NbExp=3; IntAct=EBI-947360, EBI-1054321;
CC Q8N137; Q14241: ELOA; NbExp=3; IntAct=EBI-947360, EBI-742350;
CC Q8N137; Q7L775: EPM2AIP1; NbExp=3; IntAct=EBI-947360, EBI-6255981;
CC Q8N137; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-947360, EBI-348259;
CC Q8N137; Q96FA3: PELI1; NbExp=3; IntAct=EBI-947360, EBI-448369;
CC Q8N137; Q96T60: PNKP; NbExp=3; IntAct=EBI-947360, EBI-1045072;
CC Q8N137; P54725: RAD23A; NbExp=3; IntAct=EBI-947360, EBI-746453;
CC Q8N137; Q9UHP6: RSPH14; NbExp=3; IntAct=EBI-947360, EBI-748350;
CC Q8N137; Q5T7P8-2: SYT6; NbExp=3; IntAct=EBI-947360, EBI-10246152;
CC Q8N137; Q15560: TCEA2; NbExp=3; IntAct=EBI-947360, EBI-710310;
CC Q8N137; Q9NRE2: TSHZ2; NbExp=3; IntAct=EBI-947360, EBI-10687282;
CC Q8N137; Q5W5X9: TTC23; NbExp=3; IntAct=EBI-947360, EBI-6447954;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome, centriole {ECO:0000269|PubMed:16275750}.
CC Note=Centriole-associated, asymmetrically localizes to the daughter
CC centriole.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q8N137-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=Q8N137-2; Sequence=VSP_016838;
CC Name=3;
CC IsoId=Q8N137-3; Sequence=VSP_016839;
CC Name=4;
CC IsoId=Q8N137-4; Sequence=VSP_016836, VSP_016837;
CC Name=5;
CC IsoId=Q8N137-5; Sequence=VSP_016840, VSP_016841;
CC -!- TISSUE SPECIFICITY: Widely expressed (at protein level). Highly
CC expressed in testis. Also expressed in spleen, thymus, prostate, small
CC intestine, colon and peripheral blood leukocytes.
CC {ECO:0000269|PubMed:16275750}.
CC -!- DEVELOPMENTAL STAGE: Preferentially incorporated into the newly
CC assembled daughter centriole during centriole assembly at the late G1
CC or early S phase. Remains in the daughter centrioles throughout the
CC cell cycle. At the next cycle of centriole duplication, its amount on
CC the original daughter centriole eventually decreases.
CC {ECO:0000269|PubMed:16275750}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG49447.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=AAG49447.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC11241.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY160226; AAO22135.1; -; mRNA.
DR EMBL; AY160227; AAO22136.1; -; mRNA.
DR EMBL; AF331638; AAL56068.2; -; mRNA.
DR EMBL; AL137669; CAH10698.1; -; mRNA.
DR EMBL; AL833907; CAD38763.1; -; mRNA.
DR EMBL; AC104581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014055; AAH14055.3; -; mRNA.
DR EMBL; BC021134; AAH21134.1; -; mRNA.
DR EMBL; AK074847; BAC11241.1; ALT_INIT; mRNA.
DR EMBL; AF141344; AAG49447.1; ALT_SEQ; mRNA.
DR CCDS; CCDS11126.1; -. [Q8N137-1]
DR CCDS; CCDS32557.1; -. [Q8N137-2]
DR CCDS; CCDS82063.1; -. [Q8N137-3]
DR RefSeq; NP_001032221.1; NM_001037144.5. [Q8N137-2]
DR RefSeq; NP_001317053.1; NM_001330124.1. [Q8N137-3]
DR RefSeq; NP_444279.2; NM_053051.3. [Q8N137-1]
DR RefSeq; XP_016879617.1; XM_017024128.1. [Q8N137-2]
DR RefSeq; XP_016879618.1; XM_017024129.1. [Q8N137-2]
DR RefSeq; XP_016879619.1; XM_017024130.1.
DR RefSeq; XP_016879620.1; XM_017024131.1.
DR RefSeq; XP_016879621.1; XM_017024132.1.
DR RefSeq; XP_016879622.1; XM_017024133.1.
DR AlphaFoldDB; Q8N137; -.
DR SMR; Q8N137; -.
DR BioGRID; 125533; 165.
DR IntAct; Q8N137; 139.
DR MINT; Q8N137; -.
DR STRING; 9606.ENSP00000369614; -.
DR iPTMnet; Q8N137; -.
DR PhosphoSitePlus; Q8N137; -.
DR BioMuta; CNTROB; -.
DR DMDM; 74728485; -.
DR EPD; Q8N137; -.
DR jPOST; Q8N137; -.
DR MassIVE; Q8N137; -.
DR MaxQB; Q8N137; -.
DR PaxDb; Q8N137; -.
DR PeptideAtlas; Q8N137; -.
DR PRIDE; Q8N137; -.
DR ProteomicsDB; 71538; -. [Q8N137-1]
DR ProteomicsDB; 71539; -. [Q8N137-2]
DR ProteomicsDB; 71540; -. [Q8N137-3]
DR ProteomicsDB; 71541; -. [Q8N137-4]
DR ProteomicsDB; 71542; -. [Q8N137-5]
DR Antibodypedia; 12323; 212 antibodies from 28 providers.
DR DNASU; 116840; -.
DR Ensembl; ENST00000380262.7; ENSP00000369614.3; ENSG00000170037.14. [Q8N137-2]
DR Ensembl; ENST00000563694.6; ENSP00000456335.1; ENSG00000170037.14. [Q8N137-1]
DR Ensembl; ENST00000565740.5; ENSP00000454840.1; ENSG00000170037.14. [Q8N137-3]
DR GeneID; 116840; -.
DR KEGG; hsa:116840; -.
DR MANE-Select; ENST00000563694.6; ENSP00000456335.1; NM_053051.5; NP_444279.2.
DR UCSC; uc060axe.1; human. [Q8N137-1]
DR CTD; 116840; -.
DR DisGeNET; 116840; -.
DR GeneCards; CNTROB; -.
DR HGNC; HGNC:29616; CNTROB.
DR HPA; ENSG00000170037; Low tissue specificity.
DR MIM; 611425; gene.
DR neXtProt; NX_Q8N137; -.
DR OpenTargets; ENSG00000170037; -.
DR PharmGKB; PA143485436; -.
DR VEuPathDB; HostDB:ENSG00000170037; -.
DR eggNOG; ENOG502QRRG; Eukaryota.
DR GeneTree; ENSGT00610000086191; -.
DR HOGENOM; CLU_344733_0_0_1; -.
DR InParanoid; Q8N137; -.
DR OMA; HSGYQPG; -.
DR OrthoDB; 247531at2759; -.
DR PhylomeDB; Q8N137; -.
DR TreeFam; TF337444; -.
DR PathwayCommons; Q8N137; -.
DR SignaLink; Q8N137; -.
DR BioGRID-ORCS; 116840; 26 hits in 1079 CRISPR screens.
DR ChiTaRS; CNTROB; human.
DR GeneWiki; CNTROB; -.
DR GenomeRNAi; 116840; -.
DR Pharos; Q8N137; Tbio.
DR PRO; PR:Q8N137; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8N137; protein.
DR Bgee; ENSG00000170037; Expressed in left testis and 164 other tissues.
DR ExpressionAtlas; Q8N137; baseline and differential.
DR Genevisible; Q8N137; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0007099; P:centriole replication; IMP:HGNC-UCL.
DR GO; GO:0051299; P:centrosome separation; IMP:HGNC-UCL.
DR GO; GO:1902410; P:mitotic cytokinetic process; IMP:BHF-UCL.
DR GO; GO:1902017; P:regulation of cilium assembly; IEA:InterPro.
DR InterPro; IPR038923; Centrobin.
DR PANTHER; PTHR34439; PTHR34439; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..903
FT /note="Centrobin"
FT /id="PRO_0000076240"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..903
FT /note="Required for centrosome localization"
FT REGION 471..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 669..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 196..560
FT /evidence="ECO:0000255"
FT COMPBIAS 474..488
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..588
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..693
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 790
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 526..554
FT /note="AREQARVCELQSGNQQLEEQRVELVERLQ -> LLLDPPAPGLRSPRRRRGG
FT SGLCLPWPWP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_016836"
FT VAR_SEQ 555..903
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_016837"
FT VAR_SEQ 838
FT /note="G -> GYKPGRKEEGFSGWKLDYGEWSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16275750"
FT /id="VSP_016838"
FT VAR_SEQ 838
FT /note="G -> GR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016839"
FT VAR_SEQ 839..864
FT /note="TDGRGDNVPRRNTDSRLGEIPRKEIP -> YKPGRKEEGFSGWKLDYGEWSG
FT CVLH (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016840"
FT VAR_SEQ 865..903
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016841"
FT VARIANT 439
FT /note="R -> Q (in dbSNP:rs35421969)"
FT /id="VAR_050877"
FT VARIANT 578
FT /note="P -> Q (in dbSNP:rs11650083)"
FT /evidence="ECO:0000269|PubMed:11984006,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_024787"
FT CONFLICT 582
FT /note="A -> D (in Ref. 7; AAG49447)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 903 AA; 101253 MW; 3F8E6DE4CEF51851 CRC64;
MATSADSPSS PLGAEDLLSD SSEPPGLNQV SSEVTSQLYA SLRLSRQAEA TARAQLYLPS
TSPPHEGLDG FAQELSRSLS VGLEKNLKKK DGSKHIFEME SVRGQLQTML QTSRDTAYRD
PLIPGAGSER REEDSFDSDS TATLLNTRPL QDLSPSSSAQ ALEELFPRYT SLRPGPPLNP
PDFQGLRDAL DSEHTRRKHC ERHIQSLQTR VLELQQQLAV AVAADRKKDT MIEQLDKTLA
RVVEGWNRHE AERTEVLRGL QEEHQAAELT RSKQQETVTR LEQSLSEAME ALNREQESAR
LQQRERETLE EERQALTLRL EAEQQRCCVL QEERDAARAG QLSEHRELET LRAALEEERQ
TWAQQEHQLK EHYQALQEES QAQLEREKEK SQREAQAAWE TQHQLALVQS EVRRLEGELD
TARRERDALQ LEMSLVQARY ESQRIQLESE LAVQLEQRVT ERLAQAQESS LRQAASLREH
HRKQLQDLSG QHQQELASQL AQFKVEMAER EERQQQVAED YELRLAREQA RVCELQSGNQ
QLEEQRVELV ERLQAMLQAH WDEANQLLST TLPPPNPPAP PAGPSSPGPQ EPEKEERRVW
TMPPMAVALK PVLQQSREAR DELPGAPPVL CSSSSDLSLL LGPSFQSQHS FQPLEPKPDL
TSSTAGAFSA LGAFHPDHRA ERPFPEEDPG PDGEGLLKQG LPPAQLEGLK NFLHQLLETV
PQNNENPSVD LLPPKSGPLT VPSWEEAPQV PRIPPPVHKT KVPLAMASSL FRVPEPPSSH
SQGSGPSSGS PERGGDGLTF PRQLMEVSQL LRLYQARGWG ALPAEDLLLY LKRLEHSGTD
GRGDNVPRRN TDSRLGEIPR KEIPSQAVPR RLATAPKTEK PPARKKSGHP APSSMRSRGG
VWR