ODFP2_RAT
ID ODFP2_RAT Reviewed; 825 AA.
AC Q6AYX5; O70408; P97575; Q62693; Q9JIZ3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Outer dense fiber protein 2;
DE AltName: Full=84 kDa outer dense fiber protein;
DE AltName: Full=Cenexin;
DE AltName: Full=Outer dense fiber of sperm tails protein 2;
GN Name=Odf2; Synonyms=Odf84; ORFNames=KKT4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), TISSUE SPECIFICITY, AND ALTERNATIVE
RP SPLICING.
RC TISSUE=Testis;
RX PubMed=9369191; DOI=10.1095/biolreprod57.5.1223;
RA Turner K.J., Sharpe R.M., Gaughan J., Millar M.R., Foster P.M.,
RA Saunders P.T.;
RT "Expression cloning of a rat testicular transcript abundant in germ cells,
RT which contains two leucine zipper motifs.";
RL Biol. Reprod. 57:1223-1232(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY, AND ALTERNATIVE
RP SPLICING.
RC STRAIN=Sprague-Dawley; TISSUE=Spermatid;
RX PubMed=9092585; DOI=10.1074/jbc.272.15.10327;
RA Brohmann H., Pinnecke S., Hoyer-Fender S.;
RT "Identification and characterization of new cDNAs encoding outer dense
RT fiber proteins of rat sperm.";
RL J. Biol. Chem. 272:10327-10332(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=9698445; DOI=10.1006/dbio.1998.8931;
RA Schalles U., Shao X., van der Hoorn F.A., Oko R.;
RT "Developmental expression of the 84-kDa ODF sperm protein: localization to
RT both the cortex and medulla of outer dense fibers and to the connecting
RT piece.";
RL Dev. Biol. 199:250-260(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA March P., Sibley K.D., Scott V., Lange B.M.H., Taylor S.S., Gull K.;
RT "Cenexin - a molecular scaffolding protein with dual functions in the
RT mammalian centrosome and sperm tail.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [7]
RP INTERACTION WITH ODF1, AND TISSUE SPECIFICITY.
RX PubMed=9045620; DOI=10.1074/jbc.272.10.6105;
RA Shao X., Tarnasky H.A., Schalles U., Oko R., van der Hoorn F.A.;
RT "Interactional cloning of the 84-kDa major outer dense fiber protein Odf84.
RT Leucine zippers mediate associations of Odf84 and Odf27.";
RL J. Biol. Chem. 272:6105-6113(1997).
RN [8]
RP SELF-ASSOCIATION, AND SUBCELLULAR LOCATION.
RX PubMed=15340007; DOI=10.1242/jcs.01303;
RA Donkor F.F., Monnich M., Czirr E., Hollemann T., Hoyer-Fender S.;
RT "Outer dense fibre protein 2 (ODF2) is a self-interacting centrosomal
RT protein with affinity for microtubules.";
RL J. Cell Sci. 117:4643-4651(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; SER-69; THR-87; SER-101;
RP SER-104; THR-105; SER-110; SER-124; SER-134; SER-256 AND SER-627,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-37 (ISOFORM 3),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Seems to be a major component of sperm tail outer dense
CC fibers (ODF). ODFs are filamentous structures located on the outside of
CC the axoneme in the midpiece and principal piece of the mammalian sperm
CC tail and may help to maintain the passive elastic structures and
CC elastic recoil of the sperm tail. May have a modulating influence on
CC sperm motility. Functions as a general scaffold protein that is
CC specifically localized at the distal/subdistal appendages of mother
CC centrioles. Component of the centrosome matrix required for the
CC localization of PLK1 and NIN to the centrosomes. Required for the
CC formation and/or maintenance of normal CETN1 assembly.
CC -!- SUBUNIT: Self-associates. Associates with microtubules and forms a
CC fibrillar structure partially linked to the microtubule network.
CC Interacts through its C-terminus with PLK1. Interacts with ODF1
CC (PubMed:9045620). Interacts with MARK4; the interaction is required for
CC localization of ODF2 to centrioles (By similarity). Interacts with
CC TSSK4 (By similarity). Interacts with AKNA (By similarity). Interacts
CC with QRICH2 (By similarity). Interacts with CFAP58 (By similarity).
CC {ECO:0000250|UniProtKB:A3KGV1, ECO:0000250|UniProtKB:Q5BJF6,
CC ECO:0000269|PubMed:9045620}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:15340007}. Cell projection,
CC cilium {ECO:0000269|PubMed:15340007}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:15340007}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:15340007}. Cell projection, cilium, flagellum
CC {ECO:0000250|UniProtKB:A3KGV1}. Note=Localized at the microtubule
CC organizing centers in interphase and spindle poles in mitosis.
CC Localized at the distal/subdistal appendages of mother centrioles.
CC {ECO:0000250|UniProtKB:A3KGV1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q6AYX5-1; Sequence=Displayed;
CC Name=2; Synonyms=Cenexin 2;
CC IsoId=Q6AYX5-2; Sequence=VSP_027684, VSP_027685;
CC Name=3;
CC IsoId=Q6AYX5-3; Sequence=VSP_027678, VSP_027679, VSP_027682,
CC VSP_027683;
CC Name=4;
CC IsoId=Q6AYX5-4; Sequence=VSP_027677, VSP_027679, VSP_027682,
CC VSP_027683;
CC Name=5;
CC IsoId=Q6AYX5-5; Sequence=VSP_027677, VSP_027679, VSP_027680,
CC VSP_027681, VSP_027683;
CC -!- TISSUE SPECIFICITY: Testis-specific (PubMed:9045620). Expressed in the
CC proximal compartment of the elongated spermatid tail; later expression
CC progresses to the distal spermatid tail compartment located in the
CC lumen of the seminiferous epithelium (PubMed:9698445). In spermatids
CC (stages II-III) expression of the tails peaks and remains strong during
CC the remaining steps of spermiogenesis (at protein level)
CC (PubMed:9698445). Expression correlates with the onset of
CC spermatogenesis and is first detected at 30 days. Higher expression is
CC seen in testis of 40-day-old and adults that are older than 50 days
CC (PubMed:9092585). No expression is seen in 10- and 20-day-old testes
CC (PubMed:9092585). {ECO:0000269|PubMed:9045620,
CC ECO:0000269|PubMed:9092585, ECO:0000269|PubMed:9369191,
CC ECO:0000269|PubMed:9698445}.
CC -!- PTM: Tyrosine phosphorylated. Phosphorylated on Ser-90 by TSSK4.
CC {ECO:0000250|UniProtKB:A3KGV1, ECO:0000250|UniProtKB:Q2MJU7}.
CC -!- SIMILARITY: Belongs to the ODF2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA64567.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X95272; CAA64567.1; ALT_FRAME; mRNA.
DR EMBL; U62821; AAC53134.1; -; mRNA.
DR EMBL; AF053971; AAC08408.1; -; mRNA.
DR EMBL; AF162756; AAF80473.2; -; mRNA.
DR EMBL; AABR03024548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC078857; AAH78857.1; -; mRNA.
DR RefSeq; NP_001138477.1; NM_001145005.1.
DR RefSeq; NP_058909.2; NM_017213.2. [Q6AYX5-3]
DR RefSeq; XP_017447024.1; XM_017591535.1. [Q6AYX5-1]
DR AlphaFoldDB; Q6AYX5; -.
DR SMR; Q6AYX5; -.
DR BioGRID; 248121; 1.
DR STRING; 10116.ENSRNOP00000041336; -.
DR iPTMnet; Q6AYX5; -.
DR PhosphoSitePlus; Q6AYX5; -.
DR PaxDb; Q6AYX5; -.
DR Ensembl; ENSRNOT00000041921; ENSRNOP00000041336; ENSRNOG00000014584. [Q6AYX5-2]
DR GeneID; 29479; -.
DR KEGG; rno:29479; -.
DR UCSC; RGD:3229; rat. [Q6AYX5-1]
DR CTD; 4957; -.
DR RGD; 3229; Odf2.
DR VEuPathDB; HostDB:ENSRNOG00000014584; -.
DR eggNOG; ENOG502QUXQ; Eukaryota.
DR GeneTree; ENSGT00530000063497; -.
DR HOGENOM; CLU_018326_0_0_1; -.
DR InParanoid; Q6AYX5; -.
DR OMA; MEWRYQS; -.
DR OrthoDB; 328077at2759; -.
DR PhylomeDB; Q6AYX5; -.
DR Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-RNO-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-RNO-8854518; AURKA Activation by TPX2.
DR PRO; PR:Q6AYX5; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000014584; Expressed in testis and 20 other tissues.
DR ExpressionAtlas; Q6AYX5; baseline and differential.
DR Genevisible; Q6AYX5; RN.
DR GO; GO:0120103; C:centriolar subdistal appendage; ISO:RGD.
DR GO; GO:0005814; C:centriole; ISO:RGD.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0097539; C:ciliary transition fiber; ISO:RGD.
DR GO; GO:0005929; C:cilium; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0001520; C:outer dense fiber; IDA:RGD.
DR GO; GO:0036126; C:sperm flagellum; ISO:RGD.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0010457; P:centriole-centriole cohesion; ISO:RGD.
DR GO; GO:0044782; P:cilium organization; ISO:RGD.
DR GO; GO:0008104; P:protein localization; ISO:RGD.
DR GO; GO:1902017; P:regulation of cilium assembly; IBA:GO_Central.
DR GO; GO:0007286; P:spermatid development; IEP:RGD.
DR InterPro; IPR026099; Odf2-rel.
DR PANTHER; PTHR23162; PTHR23162; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium; Coiled coil; Cytoplasm;
KW Cytoskeleton; Developmental protein; Differentiation; Flagellum;
KW Isopeptide bond; Microtubule; Phosphoprotein; Reference proteome;
KW Spermatogenesis; Ubl conjugation.
FT CHAIN 1..825
FT /note="Outer dense fiber protein 2"
FT /id="PRO_0000299460"
FT REGION 27..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 139..212
FT /evidence="ECO:0000255"
FT COILED 240..418
FT /evidence="ECO:0000255"
FT COILED 456..793
FT /evidence="ECO:0000255"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 87
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 90
FT /note="Phosphoserine; by TSSK4"
FT /evidence="ECO:0000250|UniProtKB:A3KGV1"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 105
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 124
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 226
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5BJF6"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CROSSLNK 133
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q5BJF6"
FT VAR_SEQ 1..42
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:9092585,
FT ECO:0000303|PubMed:9369191"
FT /id="VSP_027677"
FT VAR_SEQ 1..36
FT /note="MKDRSSTPPLHVHVDENTPVHVHIKKLPKPSAASSQ -> MSASSSGGSPRF
FT PSCGKNGVTSLTQKKVLRTPCGAPSVTVT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9698445"
FT /id="VSP_027678"
FT VAR_SEQ 60..78
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9092585, ECO:0000303|PubMed:9369191,
FT ECO:0000303|PubMed:9698445"
FT /id="VSP_027679"
FT VAR_SEQ 276
FT /note="E -> ELCLKVPECARQHRPGRERQEDCQ (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:9369191"
FT /id="VSP_027680"
FT VAR_SEQ 630..652
FT /note="RSRIEHQGDKLELAREKHQASQK -> HSRVRDWQKGSHELARAGARLPR
FT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:9369191"
FT /id="VSP_027681"
FT VAR_SEQ 633..652
FT /note="IEHQGDKLELAREKHQASQK -> VRDWQKGSHELARAGARLPR (in
FT isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9092585, ECO:0000303|PubMed:9698445"
FT /id="VSP_027682"
FT VAR_SEQ 653..825
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9092585, ECO:0000303|PubMed:9369191,
FT ECO:0000303|PubMed:9698445"
FT /id="VSP_027683"
FT VAR_SEQ 763..769
FT /note="VDRRYQS -> ENQKCWK (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_027684"
FT VAR_SEQ 770..825
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_027685"
FT CONFLICT 46
FT /note="D -> Y (in Ref. 2; AAC53134)"
FT /evidence="ECO:0000305"
FT CONFLICT 107..108
FT /note="DD -> EE (in Ref. 1; CAA64567)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="K -> E (in Ref. 2; AAC53134)"
FT /evidence="ECO:0000305"
FT CONFLICT 483
FT /note="D -> H (in Ref. 2; AAC53134)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="A -> P (in Ref. 3; AAC08408)"
FT /evidence="ECO:0000305"
FT CONFLICT 543
FT /note="S -> T (in Ref. 1; CAA64567)"
FT /evidence="ECO:0000305"
FT MOD_RES Q6AYX5-3:22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES Q6AYX5-3:37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT Q6AYX5-3:25
FT /note="Q -> E (in Ref. 3; AAC08408)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 825 AA; 95440 MW; FF1490FF9F96CEC7 CRC64;
MKDRSSTPPL HVHVDENTPV HVHIKKLPKP SAASSQKSHK RGMKGDTVNV RRSVRVKTKV
PWMPPGKSSA RHVGCKWENP PHCLEITPPS SEKLVSVMRL SDLSTEDDDS GHCKMNRYDK
KIDSLMNAVG CLKSEVKMQK GERQMAKRFL EERKEELEEV AHELAETEHE NTVLRHNIER
IKEEKDFTML QKKHLQQEKE CLMSKLVEAE MDGAAAAKQV MALKDTIGKL KTEKQMTCTD
INTLTRQKEL LLQKLSTFEE TNRTLRDLLR EQHCKEDSER LMEQQGALLK RLAEADSEKA
RLLLLLQDKD KEVEELLQEI QCEKAQAKTA SELSKSMESM RGHLQAQLRC KEAENSRLCM
QIKNLERSGN QHKAEVEAIM EQLKELKQKG DRDKETLKKA IRAQKERAEK SEEYAEQLHV
QLADKDLYVA EALSTLESWR SRYNQVVKDK GDLELEIIVL NDRVTDLVNQ QQSLEEKMRE
DRDSLVERLH RQTAEYSAFK LENERLKASF APMEDKLNQA HLEVQQLKAS VKNYEGMIDN
YKSQVMKTRL EADEVAAQLE RCDKENKMLK DEMNKEIEAA RRQFQSQLAD LQQLPDILKI
TEAKLAECQD QLQGYERKNI DLTAIISDLR SRIEHQGDKL ELAREKHQAS QKENKQLSQK
VDELERKLEA TSTQNVEFLQ VIAKREEAIH QAQLRLEEKT RECGSLARQL ESAIEDARRQ
VEQTKEQALS KERAAQSKIL DLETQLSRTK TELGQLRRTR DDVDRRYQSR LQDLKDRLEQ
SESTNRSMQN YVQFLKSSYA NVFGDGPYTS SYLTSSPIRS RSPPA
