KI21B_HUMAN
ID KI21B_HUMAN Reviewed; 1637 AA.
AC O75037; B2RP62; B7ZMI0; Q5T4J3;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Kinesin-like protein KIF21B;
GN Name=KIF21B; Synonyms=KIAA0449;
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 2).
RC TISSUE=Brain;
RX PubMed=9455484; DOI=10.1093/dnares/4.5.345;
RA Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D.,
RA Nomura N., Ohara O.;
RT "Characterization of cDNA clones in size-fractionated cDNA libraries from
RT human brain.";
RL DNA Res. 4:345-349(1997).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (AUG-2005) 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 3 AND 4).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1237, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1237 AND SER-1241, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1167 AND THR-1237, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1149; SER-1167 AND SER-1215,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: Plus-end directed microtubule-dependent motor protein which
CC displays processive activity. Is involved in regulation of microtubule
CC dynamics, synapse function and neuronal morphology, including dendritic
CC tree branching and spine formation. Plays a role in lerning and memory.
CC Involved in delivery of gamma-aminobutyric acid (GABA(A)) receptor to
CC cell surface. {ECO:0000250|UniProtKB:Q9QXL1}.
CC -!- SUBUNIT: Interacts with TRIM3; the interaction positively affects
CC motility of KIF21B. Interacts with GABARAP and GABA(A) receptor
CC subunits: GABRG2, GABRA1 and GABRA2. May interact with GABA(A) receptor
CC subunits: GABRB2 and GABRB3. {ECO:0000250|UniProtKB:F1M5N7,
CC ECO:0000250|UniProtKB:Q9QXL1}.
CC -!- INTERACTION:
CC O75037-4; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-12897871, EBI-741158;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9QXL1}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9QXL1}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q9QXL1}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q9QXL1}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:F1M5N7}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O75037-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75037-2; Sequence=VSP_016217;
CC Name=3;
CC IsoId=O75037-3; Sequence=VSP_016217, VSP_045333;
CC Name=4;
CC IsoId=O75037-4; Sequence=VSP_045333;
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA32294.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB007918; BAA32294.2; ALT_INIT; mRNA.
DR EMBL; AC099756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL358473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91328.1; -; Genomic_DNA.
DR EMBL; BC137281; AAI37282.1; -; mRNA.
DR EMBL; BC144557; AAI44558.1; -; mRNA.
DR CCDS; CCDS30965.1; -. [O75037-2]
DR CCDS; CCDS58054.1; -. [O75037-3]
DR CCDS; CCDS58055.1; -. [O75037-4]
DR CCDS; CCDS58056.1; -. [O75037-1]
DR PIR; T00066; T00066.
DR RefSeq; NP_001239029.1; NM_001252100.1. [O75037-1]
DR RefSeq; NP_001239031.1; NM_001252102.1. [O75037-4]
DR RefSeq; NP_001239032.1; NM_001252103.1. [O75037-3]
DR RefSeq; NP_060066.2; NM_017596.3. [O75037-2]
DR AlphaFoldDB; O75037; -.
DR SMR; O75037; -.
DR BioGRID; 116684; 43.
DR IntAct; O75037; 37.
DR MINT; O75037; -.
DR STRING; 9606.ENSP00000411831; -.
DR GlyGen; O75037; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75037; -.
DR PhosphoSitePlus; O75037; -.
DR BioMuta; KIF21B; -.
DR EPD; O75037; -.
DR jPOST; O75037; -.
DR MassIVE; O75037; -.
DR MaxQB; O75037; -.
DR PaxDb; O75037; -.
DR PeptideAtlas; O75037; -.
DR PRIDE; O75037; -.
DR ProteomicsDB; 3445; -.
DR ProteomicsDB; 49715; -. [O75037-1]
DR ProteomicsDB; 49716; -. [O75037-2]
DR ProteomicsDB; 7261; -.
DR Antibodypedia; 20638; 64 antibodies from 15 providers.
DR DNASU; 23046; -.
DR Ensembl; ENST00000332129.6; ENSP00000328494.2; ENSG00000116852.15. [O75037-2]
DR Ensembl; ENST00000360529.9; ENSP00000353724.5; ENSG00000116852.15. [O75037-3]
DR Ensembl; ENST00000422435.2; ENSP00000411831.2; ENSG00000116852.15. [O75037-1]
DR Ensembl; ENST00000461742.7; ENSP00000433808.1; ENSG00000116852.15. [O75037-4]
DR GeneID; 23046; -.
DR KEGG; hsa:23046; -.
DR MANE-Select; ENST00000461742.7; ENSP00000433808.1; NM_001252102.2; NP_001239031.1. [O75037-4]
DR UCSC; uc001gvr.3; human. [O75037-1]
DR CTD; 23046; -.
DR DisGeNET; 23046; -.
DR GeneCards; KIF21B; -.
DR HGNC; HGNC:29442; KIF21B.
DR HPA; ENSG00000116852; Tissue enhanced (bone marrow, brain, retina).
DR MIM; 608322; gene.
DR neXtProt; NX_O75037; -.
DR OpenTargets; ENSG00000116852; -.
DR PharmGKB; PA134925106; -.
DR VEuPathDB; HostDB:ENSG00000116852; -.
DR eggNOG; KOG0244; Eukaryota.
DR GeneTree; ENSGT00940000159650; -.
DR HOGENOM; CLU_001485_4_5_1; -.
DR InParanoid; O75037; -.
DR OMA; HKQRVIQ; -.
DR PhylomeDB; O75037; -.
DR TreeFam; TF105224; -.
DR PathwayCommons; O75037; -.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; O75037; -.
DR BioGRID-ORCS; 23046; 17 hits in 1085 CRISPR screens.
DR ChiTaRS; KIF21B; human.
DR GenomeRNAi; 23046; -.
DR Pharos; O75037; Tbio.
DR PRO; PR:O75037; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O75037; protein.
DR Bgee; ENSG00000116852; Expressed in cortical plate and 153 other tissues.
DR Genevisible; O75037; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR24115; PTHR24115; 1.
DR Pfam; PF00225; Kinesin; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Microtubule; Motor protein;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1637
FT /note="Kinesin-like protein KIF21B"
FT /id="PRO_0000125464"
FT DOMAIN 8..370
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REPEAT 1306..1343
FT /note="WD 1"
FT REPEAT 1346..1384
FT /note="WD 2"
FT REPEAT 1410..1448
FT /note="WD 3"
FT REPEAT 1451..1493
FT /note="WD 4"
FT REPEAT 1502..1539
FT /note="WD 5"
FT REPEAT 1543..1582
FT /note="WD 6"
FT REPEAT 1585..1622
FT /note="WD 7"
FT REGION 400..1099
FT /note="Interaction with TRIM3"
FT /evidence="ECO:0000250|UniProtKB:Q9QXL1"
FT REGION 509..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1194..1251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 376..604
FT /evidence="ECO:0000255"
FT COILED 631..824
FT /evidence="ECO:0000255"
FT COILED 928..1016
FT /evidence="ECO:0000255"
FT COMPBIAS 552..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..623
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 848..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 87..94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXL1"
FT MOD_RES 582
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QXL1"
FT MOD_RES 1149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1237
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT MOD_RES 1241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1269..1281
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9455484"
FT /id="VSP_016217"
FT VAR_SEQ 1607..1636
FT /note="CRVKLWNYVPGLTPCLPRRVLAIKGRATTL -> LTVKFWSVRRLPHSGP
FT (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045333"
SQ SEQUENCE 1637 AA; 182662 MW; 792647EA1D909C24 CRC64;
MAGQGDCCVK VAVRIRPQLS KEKIEGCHIC TSVTPGEPQV LLGKDKAFTY DFVFDLDTWQ
EQIYSTCVSK LIEGCFEGYN ATVLAYGQTG AGKTYTMGTG FDMATSEEEQ GIIPRAIAHL
FGGIAERKRR AQEQGVAGPE FKVSAQFLEL YNEEILDLFD STRDPDTRHR RSNIKIHEDA
NGGIYTTGVT SRLIHSQEEL IQCLKQGALS RTTASTQMNV QSSRSHAIFT IHLCQMRMCT
QPDLVNEAVT GLPDGTPPSS EYETLTAKFH FVDLAGSERL KRTGATGERA KEGISINCGL
LALGNVISAL GDQSKKVVHV PYRDSKLTRL LQDSLGGNSQ TIMIACVSPS DRDFMETLNT
LKYANRARNI KNKVVVNQDK TSQQISALRA EIARLQMELM EYKAGKRVIG EDGAEGYSDL
FRENAMLQKE NGALRLRVKA MQEAIDAINN RVTQLMSQEA NLLLAKAGDG NEAIGALIQN
YIREIEELRT KLLESEAMNE SLRRSLSRAS ARSPYSLGAS PAAPAFGGSP ASSMEDASEV
IRRAKQDLER LKKKEVRQRR KSPEKEAFKK RAKLQQENSE ETDENEAEEE EEERDESGCE
EEEGREDEDE DSGSEESLVD SDSDPEEKEV NFQADLADLT CEIEIKQKLI DELENSQRRL
QTLKHQYEEK LILLQNKIRD TQLERDRVLQ NLSTMECYTE EKANKIKADY EKRLREMNRD
LQKLQAAQKE HARLLKNQSR YERELKKLQA EVAEMKKAKV ALMKQMREEQ QRRRLVETKR
NREIAQLKKE QRRQEFQIRA LESQKRQQEM VLRRKTQEVS ALRRLAKPMS ERVAGRAGLK
PPMLDSGAEV SASTTSSEAE SGARSVSSIV RQWNRKINHF LGDHPAPTVN GTRPARKKFQ
KKGASQSFSK AARLKWQSLE RRIIDIVMQR MTIVNLEADM ERLIKKREEL FLLQEALRRK
RERLQAESPE EEKGLQELAE EIEVLAANID YINDGITDCQ ATIVQLEETK EELDSTDTSV
VISSCSLAEA RLLLDNFLKA SIDKGLQVAQ KEAQIRLLEG RLRQTDMAGS SQNHLLLDAL
REKAEAHPEL QALIYNVQQE NGYASTDEEI SEFSEGSFSQ SFTMKGSTSH DDFKFKSEPK
LSAQMKAVSA ECLGPPLDIS TKNITKSLAS LVEIKEDGVG FSVRDPYYRD RVSRTVSLPT
RGSTFPRQSR ATETSPLTRR KSYDRGQPIR STDVGFTPPS SPPTRPRNDR NVFSRLTSNQ
SQGSALDKSD DSDSSLSEVL RGIISPVGGA KGARTAPLQC VSMAEGHTKP ILCLDATDEL
LFTGSKDRSC KMWNLVTGQE IAALKGHPNN VVSIKYCSHS GLVFSVSTSY IKVWDIRDSA
KCIRTLTSSG QVISGDACAA TSTRAITSAQ GEHQINQIAL SPSGTMLYAA SGNAVRIWEL
SRFQPVGKLT GHIGPVMCLT VTQTASQHDL VVTGSKDHYV KMFELGECVT GTIGPTHNFE
PPHYDGIECL AIQGDILFSG SRDNGIKKWD LDQQELIQQI PNAHKDWVCA LAFIPGRPML
LSACRAGVIK VWNVDNFTPI GEIKGHDSPI NAICTNAKHI FTASSDCRVK LWNYVPGLTP
CLPRRVLAIK GRATTLP
