CK5P2_MOUSE
ID CK5P2_MOUSE Reviewed; 1822 AA.
AC Q8K389; A2AVA1; Q6PCN1; Q6ZPL0;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=CDK5 regulatory subunit-associated protein 2;
DE AltName: Full=CDK5 activator-binding protein C48;
GN Name=Cdk5rap2; Synonyms=Kiaa1633;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 438-1822.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [5]
RP LACK OF INTERACTION WITH MAPRE1, AND SUBCELLULAR LOCATION.
RX PubMed=19553473; DOI=10.1091/mbc.e09-01-0009;
RA Fong K.W., Hau S.Y., Kho Y.S., Jia Y., He L., Qi R.Z.;
RT "Interaction of CDK5RAP2 with EB1 to track growing microtubule tips and to
RT regulate microtubule dynamics.";
RL Mol. Biol. Cell 20:3660-3670(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485; THR-1195; SER-1245 AND
RP SER-1497, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20627074; DOI=10.1016/j.devcel.2010.05.017;
RA Barrera J.A., Kao L.R., Hammer R.E., Seemann J., Fuchs J.L., Megraw T.L.;
RT "CDK5RAP2 regulates centriole engagement and cohesion in mice.";
RL Dev. Cell 18:913-926(2010).
RN [8]
RP FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=20460369; DOI=10.1242/dev.040410;
RA Lizarraga S.B., Margossian S.P., Harris M.H., Campagna D.R., Han A.P.,
RA Blevins S., Mudbhary R., Barker J.E., Walsh C.A., Fleming M.D.;
RT "Cdk5rap2 regulates centrosome function and chromosome segregation in
RT neuronal progenitors.";
RL Development 137:1907-1917(2010).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=20466722; DOI=10.1074/jbc.m110.105965;
RA Wang Z., Wu T., Shi L., Zhang L., Zheng W., Qu J.Y., Niu R., Qi R.Z.;
RT "Conserved motif of CDK5RAP2 mediates its localization to centrosomes and
RT the Golgi complex.";
RL J. Biol. Chem. 285:22658-22665(2010).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INTERACTION WITH
RP PCNT.
RX PubMed=20471352; DOI=10.1016/j.neuron.2010.03.036;
RA Buchman J.J., Tseng H.C., Zhou Y., Frank C.L., Xie Z., Tsai L.H.;
RT "Cdk5rap2 interacts with pericentrin to maintain the neural progenitor pool
RT in the developing neocortex.";
RL Neuron 66:386-402(2010).
CC -!- FUNCTION: Potential regulator of CDK5 activity via its interaction with
CC CDK5R1. Negative regulator of centriole disengagement (licensing) which
CC maintains centriole engagement and cohesion (PubMed:20627074). Involved
CC in regulation of mitotic spindle orientation (PubMed:20460369). Plays a
CC role in the spindle checkpoint activation by acting as a
CC transcriptional regulator of both BUBR1 and MAD2 promoter. Required for
CC the recruitment of AKAP9 to centrosomes (By similarity). Plays a role
CC in neurogenesis (PubMed:20471352). Contrary to higher mammalian
CC orthologs, including human, chimpanzee, bovine and dog, does not
CC interact with EB1/MAPRE1, therefore its function in the regulation of
CC microtubule dynamics is unclear (PubMed:19553473).
CC {ECO:0000250|UniProtKB:Q96SN8, ECO:0000269|PubMed:19553473,
CC ECO:0000269|PubMed:20460369, ECO:0000269|PubMed:20471352,
CC ECO:0000269|PubMed:20627074}.
CC -!- SUBUNIT: Interacts with CDK5R1 (p35 form) (By similarity). CDK5RAP1,
CC CDK5RAP2 and CDK5RAP3 show competitive binding to CDK5R1. May form a
CC complex with CDK5R1 and CDK5 (By similarity). Interacts (via C-
CC terminus) with PCNT; the interaction is leading to centrosomal
CC localization of CDK5RAP2 and PCNT. Interacts with AKAP9; the
CC interaction is leading to Golgi localization of CDK5RAP2 and AKAP9 (By
CC similarity). Interacts with TUBG1; the interaction is leading to the
CC centrosomal localization of CDK5RAP2 and TUBG1 (By similarity).
CC Interacts with TUBGCP3 (By similarity). Interacts with CALM1 (By
CC similarity). Interacts with CDC20 (By similarity). Interacts with
CC CEP68; degradation of CEP68 in early mitosis leads to removal of
CC CDK5RAP2 from the centrosome which promotes centriole disengagement and
CC subsequent centriole separation (By similarity). Interacts with NCKAP5L
CC (By similarity). Interacts with LGALS3BP; this interaction may connect
CC the pericentrosomal complex to the gamma-tubulin ring complex (gamma-
CC TuRC) to promote microtubule assembly and acetylation (By similarity).
CC Contrary to human, chimpanzee, bovine and dog orthologous proteins,
CC does not interact with EB1/MAPRE1, possibly due to a divergence at the
CC level of the critical residue 940, which is a proline in MAPRE1-binding
CC orthologs and a leucine in mouse and rat (PubMed:19553473).
CC {ECO:0000250|UniProtKB:Q96SN8, ECO:0000250|UniProtKB:Q9JLH5,
CC ECO:0000269|PubMed:19553473, ECO:0000269|PubMed:20471352}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:20466722,
CC ECO:0000269|PubMed:20471352, ECO:0000269|PubMed:20627074,
CC ECO:0000305|PubMed:19553473}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q96SN8}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96SN8}. Note=Found in the pericentriolar region
CC adhering to the surface of the centrosome and in the region of the
CC centrosomal appendages. Due to the lack of interaction with EB1/MAPRE1,
CC its localization to microtubule plus ends may not be conserved in mice
CC (Probable). Localization to centrosomes versus Golgi apparatus may be
CC cell type-dependent (By similarity). {ECO:0000250|UniProtKB:Q96SN8,
CC ECO:0000305|PubMed:19553473}.
CC -!- TISSUE SPECIFICITY: Expressed in testis, thymus, heart and brain.
CC {ECO:0000269|PubMed:20460369}.
CC -!- DEVELOPMENTAL STAGE: Detected in the developing cortex at 9.5 dpc.
CC Expression peaks between 10.5 and 13.5 dpc, remains robust at 15.5 dpc
CC and declines thereafter. This peak corresponds to periods of active
CC neurogenesis. {ECO:0000269|PubMed:20460369,
CC ECO:0000269|PubMed:20471352}.
CC -!- PTM: Phosphorylated in vitro by CDK5. {ECO:0000250|UniProtKB:Q9JLH5}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98221.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK129411; BAC98221.1; ALT_INIT; mRNA.
DR EMBL; AL845502; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929409; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC059253; AAH59253.1; -; mRNA.
DR CCDS; CCDS38779.1; -.
DR RefSeq; NP_666102.2; NM_145990.4.
DR AlphaFoldDB; Q8K389; -.
DR SMR; Q8K389; -.
DR BioGRID; 229527; 33.
DR IntAct; Q8K389; 21.
DR MINT; Q8K389; -.
DR STRING; 10090.ENSMUSP00000119891; -.
DR iPTMnet; Q8K389; -.
DR PhosphoSitePlus; Q8K389; -.
DR EPD; Q8K389; -.
DR jPOST; Q8K389; -.
DR MaxQB; Q8K389; -.
DR PaxDb; Q8K389; -.
DR PRIDE; Q8K389; -.
DR ProteomicsDB; 279089; -.
DR Antibodypedia; 30055; 143 antibodies from 24 providers.
DR DNASU; 214444; -.
DR Ensembl; ENSMUST00000144099; ENSMUSP00000119891; ENSMUSG00000039298.
DR GeneID; 214444; -.
DR KEGG; mmu:214444; -.
DR UCSC; uc008thy.1; mouse.
DR CTD; 55755; -.
DR MGI; MGI:2384875; Cdk5rap2.
DR VEuPathDB; HostDB:ENSMUSG00000039298; -.
DR eggNOG; ENOG502QTI7; Eukaryota.
DR GeneTree; ENSGT00950000183190; -.
DR HOGENOM; CLU_002129_0_0_1; -.
DR InParanoid; Q8K389; -.
DR OMA; RICLAEQ; -.
DR OrthoDB; 1046642at2759; -.
DR PhylomeDB; Q8K389; -.
DR TreeFam; TF329233; -.
DR Reactome; R-MMU-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-MMU-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-MMU-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-MMU-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-MMU-8854518; AURKA Activation by TPX2.
DR BioGRID-ORCS; 214444; 10 hits in 72 CRISPR screens.
DR ChiTaRS; Cdk5rap2; mouse.
DR PRO; PR:Q8K389; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8K389; protein.
DR Bgee; ENSMUSG00000039298; Expressed in dorsal pancreas and 175 other tissues.
DR ExpressionAtlas; Q8K389; baseline and differential.
DR Genevisible; Q8K389; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000931; C:gamma-tubulin large complex; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:MGI.
DR GO; GO:0000242; C:pericentriolar material; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0071889; F:14-3-3 protein binding; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0043015; F:gamma-tubulin binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0015631; F:tubulin binding; ISO:MGI.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:0007099; P:centriole replication; IBA:GO_Central.
DR GO; GO:0007098; P:centrosome cycle; ISS:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR GO; GO:0031023; P:microtubule organizing center organization; ISS:UniProtKB.
DR GO; GO:0046600; P:negative regulation of centriole replication; IMP:UniProtKB.
DR GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0022008; P:neurogenesis; IMP:UniProtKB.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0090266; P:regulation of mitotic cell cycle spindle assembly checkpoint; ISS:UniProtKB.
DR InterPro; IPR042791; CDK5RAP2.
DR InterPro; IPR012943; Cnn_1N.
DR PANTHER; PTHR46930; PTHR46930; 1.
DR Pfam; PF07989; Cnn_1N; 1.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Cytoplasm; Cytoskeleton; Golgi apparatus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1822
FT /note="CDK5 regulatory subunit-associated protein 2"
FT /id="PRO_0000089837"
FT REGION 57..195
FT /note="Interaction with NCKAP5L"
FT /evidence="ECO:0000250|UniProtKB:Q96SN8"
FT REGION 1022..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1201..1822
FT /note="Interaction with PCNT and AKAP9"
FT /evidence="ECO:0000269|PubMed:20471352"
FT REGION 1350..1391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1655..1822
FT /note="Required for centrosomal attachment, Golgi targeting
FT and CALM1 interaction"
FT /evidence="ECO:0000250"
FT REGION 1655..1697
FT /note="Interaction with CDK5R1"
FT /evidence="ECO:0000250"
FT REGION 1688..1822
FT /note="Interaction with PCNT"
FT /evidence="ECO:0000269|PubMed:20471352"
FT REGION 1790..1799
FT /note="Required for centrosomal attachment, Golgi
FT localization and CALM1 interaction"
FT /evidence="ECO:0000250"
FT COMPBIAS 1366..1389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96SN8"
FT MOD_RES 1195
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96SN8"
FT MOD_RES 1245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1497
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1592
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLH5"
FT MOD_RES 1595
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JLH5"
FT MOD_RES 1822
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96SN8"
SQ SEQUENCE 1822 AA; 205945 MW; DDD6CD7B8CFC8DA9 CRC64;
MDSGMEEEGA LPGTLSGCSG LHPVLPSDLD VISDTSGLGN GVLPSMSEEK VSPTRARNMK
DFENQITELK KENFNLKLRI YFLEERIQQE FAGPTEHIYK TNIELKVEVE SLKRELQEKD
QLLVKASKAV ESLAERGGSE VQRVKEDARK KVQQVEDLLT KRIHLLEEDV KAAQAELEKA
FAGTETEKAL RLSLESKLSA MKKMQEGDLE MTLALEEKDR LIEELKLSLK SKEALIQCLK
EEKSQMASPD ENVSSGELRG LSATLREEKE RDAEEWQKER NHFEERIQAL QEDLREKERE
IATEKKNNLK SYKAIQGLTM ALKSKEREVE ELDSKIKEVT TDSTKGREDP LKTQIPRFQL
REGSEDCEAA LVEKEALLAK LHSENVTKST ENHRLLRNVK KVTQELNDLK KEKLRLEQAL
EEAHQEGNRG ARTIHDLRNE VEKLRKEVSE REKAVEKHYK SLPGESKTKF HTQEQVVRSL
TGSGSQEDLL LQKSNEKDLE AIQQNCYLMT AEELKFGSDG LITEKCSQQS PDSKLIFSKE
KQQSEYEGLT GDLKAEQNIY AHLAKTQDTD SVSNLQAELK EVLALRKQLE QDVLAYRNLQ
KALQEQLSEI RSREEEPFSF YSDQTSYLSI CLEEHNQFQL EHFSQEELKK KVSDLIQLVK
DLHTDNQHLK KTIFDLSSVG FQGSDRLELT KQEELVASKE DEDTLKFEAD VETPFQSDQH
LEQSREIMED YAEGGCKSGY GRHMDSNILG HDGAQTPGAS EEHTLEDELL GLLATLFSKK
ATPLLESRPD LLKALGALLL ERICLAEQGR PGDHLDSKTE KALQQVAVQL RDELGHSFPA
NSFSKSYNEV KSMWGNWLVK TGDEDTVELK SVSVQTMAIE DTPHGFKPQS KRDAWAEKQE
EAIFSTELES EALGEMPGQQ ATHLSFPSAI NPDAEKTGLL IQLKTPELLE NLYNLPASPE
VVVAQLQGQV LELQRELKEF KTRNKQLHEK LILAEAMMEG LPVPNSALVN VPAAQAVVRT
AFQDNPGEQE GPETTQSAGR DKDMDSDQYT SFEIDSEICP PDDLALLPAC KENLEDLLGP
SSIATYLDSK SQLSVKVSVN GTDQSENINI PDDTEDLKQK IHDLQTELEG YRNIIVQLLK
HSQCSEAIIT VLCGTEGAQD GLNKPKGHID EEEMTFSSLH QVRYVKHMKI LRPLTPEMID
GKMLESLKQQ LVDQEQELQK EQDLNLELFG EIHDLQNKFQ DLSPSRYDSL VQSQARELSL
QRQQIKDSHG ICVIYRQHMS TMIKAFEELL QASDVDSCVA EGFREQLTQC AGLLEQLERL
FLHGKSARVE PHPQNELLKG LRTVEGNLPY HHLLPESPEP SASHALSDDE MSEKSFLSRD
PKPDSDTEKY PAMASHFPQD LLMEHIQEIR TLRKHLEESI KTNEKLRKQL ERQGSETDQG
SRNVSACGLA LHSSLTSEIH FLRKQNEALS MMLEKGSKDK QKESEKLRES LARKAESLEQ
LQLEYTSVRE ENERLQRDII EKERHNQELT EEVCSSRQEL SRVQEEAKSR QQLLSQKDKL
LQSLQMELKV YEKLAEEHPR LQQDGSKCPE ASDNSFDLFE STQAMAPKSA SETPLLSGTD
VDSLSCDSTS SATSPTSMPC LVAGHHMWAS KSGHHMLGLI EDYDALYKQI SWGQTLLAKM
DVQTQEALSP TSHKLGPKGS SSVPLSKFLS SMNTAKLVLE KASRLLKLFW RVSVPTNGQC
SLHCEQIGEM KAENTKLHKK LFEQEKKLQN TAKLLQQSKH QEKVIFDQLV ITHQVLRKAR
GNLELRPGAT RPGASSPSRP GS
