ID H7BXZ5_HUMAN Unreviewed; 2955 AA.
AC H7BXZ5;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE Flags: Fragment;
GN Name=KALRN {ECO:0000313|Ensembl:ENSP00000346122.4};
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 {ECO:0000313|Ensembl:ENSP00000346122.4, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000346122.4, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [2] {ECO:0007829|PubMed:18088087}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schutz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [3] {ECO:0007829|PubMed:18669648}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [4] {ECO:0000313|Ensembl:ENSP00000346122.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
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DR EMBL; AC022336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC069233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC080008; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC117401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF457679; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR MassIVE; H7BXZ5; -.
DR MaxQB; H7BXZ5; -.
DR PeptideAtlas; H7BXZ5; -.
DR ProteomicsDB; 43450; -.
DR Antibodypedia; 2142; 205 antibodies from 34 providers.
DR Ensembl; ENST00000354186.8; ENSP00000346122.4; ENSG00000160145.16.
DR UCSC; uc062neo.1; human.
DR HGNC; HGNC:4814; KALRN.
DR VEuPathDB; HostDB:ENSG00000160145; -.
DR GeneTree; ENSGT00940000155248; -.
DR HOGENOM; CLU_000373_2_0_1; -.
DR ChiTaRS; KALRN; human.
DR Proteomes; UP000005640; Chromosome 3.
DR Bgee; ENSG00000160145; Expressed in secondary oocyte and 167 other cell types or tissues.
DR ExpressionAtlas; H7BXZ5; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt.
DR CDD; cd00063; FN3; 1.
DR CDD; cd13240; PH1_Kalirin_Trio_like; 1.
DR CDD; cd13241; PH2_Kalirin_Trio_p63RhoGEF; 1.
DR CDD; cd00160; RhoGEF; 2.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd11852; SH3_Kalirin_1; 1.
DR CDD; cd11853; SH3_Kalirin_2; 1.
DR CDD; cd00176; SPEC; 5.
DR CDD; cd14115; STKc_Kalirin_C; 1.
DR Gene3D; 1.20.58.60; -; 5.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR047054; Kalirin_TRIO_PH_1.
DR InterPro; IPR028570; Kalirin_TRIO_SH3_1.
DR InterPro; IPR047053; Kalirin_TRIO_SH3_2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR22826:SF49; KALIRIN; 1.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00621; RhoGEF; 2.
DR Pfam; PF16609; SH3-RhoG_link; 1.
DR Pfam; PF00435; Spectrin; 4.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 2.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00516; SEC14; 1.
DR SMART; SM00326; SH3; 2.
DR SMART; SM00150; SPEC; 7.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR SUPFAM; SSF46966; Spectrin repeat; 6.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50010; DH_2; 2.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50002; SH3; 2.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Proteomics identification {ECO:0007829|EPD:H7BXZ5,
KW ECO:0007829|MaxQB:H7BXZ5};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..158
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1250..1425
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1437..1549
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1615..1680
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1898..2073
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2085..2195
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2290..2355
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2440..2533
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2540..2634
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2653..2907
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 686..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1563..1604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1699..1832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1869..1890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2214..2284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2381..2423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 897..924
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 699..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1586..1604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1699..1742
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1751..1773
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1782..1806
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2255..2269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2381..2403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2682
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT NON_TER 1
FT /evidence="ECO:0000313|Ensembl:ENSP00000346122.4"
SQ SEQUENCE 2955 AA; 336289 MW; CD1C4376D04CE4F4 CRC64;
XSFRNDGLKA SDVLPILKEK VAFVSGGRDK RGGPILTFPA RSNHDRIRQE DLRKLVTYLA
SVPSEDVCKR GFTVIIDMRG SKWDLIKPLL KTLQEAFPAE IHVALIIKPD NFWQKQKTNF
GSSKFIFETS MVSVEGLTKL VDPSQLTEEF DGSLDYNHEE WIELRLSLEE FFNSAVHLLS
RLEDLQEMLA RKEFPVDVEG SRRLIDEHTQ LKKKVLKAPV EELDREGQRL LQCIRCSDGF
SGRNCIPGSA DFQSLVPKIT SLLDKLHSTR QHLHQMWHVR KLKLDQCFQL RLFEQDAEKM
FDWISHNKEL FLQSHTEIGV SYQYALDLQT QHNHFAMNSM NAYVNINRIM SVASRLSEAG
HYASQQIKQI STQLDQEWKS FAAALDERST ILAMSAVFHQ KAEQFLSGVD AWCKMCSEGG
LPSEMQDLEL AIHHHQTLYE QVTQAYTEVS QDGKALLDVL QRPLSPGNSE SLTATANYSK
AVHQVLDVVH EVLHHQRRLE SIWQHRKVRL HQRLQLCVFQ QDVQQVLDWI ENHGEAFLSK
HTGVGKSLHR ARALQKRHDD FEEVAQNTYT NADKLLEAAE QLAQTGECDP EEIYKAARHL
EVRIQDFVRR VEQRKLLLDM SVSFHTHTKE LWTWMEDLQK EMLEDVCADS VDAVQELIKQ
FQQQQTATLD ATLNVIKEGE DLIQQLRSAP PSLGEPSEAR DSAVSNNKTP HSSSISHIES
VLQQLDDAQV QMEELFHERK IKLDIFLQLR IFEQYTIEVT AELDAWNEDL LRQMNDFNTE
DLTLAEQRLQ RHTERKLAMN NMTFEVIQQG QDLHQYITEV QASGIELICE KDIDLAAQVQ
ELLEFLHEKQ HELELNAEQT HKRLEQCLQL RHLQAEVKQV LGWIRNGESM LNASLVNASS
LSEAEQLQRE HEQFQLAIEK THQSALQVQQ KAEVLLQAGH YDADAIRECA EKVALHWQQL
MLKMEDRLKL VNASVAFYKT SEQVCSVLES LEQEYRRDED WCGGRDKLGP AAEIDHVIPL
ISKHLEQKEA FLKACTLARR NAEVFLKYIH RNNVSMPSVA SHTRGPEQQV KAILSELLQR
ENRVLHFWTL KKRRLDQCQQ YVVFERSAKQ ALDWIQETGE FYLSTHTSTG ETTEETQELL
KEYGEFRVPA KQTKEKVKLL IQLADSFVEK GHIHATEIRK WVTTVDKHYR DFSLRMGKYR
YSLEKALGVN TEDNKDLELD IIPASLSDRE VKLRDANHEV NEEKRKSARK KEFIMAELLQ
TEKAYVRDLH ECLETYLWEM TSGVEEIPPG ILNKEHIIFG NIQEIYDFHN NIFLKELEKY
EQLPEDVGHC FVTWADKFQM YVTYCKNKPD SNQLILEHAG TFFDEIQQRH GLANSISSYL
IKPVQRITKY QLLLKELLTC CEEGKGELKD GLEVMLSVPK KANDAMHVSM LEGFDENLDV
QGELILQDAF QVWDPKSLIR KGRERHLFLF EISLVFSKEI KDSSGHTKYV YKNKLLTSEL
GVTEHVEGDP CKFALWSGRT PSSDNKTVLK ASNIETKQEW IKNIREVIQE RIIHLKGALK
EPLQLPKTPA KQRNNSKRDG VEDIDSQGDG SSQPDTISIA SRTSQNTVDS DKLSGGCELT
VVLQDFSAGH SSELTIQVGQ TVELLERPSE RPGWCLVRTT ERSPPLEGLV PSSALCISHS
RSSVEMDCFF PLVKDAYSHS SSENGGKSES VANLQAQPSL NSIHSSPGPK RSTNTLKKWL
TSPVRRLNSG KADGNIKKQK KVRDGRKSFD LGSPKPGDET TPQGDSADEK SKKGWGEDEP
DEESHTPLPP PMKIFDNDPT QDEMSSSLLA ARQASTEVPT AADLVNAIEK LVKNKLSLEG
SSYRGSLKDP AGCLNEGMAP PTPPKNPEEE QKAKALRGRM FVLNELVQTE KDYVKDLGIV
VEGFMKRIEE KGVPEDMRGK DKIVFGNIHQ IYDWHKDFFL AELEKCIQEQ DRLAQLFIKH
ERKLHIYVWY CQNKPRSEYI VAEYDAYFEE VKQEINQRLT LSDFLIKPIQ RITKYQLLLK
DFLRYSEKAG LECSDIEKAV ELMCLVPKRC NDMMNLGRLQ GFEGTLTAQG KLLQQDTFYV
IELDAGMQSR TKERRVFLFE QIVIFSELLR KGSLTPGYMF KRSIKMNYLV LEENVDNDPC
KFALMNRETS ERVVLQAANA DIQQAWVQDI NQVLETQRDF LNALQSPIEY QRKERSTAVM
RSQPARLPQA SPRPYSSVPA GSEKPPKGSS YNPPLPPLKI STSNGSPGFE YHQPGDKFEA
SKQNDLGGCN GTSSMAVIKD YYALKENEIC VSQGEVVQVL AVNQQNMCLV YQPASDHSPA
AEGWVPGSIL APLTKATAAE SSDGSIKKSC SWHTLRMRKR AEVENTGKNE ATGPRKPKDI
LGNKVSVKET NSSEESECDD LDPNTSMEIL NPNFIQEVAP EFLVPLVDVT CLLGDTVILQ
CKVCGRPKPT ITWKGPDQNI LDTDNSSATY TVSSCDSGEI TLKICNLMPQ DSGIYTCIAT
NDHGTTSTSA TVKVQGVPAA PNRPIAQERS CTSVILRWLP PSSTGNCTIS GYTVEYREEG
SQIWQQSVAS TLDTYLVIED LSPGCPYQFR VSASNPWGIS LPSEPSEFVR LPEYDAAADG
ATISWKENFD SAYTELNEIG RGRFSIVKKC IHKATRKDVA VKFVSKKMKK KEQAAHEAAL
LQHLQHPQYI TLHDTYESPT SYILILELMD DGRLLDYLMN HDELMEEKVA FYIRDIMEAL
QYLHNCRVAH LDIKPENLLI DLRIPVPRVK LIDLEDAVQI SGHFHIHHLL GNPEFAAPEV
IQGIPVSLGT DIWSIGVLTY VMLSGVSPFL DESKEETCIN VCRVDFSFPH EYFCGVSNAA
RDFINVILQE DFRRRPTAAT CLQHPWLQPH NGSYSKIPLD TSRLACFIER RKHQNDVRPI
PNVKSYIVNR VNQGT
//
