CTRO_RAT
ID CTRO_RAT Reviewed; 2055 AA.
AC E9PSL7; A0A0G2JWA9; Q9QX19;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Citron rho-interacting kinase {ECO:0000250|UniProtKB:O14578};
DE Short=CRIK {ECO:0000250|UniProtKB:O14578};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P49025};
DE AltName: Full=Rho-interacting, serine/threonine-protein kinase 21 {ECO:0000250|UniProtKB:P49025};
GN Name=Cit {ECO:0000312|RGD:70878};
GN Synonyms=CRIK {ECO:0000250|UniProtKB:O14578};
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 {ECO:0000312|Proteomes:UP000002494};
RN [1] {ECO:0000312|EMBL:AAC25483.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Zhang W., Apperson M.L., Vasquez L.E., Kennedy M.B.;
RT "Citron, a PSD-95-binding protein at glutamatergic synapses on inhibitory
RT neurons.";
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000002494}
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 [3] {ECO:0007744|PubMed:22673903}
RP 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).
RN [4] {ECO:0000305}
RP FUNCTION.
RX PubMed=24695496; DOI=10.1371/journal.pone.0093721;
RA Berto G.E., Iobbi C., Camera P., Scarpa E., Iampietro C., Bianchi F.,
RA Gai M., Sgro F., Cristofani F., Gaertner A., Dotti C.G., Di Cunto F.;
RT "The DCR protein TTC3 affects differentiation and Golgi compactness in
RT neurons through specific actin-regulating pathways.";
RL PLoS ONE 9:E93721-E93721(2014).
CC -!- FUNCTION: Plays a role in cytokinesis (By similarity). Required for
CC KIF14 localization to the central spindle and midbody (By similarity).
CC Putative RHO/RAC effector that binds to the GTP-bound forms of RHO and
CC RAC1 (By similarity). It probably binds p21 with a tighter specificity
CC in vivo (By similarity). Displays serine/threonine protein kinase
CC activity (By similarity). Plays an important role in the regulation of
CC cytokinesis and the development of the central nervous system
CC (PubMed:24695496). Phosphorylates MYL9/MLC2 (By similarity).
CC {ECO:0000250|UniProtKB:O14578, ECO:0000269|PubMed:24695496}.
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:0000250|UniProtKB:P49025};
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:0000250|UniProtKB:P49025};
CC -!- SUBUNIT: Homodimer (By similarity). Directly interacts with KIF14
CC depending on the activation state (stronger interaction with the
CC kinase-dead form) (By similarity). Interacts with TTC3 (By similarity).
CC {ECO:0000250|UniProtKB:O14578, ECO:0000250|UniProtKB:P49025}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49025}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=E9PSL7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=E9PSL7-2; Sequence=VSP_060430, VSP_060431, VSP_060432,
CC VSP_060433;
CC Name=3;
CC IsoId=E9PSL7-3; Sequence=VSP_060432, VSP_060433;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AF039218; AAC25483.1; -; mRNA.
DR EMBL; AABR07036527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07036528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07036529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07036530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07036531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001025082.1; NM_001029911.1. [E9PSL7-1]
DR RefSeq; XP_006249534.1; XM_006249472.3. [E9PSL7-1]
DR AlphaFoldDB; E9PSL7; -.
DR SMR; E9PSL7; -.
DR IntAct; E9PSL7; 5.
DR MINT; E9PSL7; -.
DR STRING; 10116.ENSRNOP00000053869; -.
DR jPOST; E9PSL7; -.
DR PaxDb; E9PSL7; -.
DR Ensembl; ENSRNOT00000086716; ENSRNOP00000069808; ENSRNOG00000001143. [E9PSL7-3]
DR GeneID; 83620; -.
DR KEGG; rno:83620; -.
DR CTD; 11113; -.
DR RGD; 70878; Cit.
DR VEuPathDB; HostDB:ENSRNOG00000001143; -.
DR eggNOG; KOG0612; Eukaryota.
DR eggNOG; KOG0976; Eukaryota.
DR GeneTree; ENSGT01030000234517; -.
DR HOGENOM; CLU_000288_140_2_1; -.
DR InParanoid; E9PSL7; -.
DR OMA; SQDTHRR; -.
DR OrthoDB; 759391at2759; -.
DR Reactome; R-RNO-5625900; RHO GTPases activate CIT.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR PRO; PR:E9PSL7; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001143; Expressed in frontal cortex and 17 other tissues.
DR ExpressionAtlas; E9PSL7; baseline and differential.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:RGD.
DR GO; GO:0032154; C:cleavage furrow; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0031985; C:Golgi cisterna; IDA:RGD.
DR GO; GO:0030496; C:midbody; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0001726; C:ruffle; ISO:RGD.
DR GO; GO:0005773; C:vacuole; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; ISO:RGD.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:RGD.
DR GO; GO:0016358; P:dendrite development; ISO:RGD.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IMP:RGD.
DR GO; GO:0048699; P:generation of neurons; ISO:RGD.
DR GO; GO:0007030; P:Golgi organization; IMP:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0007091; P:metaphase/anaphase transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:0000278; P:mitotic cell cycle; ISO:RGD.
DR GO; GO:0000281; P:mitotic cytokinesis; ISO:RGD.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; ISO:RGD.
DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; ISO:RGD.
DR GO; GO:0035331; P:negative regulation of hippo signaling; ISO:RGD.
DR GO; GO:0051402; P:neuron apoptotic process; ISO:RGD.
DR GO; GO:0032467; P:positive regulation of cytokinesis; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR GO; GO:0008064; P:regulation of actin polymerization or depolymerization; IDA:RGD.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR CDD; cd00029; C1; 1.
DR CDD; cd05601; STKc_CRIK; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR017405; Citron_Rho-interacting_kinase.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR037708; CRIK_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
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 PANTHER; PTHR22988:SF26; PTHR22988:SF26; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF038145; Citron_Rho-interacting_kinase; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coiled coil; Cytoplasm; Kinase;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..2055
FT /note="Citron rho-interacting kinase"
FT /id="PRO_0000448698"
FT DOMAIN 97..359
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 360..430
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 1469..1589
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1617..1907
FT /note="CNH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT ZN_FING 1388..1437
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 375..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1349..1376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1932..2040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 457..747
FT /evidence="ECO:0000255"
FT COILED 773..1238
FT /evidence="ECO:0000255"
FT COILED 1284..1318
FT /evidence="ECO:0000255"
FT COMPBIAS 1934..1953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1977..2027
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 221
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 103..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT VAR_SEQ 1..466
FT /note="Missing (in isoform 2)"
FT /id="VSP_060430"
FT VAR_SEQ 1279
FT /note="K -> KGLFSRRKEDPALPTQ (in isoform 2)"
FT /id="VSP_060431"
FT VAR_SEQ 1602
FT /note="A -> AAWDCTSCERLPVWVE (in isoform 2 and isoform 3)"
FT /id="VSP_060432"
FT VAR_SEQ 1945
FT /note="Missing (in isoform 2 and isoform 3)"
FT /id="VSP_060433"
SQ SEQUENCE 2055 AA; 235310 MW; 237329B7CF7C0596 CRC64;
MLKFKYGVRN PSEASAPEPI ASRASRLNLF FQGKPPLMTQ QQMSALSREG VLDALFVLLE
ECSQPALMKI KHVSSFVRKY SDTIAELREL QPSVRDFEVR SLVGCGHFAE VQVVREKATG
DVYAMKIMKK AALRAQEQVS FFEEERNILS QSTSPWIPQL QYAFQDKNNL YLVMEYQPGG
DLLSLLNRYE DQLDENMIQF YLAELILAVH SVHQMGYVHR DIKPENILID RTGHIKLVDF
GSAAKMNSNK VDAKLPIGTP DYMAPEVLTV MNEDRRGTYG LDCDWWSVGV VAYEMLYGKT
PFTEGTSART FNNIMNFQRF LKFPDDPKVS SELLDLIQSL LCVQKERLKF EGLCCHPFFA
RTDWNNIRNS PPPFVPTLKS DDDTSNFDEP EKNSWVSSSP CQLSPSGFSG EELPFVGFSY
SKALGYLGRS ESVVSGLDSP AKISSMEKKL LIKSKELQDS QDKCHKMEQE MARLHRRVSE
VEAVLSQKEV ELKASETQRS LLEQDLATYI TECSSLKRSL EQARMEVSQE DDKALQLLHD
IREQSRKLQE IKEQEYQAQV EEMRLMMNQL EEDLVSARRR SDLYESELRE SRLAAEEFKR
KANECQHKLM KAKDLGKPEV GECSRLEKIN AEQQLKIQEL QEKLEKAVKA STEATELLQN
IRQAKERAER ELEKLHNRED SSEGIKKKLV EAEERRHSLE NKVKRLETME RRENRLKDDI
QTKSEQIQQM ADKILELEEK HREAQVSAQH LEVHLKQKEQ HYEEKIKVLD NQIKKDLADK
ESLETMMQRH EEEAHEKGKI LSEQKAMINA MDSKIRSLEQ RIVELSEANK LAANSSLFTQ
RNMKAQEEMI SELRQQKFYL ETQAGKLEAQ NRKLEEQLEK ISHQDHSDKN RLLELETRLR
EVSLEHEEQK LELKRQLTEL QLSLQERESQ LTALQAARAA LESQLRQAKT ELEETTAEAE
EEIQALTAHR DEIQRKFDAL RNSCTVITDL EEQLNQLTED NAELNNQNFY LSKQLDEASG
ANDEIVQLRS EVDHLRREIT EREMQLTSQK QTMEALKTTC TMLEEQVMDL EALNDELLEK
ERQWEAWRSV LGDEKSQFEC RVRELQRMLD TEKQSRARAD QRITESRQVV ELAVKEHKAE
ILALQQALKE QKLKAESLSD KLNDLEKKHA MLEMNARSLQ QKLETERELK QRLLEEQAKL
QQQMDLQKNH IFRLTQGLQE ALDRADLLKT ERSDLEYQLE NIQVLYSHEK VKMEGTISQQ
TKLIDFLQAK MDQPAKKKKV PLQYNELKLA LEKEKARCAE LEEALQKTRI ELRSAREEAA
HRKATDHPHP STPATARQQI AMSAIVRSPE HQPSAMSLLA PPSSRRKEAS TPEEFSRRLK
ERMHHNIPHR FNVGLNMRAT KCAVCLDTVH FGRQASKCLE CQVMCHPKCS TCLPATCGLP
AEYATHFTEA FCRDKVSSPG LQSKEPSSSL HLEGWMKVPR NNKRGQQGWD RKYIVLEGSK
VLIYDNEARE AGQRPVEEFE LCLPDGDVSI HGAVGASELA NTAKADVPYI LKMESHPHTT
CWPGRTLYLL APSFPDKQRW VTALESVVAG GRVSREKAEA DAKLLGNSLL KLEGDDRLDM
NCTLPFSDQV VLVGTEEGLY ALNVLKNSLT HIPGIGAVFQ IYIIKDLEKL LMIAGEERAL
CLVDVKKVKQ SLAQSHLPAQ PDVSPNIFEA VKGCHLFAAG KIENSLCICA AMPSKVVILR
YNDNLSKFCI RKEIETSEPC SCIHFTNYSI LIGTNKFYEI DMKQYTLEEF LDKNDHSLAP
AVFASSTNSF PVSIVQANST GQREEYLLCF HEFGVFVDSY GRRSRTDDLK WSRLPLAFAY
REPYLFVTHF NSLEVIEIQA RSSLGTPARA YLEIPNPRYL GPAISSGAIY LASSYQDKLR
VICCKGNLVK ESGTEQHRVP STSRSSPNKR GPPTYNEHIT KRVASSPAPP EGPSHPREPS
TPHRYRDREG RTELRRDKSP GRPLEREKSP GRMLSTRRER SPGRLFEDSS RGRLPAGAVR
TPLSQVNKVW DQSSV
