KRIT1_MOUSE
ID KRIT1_MOUSE Reviewed; 736 AA.
AC Q6S5J6; Q6VSV2; Q7TPR8; Q8C9Q6; Q9EPY2; Q9ERH0;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Krev interaction trapped protein 1;
DE Short=Krev interaction trapped 1;
DE AltName: Full=Cerebral cavernous malformations 1 protein homolog;
GN Name=Krit1; Synonyms=Ccm1;
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 [MRNA] (ISOFORM 1).
RC STRAIN=MALK/c;
RX PubMed=11161791; DOI=10.1006/geno.2000.6410;
RA Zhang J., Clatterbuck R.E., Rigamonti D., Dietz H.C.;
RT "Cloning of the murine Krit1 cDNA reveals novel mammalian 5' coding
RT exons.";
RL Genomics 70:392-395(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12172908; DOI=10.1007/s00401-002-0552-6;
RA Kehrer-Sawatzki H., Wilda M., Braun V.M., Richter H.-P., Hameister H.;
RT "Mutation and expression analysis of the KRIT1 gene associated with
RT cerebral cavernous malformations (CCM1).";
RL Acta Neuropathol. 104:231-240(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, AND
RP TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=14697511; DOI=10.1016/j.gene.2003.09.046;
RA Retta S.F., Avolio M., Francalanci F., Procida S., Balzac F., Degani S.,
RA Tarone G., Silengo L.;
RT "Identification of Krit1B: a novel alternative splicing isoform of cerebral
RT cavernous malformation gene-1.";
RL Gene 325:63-78(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Olfactory epithelium;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 517-736 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP INTERACTION WITH HEG1 AND CCM2.
RX PubMed=19151727; DOI=10.1038/nm.1918;
RA Kleaveland B., Zheng X., Liu J.J., Blum Y., Tung J.J., Zou Z.,
RA Sweeney S.M., Chen M., Guo L., Lu M.M., Zhou D., Kitajewski J.,
RA Affolter M., Ginsberg M.H., Kahn M.L.;
RT "Regulation of cardiovascular development and integrity by the heart of
RT glass-cerebral cavernous malformation protein pathway.";
RL Nat. Med. 15:169-176(2009).
RN [7]
RP FUNCTION.
RX PubMed=20332120; DOI=10.1242/jcs.059329;
RA Lampugnani M.G., Orsenigo F., Rudini N., Maddaluno L., Boulday G.,
RA Chapon F., Dejana E.;
RT "CCM1 regulates vascular-lumen organization by inducing endothelial
RT polarity.";
RL J. Cell Sci. 123:1073-1080(2010).
RN [8]
RP FUNCTION.
RX PubMed=20668652; DOI=10.1371/journal.pone.0011786;
RA Goitre L., Balzac F., Degani S., Degan P., Marchi S., Pinton P.,
RA Retta S.F.;
RT "KRIT1 regulates the homeostasis of intracellular reactive oxygen
RT species.";
RL PLoS ONE 5:E11786-E11786(2010).
RN [9]
RP FUNCTION.
RX PubMed=20616044; DOI=10.1073/pnas.1000132107;
RA Wuestehube J., Bartol A., Liebler S.S., Bruetsch R., Zhu Y., Felbor U.,
RA Sure U., Augustin H.G., Fischer A.;
RT "Cerebral cavernous malformation protein CCM1 inhibits sprouting
RT angiogenesis by activating DELTA-NOTCH signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:12640-12645(2010).
RN [10]
RP FUNCTION.
RX PubMed=26417067; DOI=10.15252/emmm.201505316;
RA Marchi S., Corricelli M., Trapani E., Bravi L., Pittaro A.,
RA Delle Monache S., Ferroni L., Patergnani S., Missiroli S., Goitre L.,
RA Trabalzini L., Rimessi A., Giorgi C., Zavan B., Cassoni P., Dejana E.,
RA Retta S.F., Pinton P.;
RT "Defective autophagy is a key feature of cerebral cavernous
RT malformations.";
RL EMBO Mol. Med. 7:1403-1417(2015).
CC -!- FUNCTION: Component of the CCM signaling pathway which is a crucial
CC regulator of heart and vessel formation and integrity. Negative
CC regulator of angiogenesis. Inhibits endothelial proliferation,
CC apoptosis, migration, lumen formation and sprouting angiogenesis in
CC primary endothelial cells. Promotes AKT phosphorylation in a NOTCH-
CC dependent and independent manner, and inhibits ERK1/2 phosphorylation
CC indirectly through activation of the DELTA-NOTCH cascade. Acts in
CC concert with CDH5 to establish and maintain correct endothelial cell
CC polarity and vascular lumen and these effects are mediated by
CC recruitment and activation of the Par polarity complex and RAP1B.
CC Required for the localization of phosphorylated PRKCZ, PARD3, TIAM1 and
CC RAP1B to the cell junction, and cell junction stabilization. Plays a
CC role in integrin signaling via its interaction with ITGB1BP1; this
CC prevents the interaction between ITGB1 and ITGB1BP1. Microtubule-
CC associated protein that binds to phosphatidylinositol 4,5-bisphosphate
CC (PIP2)-containing membranes in a GTP-bound RAP1-dependent manner (By
CC similarity). Plays an important role in the maintenance of the
CC intracellular reactive oxygen species (ROS) homeostasis to prevent
CC oxidative cellular damage. Regulates the homeostasis of intracellular
CC ROS through an antioxidant pathway involving FOXO1 and SOD2.
CC Facilitates the down-regulation of cyclin-D1 (CCND1) levels required
CC for cell transition from proliferative growth to quiescence by
CC preventing the accumulation of intracellular ROS through the modulation
CC of FOXO1 and SOD2 levels. May play a role in the regulation of
CC macroautophagy through the down-regulation of the mTOR pathway
CC (PubMed:26417067). {ECO:0000250|UniProtKB:O00522,
CC ECO:0000269|PubMed:20332120, ECO:0000269|PubMed:20616044,
CC ECO:0000269|PubMed:20668652, ECO:0000269|PubMed:26417067}.
CC -!- SUBUNIT: Found in a complex, at least composed of ITGB1BP1, KRIT1 and
CC RAP1A. Interacts (via C-terminus FERM domain) with RAP1A (active GTP-
CC bound form preferentially); the interaction does not induce the opening
CC conformation of KRIT1. Interacts (via N-terminus NPXY motif) with
CC ITGB1BP1; the interaction induces the opening conformation of KRIT1 and
CC competes with ITGB1 for ITGB1BP1 interaction. Associates (via N-
CC terminus and C-terminus regions) with microtubules; the interaction is
CC inhibited in presence of ITGB1BP1 and active GTP-bound RAP1A. Interacts
CC (via FERM domain) with RAP1B. Interacts with CDH5. Interacts with RAP1A
CC (By similarity). Interacts with HEG1 and CCM2; greatly facilitates
CC CCM2-binding to HEG1 (PubMed:19151727). {ECO:0000250|UniProtKB:O00522,
CC ECO:0000269|PubMed:19151727}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell
CC junction {ECO:0000250}. Note=KRIT1 and CDH5 reciprocally regulate their
CC localization to endothelial cell-cell junctions. Association with RAP1
CC relocalizes KRIT1 from microtubules to cell junction membranes.
CC Translocates from the cytoplasm along microtubules to the cell membrane
CC in an ITGB1BP1-dependent manner (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Krit1A;
CC IsoId=Q6S5J6-1; Sequence=Displayed;
CC Name=2; Synonyms=Krit1B;
CC IsoId=Q6S5J6-2; Sequence=VSP_015803;
CC Name=3;
CC IsoId=Q6S5J6-3; Sequence=VSP_015801;
CC Name=4;
CC IsoId=Q6S5J6-4; Sequence=VSP_015802;
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung, thymus,
CC kidney and testis. Isoform 2 was more frequently expressed in the
CC thymus than isoform 1. {ECO:0000269|PubMed:12172908,
CC ECO:0000269|PubMed:14697511}.
CC -!- DEVELOPMENTAL STAGE: At stage 9.5 dpc ubiquitously expressed, at 12.5
CC dpc expressed in structures of the CNS, especially in zones of the
CC proliferative active ventricular zones of the brain and in the spinal
CC cord. Expression increased in organs that were in the state of organ
CC expansion like lung and liver. At 17.5 dpc, expression was strongly
CC reduced in endoderm-derived tissues. In early postnatal development,
CC strongly expressed in regions of ossification.
CC {ECO:0000269|PubMed:12172908}.
CC -!- DOMAIN: The FERM domain mediates binding to RAP1A and RAP1B and is
CC necessary for binding to phosphatidylinositol 4,5-bisphosphate (PIP2).
CC {ECO:0000250|UniProtKB:O00522}.
CC -!- DOMAIN: The N-terminal domain has structural similarity to the nudix
CC hydrolase domain, despite the absence of a nudix box and low sequence
CC similarity with nudix hydrolase domains. The N-terminus and the C-
CC terminus part associate together via the NPAY binding motif and adopt a
CC lose conformation that is disrupted by ITGB1BP1, but not by RAP1A.
CC {ECO:0000250|UniProtKB:O00522}.
CC -!- DOMAIN: Contains 4 ANK repeats that precede the FERM domain.
CC {ECO:0000250|UniProtKB:O00522}.
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DR EMBL; AF310134; AAG47775.1; -; mRNA.
DR EMBL; AF306509; AAG18456.1; -; mRNA.
DR EMBL; AY328895; AAQ92980.1; -; mRNA.
DR EMBL; AY464945; AAR24089.1; -; mRNA.
DR EMBL; BC054819; AAH54819.1; -; mRNA.
DR EMBL; AK041574; BAC30991.1; -; mRNA.
DR CCDS; CCDS39002.1; -. [Q6S5J6-1]
DR CCDS; CCDS51409.1; -. [Q6S5J6-2]
DR RefSeq; NP_001164023.1; NM_001170552.1. [Q6S5J6-2]
DR RefSeq; NP_109600.2; NM_030675.3. [Q6S5J6-1]
DR RefSeq; XP_006503680.1; XM_006503617.3. [Q6S5J6-1]
DR RefSeq; XP_006503681.1; XM_006503618.3. [Q6S5J6-1]
DR AlphaFoldDB; Q6S5J6; -.
DR SMR; Q6S5J6; -.
DR BioGRID; 219753; 2.
DR ComplexPortal; CPX-4621; CCM complex.
DR CORUM; Q6S5J6; -.
DR IntAct; Q6S5J6; 1.
DR MINT; Q6S5J6; -.
DR STRING; 10090.ENSMUSP00000078985; -.
DR iPTMnet; Q6S5J6; -.
DR PhosphoSitePlus; Q6S5J6; -.
DR EPD; Q6S5J6; -.
DR jPOST; Q6S5J6; -.
DR MaxQB; Q6S5J6; -.
DR PaxDb; Q6S5J6; -.
DR PRIDE; Q6S5J6; -.
DR ProteomicsDB; 264866; -. [Q6S5J6-1]
DR ProteomicsDB; 264867; -. [Q6S5J6-2]
DR ProteomicsDB; 264868; -. [Q6S5J6-3]
DR ProteomicsDB; 264869; -. [Q6S5J6-4]
DR DNASU; 79264; -.
DR Ensembl; ENSMUST00000080085; ENSMUSP00000078985; ENSMUSG00000000600. [Q6S5J6-1]
DR Ensembl; ENSMUST00000171023; ENSMUSP00000132375; ENSMUSG00000000600. [Q6S5J6-2]
DR Ensembl; ENSMUST00000200577; ENSMUSP00000143776; ENSMUSG00000000600. [Q6S5J6-4]
DR GeneID; 79264; -.
DR KEGG; mmu:79264; -.
DR UCSC; uc008whs.2; mouse. [Q6S5J6-1]
DR UCSC; uc008whv.2; mouse. [Q6S5J6-2]
DR CTD; 889; -.
DR MGI; MGI:1930618; Krit1.
DR VEuPathDB; HostDB:ENSMUSG00000000600; -.
DR eggNOG; KOG4335; Eukaryota.
DR GeneTree; ENSGT00530000063721; -.
DR HOGENOM; CLU_022188_0_0_1; -.
DR InParanoid; Q6S5J6; -.
DR OMA; FAIWIAS; -.
DR PhylomeDB; Q6S5J6; -.
DR TreeFam; TF317921; -.
DR BioGRID-ORCS; 79264; 7 hits in 74 CRISPR screens.
DR ChiTaRS; Krit1; mouse.
DR PRO; PR:Q6S5J6; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6S5J6; protein.
DR Bgee; ENSMUSG00000000600; Expressed in rostral migratory stream and 308 other tissues.
DR ExpressionAtlas; Q6S5J6; baseline and differential.
DR Genevisible; Q6S5J6; MM.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0030695; F:GTPase regulator activity; TAS:MGI.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0045454; P:cell redox homeostasis; IMP:UniProtKB.
DR GO; GO:0003158; P:endothelium development; IC:ComplexPortal.
DR GO; GO:0033622; P:integrin activation; ISO:MGI.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IMP:UniProtKB.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0032092; P:positive regulation of protein binding; IDA:MGI.
DR GO; GO:0045765; P:regulation of angiogenesis; IC:ComplexPortal.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13197; FERM_C_CCM1; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.70.2240; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR041791; KRIT1_FERM_C.
DR InterPro; IPR032022; NUDIX.
DR InterPro; IPR043058; NUDIX_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF16705; NUDIX_5; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM00295; B41; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50057; FERM_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Angiogenesis; ANK repeat; Cell junction;
KW Cell membrane; Cytoplasm; Cytoskeleton; Membrane; Reference proteome;
KW Repeat.
FT CHAIN 1..736
FT /note="Krev interaction trapped protein 1"
FT /id="PRO_0000067024"
FT REPEAT 287..316
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 320..350
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 354..384
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 388..419
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT DOMAIN 420..736
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 1..170
FT /note="N-terminal domain similar to Nudix hydrolase domain"
FT /evidence="ECO:0000250"
FT REGION 172..195
FT /note="Interaction with ITGB1BP1"
FT /evidence="ECO:0000250"
FT REGION 430..452
FT /note="Interaction with RAP1B"
FT /evidence="ECO:0000250"
FT VAR_SEQ 295..300
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12172908"
FT /id="VSP_015801"
FT VAR_SEQ 330..736
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_015802"
FT VAR_SEQ 676..714
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14697511,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_015803"
FT CONFLICT 47
FT /note="K -> E (in Ref. 2; AAG18456)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="N -> D (in Ref. 2; AAG18456)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="P -> R (in Ref. 1; AAG47775)"
FT /evidence="ECO:0000305"
FT CONFLICT 550..552
FT /note="KLI -> RLD (in Ref. 1; AAG47775)"
FT /evidence="ECO:0000305"
FT CONFLICT 665
FT /note="K -> R (in Ref. 1; AAG47775)"
FT /evidence="ECO:0000305"
FT CONFLICT 684..689
FT /note="CCFTWQ -> WLLTWA (in Ref. 1; AAG47775)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 736 AA; 83982 MW; 441333F62A1D208A CRC64;
MGNPENIEDA YVAVIRPKNT ASLNSREYRA KSYEILLHEV PIEGQKKKRK KVLLETKLQS
NSEIAQGILD YVVETTKPIS PANQGIKGKR VVLMRKFPLD GEKTGREAAL FIVPSVVKDN
TKYAYTPGCP IFYCLQDIMR VCSESSTHFA TLTARMLIAL DKWLDERHAQ SHFIPALFRP
SPLERIKTNV INPAYAAELG QVDNSLHMGY SALEIKSKML ALEKADTCIY NPLFGSDLQY
TNRVDKVVIN PYFGLGAPDY SKIQIPKQEK WQRSMSSVVE DKERQWVDDF PLHRNACEGD
SELLSHLLDK GLSVNQLDND HWAPIHYACW YGKVEATRIL LEKGKCNPNL LNGQLSSPLH
FAAGGGHAEI VQILLTHPDI DRHITDQQGR SPLNVCEENK QNNWEEAAKL LKDAINKPYE
KVRIYRMDGS YRSVELKHGN NTTAQQIMEG MRLSQETQRY FTIWICSENL SLQFKPYHKP
LQQVHDWPEI LAELTNLDPQ RETPQLFLRR DVGLPLEVEK KIEDPLAILI LFDEARYNLL
KGFYTAPDAK LITLASLLLQ IVYGNYESKK HKQGFLNEET LKSIVPITKL KSKAPHWINR
ILHEYKNLSL SEGVSKEMHH LQRMFLQNCW EIPTYGAAFF TGQIFTKASP SNHKVIPVYV
GVNIKGLHLL NMETKALLIS LKYCCFTWQL GDAGTCFQIH SMENKMSFIV HTKQAGLVVK
LLMKLNGQLM PSERNS
