MILK2_MOUSE
ID MILK2_MOUSE Reviewed; 1009 AA.
AC Q3TN34; Q3TPY3; Q3UB65;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=MICAL-like protein 2;
DE AltName: Full=Junctional Rab13-binding protein;
DE AltName: Full=Molecule interacting with CasL-like 2;
DE Short=MICAL-L2;
GN Name=Micall2; Synonyms=Jrab;
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], FUNCTION IN TIGHT JUNCTION ASSEMBLY,
RP INTERACTION WITH RAB13, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=16525024; DOI=10.1091/mbc.e05-09-0826;
RA Terai T., Nishimura N., Kanda I., Yasui N., Sasaki T.;
RT "JRAB/MICAL-L2 is a junctional Rab13-binding protein mediating the
RT endocytic recycling of occludin.";
RL Mol. Biol. Cell 17:2465-2475(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ; TISSUE=B-cell, Bone marrow, and Embryo;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION IN ENDOCYTIC RECYCLING, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP RAB8A; RAB8B AND RAB13.
RX PubMed=18094055; DOI=10.1091/mbc.e07-06-0551;
RA Yamamura R., Nishimura N., Nakatsuji H., Arase S., Sasaki T.;
RT "The interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates the
RT assembly of tight junctions and adherens junctions.";
RL Mol. Biol. Cell 19:971-983(2008).
RN [6]
RP INTERACTION WITH ACTN4, AND SUBCELLULAR LOCATION.
RX PubMed=18332111; DOI=10.1128/mcb.00144-08;
RA Nakatsuji H., Nishimura N., Yamamura R., Kanayama H.O., Sasaki T.;
RT "Involvement of actinin-4 in the recruitment of JRAB/MICAL-L2 to cell-cell
RT junctions and the formation of functional tight junctions.";
RL Mol. Cell. Biol. 28:3324-3335(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-832, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-766, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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 [9]
RP FUNCTION IN NEURITE OUTGROWTH, INTERACTION WITH RAB13, SUBCELLULAR
RP LOCATION, AND DOMAIN.
RX PubMed=20008558; DOI=10.1128/mcb.01067-09;
RA Sakane A., Honda K., Sasaki T.;
RT "Rab13 regulates neurite outgrowth in PC12 cells through its effector
RT protein, JRAB/MICAL-L2.";
RL Mol. Cell. Biol. 30:1077-1087(2010).
RN [10]
RP FUNCTION IN CYTOSKELETON ORGANIZATION, INTERACTION WITH ACTN1 AND ACTN4,
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=23100251; DOI=10.1074/jbc.m112.383653;
RA Sakane A., Abdallah A.A., Nakano K., Honda K., Ikeda W., Nishikawa Y.,
RA Matsumoto M., Matsushita N., Kitamura T., Sasaki T.;
RT "Rab13 small G protein and junctional Rab13-binding protein (JRAB)
RT orchestrate actin cytoskeletal organization during epithelial junctional
RT development.";
RL J. Biol. Chem. 287:42455-42468(2012).
RN [11]
RP FUNCTION IN CYTOSKELETON ORGANIZATION, SUBCELLULAR LOCATION, INTERACTION
RP WITH ACTN1; ACTN4; FLNA; FLNB AND FLNC, AND DOMAIN.
RX PubMed=23890175; DOI=10.1111/gtc.12078;
RA Sakane A., Alamir Mahmoud Abdallah A., Nakano K., Honda K., Kitamura T.,
RA Imoto I., Matsushita N., Sasaki T.;
RT "Junctional Rab13-binding protein (JRAB) regulates cell spreading via
RT filamins.";
RL Genes Cells 18:810-822(2013).
CC -!- FUNCTION: Effector of small Rab GTPases which is involved in junctional
CC complexes assembly through the regulation of cell adhesion molecules
CC transport to the plasma membrane and actin cytoskeleton reorganization.
CC Regulates the endocytic recycling of occludins, claudins and E-cadherin
CC to the plasma membrane and may thereby regulate the establishment of
CC tight junctions and adherens junctions. In parallel, may regulate actin
CC cytoskeleton reorganization directly through interaction with F-actin
CC or indirectly through actinins and filamins. Most probably involved in
CC the processes of epithelial cell differentiation, cell spreading and
CC neurite outgrowth. {ECO:0000269|PubMed:16525024,
CC ECO:0000269|PubMed:18094055, ECO:0000269|PubMed:20008558,
CC ECO:0000269|PubMed:23100251, ECO:0000269|PubMed:23890175}.
CC -!- SUBUNIT: Interacts with RAB13 (GTP-bound form); competes with RAB8A and
CC is involved in tight junctions assembly. Interacts with RAB8A; competes
CC with RAB13 and is involved in E-cadherin endocytic recycling. Interacts
CC with RAB8B. Interacts (preferentially in opened conformation) with
CC ACTN1 and ACTN4; stimulated by RAB13 activation. Interacts (via
CC calponin-homology (CH) domain) with the filamins FLNA, FLNB and FLNC
CC (via actin-binding domain). {ECO:0000269|PubMed:16525024,
CC ECO:0000269|PubMed:18094055, ECO:0000269|PubMed:18332111,
CC ECO:0000269|PubMed:20008558, ECO:0000269|PubMed:23100251,
CC ECO:0000269|PubMed:23890175}.
CC -!- INTERACTION:
CC Q3TN34; P57780: Actn4; NbExp=9; IntAct=EBI-1779852, EBI-445071;
CC Q3TN34; P51153: RAB13; Xeno; NbExp=8; IntAct=EBI-1779852, EBI-1780121;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cell
CC junction, tight junction. Recycling endosome. Cell projection
CC {ECO:0000250}. Cytoplasm, cytoskeleton. Cytoplasm, cytosol.
CC -!- TISSUE SPECIFICITY: Detected in brain, lung, liver and kidney (at
CC protein level). {ECO:0000269|PubMed:16525024}.
CC -!- DOMAIN: Probably exists in a closed and an open conformation due to
CC interaction of the C-terminal coiled-coil domain with an N-terminal
CC region including the calponin-homology (CH) and the LIM zinc-binding
CC domain. The conformational change is regulated by RAB13.
CC {ECO:0000269|PubMed:20008558, ECO:0000269|PubMed:23100251,
CC ECO:0000269|PubMed:23890175}.
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DR EMBL; AB182579; BAE86912.1; -; mRNA.
DR EMBL; AK151086; BAE30099.1; -; mRNA.
DR EMBL; AK164043; BAE37602.1; -; mRNA.
DR EMBL; AK165558; BAE38255.1; -; mRNA.
DR EMBL; AC167333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466529; EDL19139.1; -; Genomic_DNA.
DR CCDS; CCDS39353.2; -.
DR RefSeq; NP_777275.2; NM_174850.3.
DR AlphaFoldDB; Q3TN34; -.
DR SMR; Q3TN34; -.
DR BioGRID; 231173; 5.
DR IntAct; Q3TN34; 3.
DR STRING; 10090.ENSMUSP00000039707; -.
DR iPTMnet; Q3TN34; -.
DR PhosphoSitePlus; Q3TN34; -.
DR jPOST; Q3TN34; -.
DR MaxQB; Q3TN34; -.
DR PaxDb; Q3TN34; -.
DR PeptideAtlas; Q3TN34; -.
DR PRIDE; Q3TN34; -.
DR ProteomicsDB; 295669; -.
DR Antibodypedia; 24191; 84 antibodies from 20 providers.
DR DNASU; 231830; -.
DR Ensembl; ENSMUST00000044642; ENSMUSP00000039707; ENSMUSG00000036718.
DR GeneID; 231830; -.
DR KEGG; mmu:231830; -.
DR UCSC; uc009agx.2; mouse.
DR CTD; 79778; -.
DR MGI; MGI:2444818; Micall2.
DR VEuPathDB; HostDB:ENSMUSG00000036718; -.
DR eggNOG; ENOG502QVVF; Eukaryota.
DR GeneTree; ENSGT00940000160222; -.
DR HOGENOM; CLU_015382_0_0_1; -.
DR InParanoid; Q3TN34; -.
DR OMA; SELMYKM; -.
DR OrthoDB; 377701at2759; -.
DR PhylomeDB; Q3TN34; -.
DR TreeFam; TF328311; -.
DR BioGRID-ORCS; 231830; 0 hits in 73 CRISPR screens.
DR PRO; PR:Q3TN34; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q3TN34; protein.
DR Bgee; ENSMUSG00000036718; Expressed in ectoplacental cone and 152 other tissues.
DR ExpressionAtlas; Q3TN34; baseline and differential.
DR Genevisible; Q3TN34; MM.
DR GO; GO:0032432; C:actin filament bundle; IDA:MGI.
DR GO; GO:0005923; C:bicellular tight junction; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0042805; F:actinin binding; IPI:UniProtKB.
DR GO; GO:0031005; F:filamin binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; IMP:UniProtKB.
DR GO; GO:0070830; P:bicellular tight junction assembly; IMP:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IDA:MGI.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR022735; bMERB_dom.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR028563; MICAL-L.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR23167:SF53; PTHR23167:SF53; 2.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF12130; DUF3585; 1.
DR Pfam; PF00412; LIM; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00132; LIM; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS51848; BMERB; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Endosome; LIM domain; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Tight junction; Zinc.
FT CHAIN 1..1009
FT /note="MICAL-like protein 2"
FT /id="PRO_0000424227"
FT DOMAIN 1..107
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 186..248
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 833..980
FT /note="bMERB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01195"
FT REGION 1..260
FT /note="Forms an intramolecular interaction with the C-
FT terminal coiled coil domain keeping the protein in a closed
FT conformation"
FT REGION 114..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..805
FT /note="Mediates targeting to the cell plasma membrane"
FT REGION 261..393
FT /note="Necessary and sufficient for interaction with
FT actinins"
FT REGION 348..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..913
FT /note="Forms an intramolecular interaction with the N-
FT terminal Calponin-homology and LIM zinc-binding domains-
FT containing region keeping the protein in a closed
FT conformation"
FT REGION 913..1009
FT /note="Mediates interaction with RAB13 and is required for
FT transition from the closed to the open conformation"
FT COILED 841..880
FT /evidence="ECO:0000255"
FT COMPBIAS 140..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY33"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY33"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY33"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY33"
FT MOD_RES 766
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 768
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IY33"
FT MOD_RES 832
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CONFLICT 770
FT /note="S -> L (in Ref. 2; BAE37602)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1009 AA; 108288 MW; 3D059CD22B8BAF53 CRC64;
MAAIKALQEW CRQQCEGYRD VSITNMTTSF RDGLAFCAIL HRHRPDLINF SALRKENIYE
NNKLAFQVAE EQLGIPALLD AEDMVALKVP DRLSILTYVS QYYNYFHGRS PIGGMAGIKR
PSSDSTEELS GKKGLSQPAK LPSPAQTQRS PLSPARTNPV VQRNEGGSQR PSPKAAPGTA
GSSVSSICGV CGKHVHLVQR HLADGRLYHR SCFRCKQCSS TLHSGAYRAT GEPGVFVCTH
HSSEVTSVSP KSSNLASRKP GGVTADTRPF GVSWTVQEAN GEGTPLRVRT AAWEHAGGNT
TAKGFVQTEL KPPSTSQVHV GSSAGPKLPT ITVTTTSVTS KALTHVTNSS PIGWSSPAQS
SPANFNSRPV VSPSARNTHL PGSQGQTASK GVKTQLNLNS ESSNTAVTPA WTSSASKTQQ
AREKFFQTPP SAPAPASAPA PAPTSKVPTV VTVPTSKVPN VVTAPTSKVP TVVTVPTSKV
PTVVSAPTSK VPTVVSAPTS KVPTVVNSTN SRVTTVVNAP TSKVPTVVSA TNGRVPTVVT
AHTGRVPAVM NTSASKVSPV VDAPAQESSR EQALSVLRKA LPALTGSGTQ APNRSFPATS
SVLVTLPKNE VPQKVPSDKL SALTTQTPNF TIKLEPSAPV NVGNTAVFLQ AGKKSPSISP
RVGKTSVGSR PQAEVAGVKG PGPISQEGQE EGPEGWRARL KPVDKKTPAG RSLEQKEPVL
AEPRIGDTSR KASSSSDSSV HITLTSIQHK RKPCPAGSGP SPAALSPSPS HRKKLAVPPS
LDVSADWLQP EPKKQEDGTR SCKEEKSPTR WSRERSAVLD SGLAPPGEAV TSPVRLHPDY
IPQEELQRQL QDIESQLDAL ELRGVELEKR LRAAEGDASE DSLMVDWFRL IHEKQLLLRL
ESELMYKSKD QRLEEQQLDL QGELRRLMDK PEGLKSPQDR QREQELLSQY VNTVNDRSDI
VDFLDEDRLR EQEEDQMLEN MIQNLGLQRK KSKSFLSKIW SSKSKSGQA
