ABLM2_MOUSE
ID ABLM2_MOUSE Reviewed; 612 AA.
AC Q8BL65; B2RUF8; Q6H8P8; Q80WK6; Q8BUT1; Q8BXI7;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Actin-binding LIM protein 2;
DE Short=abLIM-2;
DE AltName: Full=Actin-binding LIM protein family member 2;
GN Name=Ablim2;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Klimov E.A., Rakhmanaliev E.R., Rudco O.I.;
RT "Structure and transcriptional activity of the ABLIM2 gene of human, mouse
RT and rat.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J;
RA Xu Z.-P., Piatigorsky J.;
RT "Identification of a novel actin-binding LIM protein (abLIM2) in developing
RT cornea.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5).
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Corpora quadrigemina, and Medulla oblongata;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Embryo;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH F-ACTIN AND
RP ABRA.
RX PubMed=17194709; DOI=10.1074/jbc.m607549200;
RA Barrientos T., Frank D., Kuwahara K., Bezprozvannaya S., Pipes G.C.T.,
RA Bassel-Duby R., Richardson J.A., Katus H.A., Olson E.N., Frey N.;
RT "Two novel members of the ABLIM protein family, ABLIM-2 and -3, associate
RT with STARS and directly bind F-actin.";
RL J. Biol. Chem. 282:8393-8403(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-294; SER-368 AND THR-473,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351 AND SER-356 (ISOFORM 4),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, and Pancreas;
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).
CC -!- FUNCTION: May act as scaffold protein. May stimulate ABRA activity and
CC ABRA-dependent SRF transcriptional activity.
CC -!- SUBUNIT: Interacts with F-actin and ABRA.
CC {ECO:0000269|PubMed:17194709}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17194709}. Note=In
CC skeletal muscle, sarcomeric or cosarcomeric localization.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8BL65-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BL65-2; Sequence=VSP_012122;
CC Name=3;
CC IsoId=Q8BL65-3; Sequence=VSP_012121, VSP_012122;
CC Name=4;
CC IsoId=Q8BL65-4; Sequence=VSP_012120, VSP_012121, VSP_012122;
CC Name=5;
CC IsoId=Q8BL65-5; Sequence=VSP_012121, VSP_012123, VSP_012124;
CC -!- TISSUE SPECIFICITY: Expressed in brain. Highly expressed in
CC caudate/putamen, moderately expressed in the olfactory bulb. In the
CC hippocampus, expressed in the CA1, CA2 and CA3 fields. In the
CC cerebellum, expressed in Purkinje cells. {ECO:0000269|PubMed:17194709}.
CC -!- DEVELOPMENTAL STAGE: At 15.5 dpc, predominantly expressed in skeletal
CC muscle tissue, including diaphragm, and to a lesser extent in the
CC central nervous system.
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DR EMBL; AJ748602; CAG38377.1; -; mRNA.
DR EMBL; AJ748603; CAG38378.1; -; mRNA.
DR EMBL; AY274116; AAP23233.1; -; mRNA.
DR EMBL; AK046243; BAC32651.1; -; mRNA.
DR EMBL; AK046879; BAC32905.1; -; mRNA.
DR EMBL; AK082707; BAC38580.1; -; mRNA.
DR EMBL; BC141125; AAI41126.1; -; mRNA.
DR CCDS; CCDS19235.1; -. [Q8BL65-1]
DR CCDS; CCDS51475.1; -. [Q8BL65-4]
DR CCDS; CCDS51476.1; -. [Q8BL65-3]
DR CCDS; CCDS51477.1; -. [Q8BL65-2]
DR RefSeq; NP_001171168.1; NM_001177697.1. [Q8BL65-4]
DR RefSeq; NP_001171170.1; NM_001177699.1. [Q8BL65-3]
DR RefSeq; NP_001171171.1; NM_001177700.1. [Q8BL65-2]
DR RefSeq; NP_808346.3; NM_177678.7. [Q8BL65-1]
DR AlphaFoldDB; Q8BL65; -.
DR BMRB; Q8BL65; -.
DR SMR; Q8BL65; -.
DR BioGRID; 231091; 11.
DR IntAct; Q8BL65; 1.
DR MINT; Q8BL65; -.
DR STRING; 10090.ENSMUSP00000123525; -.
DR iPTMnet; Q8BL65; -.
DR PhosphoSitePlus; Q8BL65; -.
DR SwissPalm; Q8BL65; -.
DR MaxQB; Q8BL65; -.
DR PeptideAtlas; Q8BL65; -.
DR PRIDE; Q8BL65; -.
DR ProteomicsDB; 285914; -. [Q8BL65-1]
DR ProteomicsDB; 285915; -. [Q8BL65-2]
DR ProteomicsDB; 285916; -. [Q8BL65-3]
DR ProteomicsDB; 285917; -. [Q8BL65-4]
DR ProteomicsDB; 285918; -. [Q8BL65-5]
DR Antibodypedia; 22725; 51 antibodies from 15 providers.
DR DNASU; 231148; -.
DR Ensembl; ENSMUST00000054598; ENSMUSP00000050571; ENSMUSG00000029095. [Q8BL65-1]
DR Ensembl; ENSMUST00000114204; ENSMUSP00000109842; ENSMUSG00000029095. [Q8BL65-3]
DR Ensembl; ENSMUST00000114205; ENSMUSP00000109843; ENSMUSG00000029095. [Q8BL65-2]
DR Ensembl; ENSMUST00000114206; ENSMUSP00000109844; ENSMUSG00000029095. [Q8BL65-4]
DR Ensembl; ENSMUST00000114210; ENSMUSP00000109848; ENSMUSG00000029095. [Q8BL65-5]
DR GeneID; 231148; -.
DR KEGG; mmu:231148; -.
DR UCSC; uc008xeg.2; mouse. [Q8BL65-1]
DR UCSC; uc033iiv.1; mouse. [Q8BL65-2]
DR UCSC; uc033iiw.1; mouse. [Q8BL65-4]
DR UCSC; uc033iix.1; mouse. [Q8BL65-3]
DR CTD; 84448; -.
DR MGI; MGI:2385758; Ablim2.
DR VEuPathDB; HostDB:ENSMUSG00000029095; -.
DR eggNOG; KOG1044; Eukaryota.
DR GeneTree; ENSGT00950000182850; -.
DR HOGENOM; CLU_001357_12_3_1; -.
DR InParanoid; Q8BL65; -.
DR OrthoDB; 192350at2759; -.
DR PhylomeDB; Q8BL65; -.
DR BioGRID-ORCS; 231148; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Ablim2; mouse.
DR PRO; PR:Q8BL65; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8BL65; protein.
DR Bgee; ENSMUSG00000029095; Expressed in superior frontal gyrus and 189 other tissues.
DR ExpressionAtlas; Q8BL65; baseline and differential.
DR Genevisible; Q8BL65; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0030016; C:myofibril; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
DR GO; GO:0030032; P:lamellipodium assembly; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR Gene3D; 1.10.950.10; -; 1.
DR InterPro; IPR028450; ABLIM2.
DR InterPro; IPR032402; AbLIM_anchor.
DR InterPro; IPR003128; Villin_headpiece.
DR InterPro; IPR036886; Villin_headpiece_dom_sf.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24213:SF6; PTHR24213:SF6; 2.
DR Pfam; PF16182; AbLIM_anchor; 2.
DR Pfam; PF00412; LIM; 4.
DR Pfam; PF02209; VHP; 1.
DR SMART; SM00132; LIM; 4.
DR SMART; SM00153; VHP; 1.
DR SUPFAM; SSF47050; SSF47050; 1.
DR PROSITE; PS51089; HP; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; LIM domain; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..612
FT /note="Actin-binding LIM protein 2"
FT /id="PRO_0000075700"
FT DOMAIN 22..81
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 81..141
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 151..210
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 210..270
FT /note="LIM zinc-binding 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 544..612
FT /note="HP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00595"
FT REGION 269..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000250"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6KC51"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6H8Q1"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 453
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6KC51"
FT MOD_RES 473
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6KC51"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6KC51"
FT VAR_SEQ 350
FT /note="E -> ESPQLLSPTPTE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012120"
FT VAR_SEQ 390
FT /note="P -> PAGTVSVGTSSCLSLSQHPSPTSVFRHHYIPYFR (in isoform
FT 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.2"
FT /id="VSP_012121"
FT VAR_SEQ 507..546
FT /note="RFPYSKPDTLPGPRKDGLDLRNANLAPCGADPDASWGTRE -> Q (in
FT isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.2"
FT /id="VSP_012122"
FT VAR_SEQ 507..526
FT /note="RFPYSKPDTLPGPRKDGLDL -> QCQPGPLWSRPGCQLGHARV (in
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012123"
FT VAR_SEQ 527..612
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_012124"
FT CONFLICT 305
FT /note="D -> N (in Ref. 3; BAC32905)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="D -> N (in Ref. 3; BAC32905)"
FT /evidence="ECO:0000305"
FT MOD_RES Q8BL65-4:351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q8BL65-4:356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 612 AA; 68107 MW; 97FE5A9C049AD455 CRC64;
MSAVSQPQAA HAPLEKPAST AILCNTCGNV CKGEVLRVQN KYFHIRCFVC KACGCDLAEG
GFFVRQGEHI CTRDYQRLYG TRCFSCDRFI EGEVVSALGK TYHPDCFVCA VCRLPFPPGD
RVTFNGKECM CQKCSPPTLL GNSAHVAQGL RSCGGCGLEI KNGQALVALD KHWHLGCFKC
KTCGKLLNAE YISKDGLPYC EADYHSKFGI RCDGCEKYIT GRVLEAGEKH YHPSCALCVR
CGQMFSEGEE MYLQGSSIWH PACRQAARTE DKSKETRTSS ESIVSVPASS TSGSPSRVIY
AKLGDEILDY RDLAALPKNK AIYNIDRPDM ISYSPYISHS AVGDRQSYGE GDQDDRSYKQ
CRTSSPSSAG SVSLGHYTPT SRSPQHYSRP GSESGRSTPS LSVHSDSRPP SSTYQQAPRH
FHVPDTGVKD NIYRKPPIYK QHAARRLDVE DSSFDQDSRK KTTWLLLKGD ADTRTNSPDL
DSQSLSLSSG TDQEPLQRMA GDSLYSRFPY SKPDTLPGPR KDGLDLRNAN LAPCGADPDA
SWGTREYKIY PYDSLIVTNR IRVKLPKDVD RTRLERHLSP EEFQEVFGMS IEEFDRLALW
KRNDLKKKAL LF
