ICA_MOUSE
ID ICA_MOUSE Reviewed; 700 AA.
AC Q9DBD0;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Inhibitor of carbonic anhydrase;
DE Flags: Precursor;
GN Name=Ica;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
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 [2]
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 [3]
RP IDENTIFICATION, FUNCTION, LACK OF IRON BINDING, GLYCOSYLATION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17511619; DOI=10.1042/bj20070384;
RA Wang F., Lothrop A.P., James N.G., Griffiths T.A., Lambert L.A.,
RA Leverence R., Kaltashov I.A., Andrews N.C., MacGillivray R.T., Mason A.B.;
RT "A novel murine protein with no effect on iron homoeostasis is homologous
RT with transferrin and is the putative inhibitor of carbonic anhydrase.";
RL Biochem. J. 406:85-95(2007).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-664.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=17330941; DOI=10.1021/pr0604559;
RA Bernhard O.K., Kapp E.A., Simpson R.J.;
RT "Enhanced analysis of the mouse plasma proteome using cysteine-containing
RT tryptic glycopeptides.";
RL J. Proteome Res. 6:987-995(2007).
RN [5]
RP FUNCTION, INTERACTION WITH CA2, MUTAGENESIS OF TRP-143 AND SER-207,
RP GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18712936; DOI=10.1021/bi801133d;
RA Mason A.B., Judson G.L., Bravo M.C., Edelstein A., Byrne S.L., James N.G.,
RA Roush E.D., Fierke C.A., Bobst C.E., Kaltashov I.A., Daughtery M.A.;
RT "Evolution reversed: the ability to bind iron restored to the N-lobe of the
RT murine inhibitor of carbonic anhydrase by strategic mutagenesis.";
RL Biochemistry 47:9847-9855(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 20-700, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=20572014; DOI=10.1002/pro.439;
RA Eckenroth B.E., Mason A.B., McDevitt M.E., Lambert L.A., Everse S.J.;
RT "The structure and evolution of the murine inhibitor of carbonic anhydrase:
RT a member of the transferrin superfamily.";
RL Protein Sci. 19:1616-1626(2010).
CC -!- FUNCTION: Inhibitor for carbonic anhydrase 2 (CA2). Does not bind iron
CC ions. {ECO:0000269|PubMed:17511619, ECO:0000269|PubMed:18712936}.
CC -!- SUBUNIT: Monomer. Interacts (via transferrin-like domain 2) with CA2.
CC {ECO:0000269|PubMed:18712936, ECO:0000269|PubMed:20572014}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17511619}.
CC -!- TISSUE SPECIFICITY: Detected in blood plasma, heart, kidney, liver,
CC colon, lung, spleen, pancreas and testis (at protein level).
CC {ECO:0000269|PubMed:17511619}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17330941,
CC ECO:0000269|PubMed:17511619, ECO:0000269|PubMed:18712936}.
CC -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00741}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC122747; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK005035; BAB23762.1; -; mRNA.
DR CCDS; CCDS23452.1; -.
DR RefSeq; NP_082194.1; NM_027918.2.
DR PDB; 3MC2; X-ray; 2.40 A; A/B/C/D=20-700.
DR PDBsum; 3MC2; -.
DR AlphaFoldDB; Q9DBD0; -.
DR SMR; Q9DBD0; -.
DR STRING; 10090.ENSMUSP00000035163; -.
DR MEROPS; S60.977; -.
DR MEROPS; S60.979; -.
DR GlyConnect; 700; 1 N-Linked glycan (1 site).
DR GlyGen; Q9DBD0; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; Q9DBD0; -.
DR PhosphoSitePlus; Q9DBD0; -.
DR SwissPalm; Q9DBD0; -.
DR CPTAC; non-CPTAC-3549; -.
DR jPOST; Q9DBD0; -.
DR MaxQB; Q9DBD0; -.
DR PaxDb; Q9DBD0; -.
DR PeptideAtlas; Q9DBD0; -.
DR PRIDE; Q9DBD0; -.
DR ProteomicsDB; 269524; -.
DR DNASU; 71775; -.
DR Ensembl; ENSMUST00000035163; ENSMUSP00000035163; ENSMUSG00000033688.
DR GeneID; 71775; -.
DR KEGG; mmu:71775; -.
DR UCSC; uc009rgk.1; mouse.
DR CTD; 71775; -.
DR MGI; MGI:1919025; 1300017J02Rik.
DR VEuPathDB; HostDB:ENSMUSG00000033688; -.
DR eggNOG; ENOG502QT0C; Eukaryota.
DR GeneTree; ENSGT00940000163596; -.
DR HOGENOM; CLU_011309_1_0_1; -.
DR InParanoid; Q9DBD0; -.
DR OMA; VQWCAVG; -.
DR OrthoDB; 232859at2759; -.
DR PhylomeDB; Q9DBD0; -.
DR TreeFam; TF324013; -.
DR BioGRID-ORCS; 71775; 4 hits in 72 CRISPR screens.
DR EvolutionaryTrace; Q9DBD0; -.
DR PRO; PR:Q9DBD0; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9DBD0; protein.
DR Bgee; ENSMUSG00000033688; Expressed in left lobe of liver and 89 other tissues.
DR ExpressionAtlas; Q9DBD0; baseline and differential.
DR Genevisible; Q9DBD0; MM.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0004857; F:enzyme inhibitor activity; IDA:MGI.
DR GO; GO:0019731; P:antibacterial humoral response; IBA:GO_Central.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
DR InterPro; IPR029785; ICA.
DR InterPro; IPR016357; Transferrin.
DR InterPro; IPR001156; Transferrin-like_dom.
DR InterPro; IPR018195; Transferrin_Fe_BS.
DR PANTHER; PTHR11485:SF20; PTHR11485:SF20; 1.
DR Pfam; PF00405; Transferrin; 2.
DR PIRSF; PIRSF002549; Transferrin; 1.
DR PRINTS; PR00422; TRANSFERRIN.
DR SMART; SM00094; TR_FER; 2.
DR PROSITE; PS00205; TRANSFERRIN_LIKE_1; 1.
DR PROSITE; PS00207; TRANSFERRIN_LIKE_3; 1.
DR PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..700
FT /note="Inhibitor of carbonic anhydrase"
FT /id="PRO_0000415376"
FT DOMAIN 25..347
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 355..685
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT CARBOHYD 664
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17330941"
FT DISULFID 28..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:20572014"
FT DISULFID 38..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:20572014"
FT DISULFID 137..213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:20572014"
FT DISULFID 172..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:20572014"
FT DISULFID 175..198
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:20572014"
FT DISULFID 185..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:20572014"
FT DISULFID 246..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:20572014"
FT DISULFID 358..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:20572014"
FT DISULFID 368..381
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:20572014"
FT DISULFID 415..695
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:20572014"
FT DISULFID 438..658
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:20572014"
FT DISULFID 470..545
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:20572014"
FT DISULFID 494..686
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:20572014"
FT DISULFID 504..518
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:20572014"
FT DISULFID 515..528
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:20572014"
FT DISULFID 585..599
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741,
FT ECO:0000269|PubMed:20572014"
FT MUTAGEN 143
FT /note="W->R: Confers ability to bind ferric iron and
FT carbonate; when associated with Y-207."
FT /evidence="ECO:0000269|PubMed:18712936"
FT MUTAGEN 207
FT /note="S->Y: Confers ability to bind ferric iron and
FT carbonate; when associated with R-143."
FT /evidence="ECO:0000269|PubMed:18712936"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 33..48
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 64..72
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 96..105
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 113..121
FT /evidence="ECO:0007829|PDB:3MC2"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:3MC2"
FT TURN 128..133
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:3MC2"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:3MC2"
FT TURN 178..180
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 206..209
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 257..259
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 269..277
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 279..292
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 293..300
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 307..311
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 330..345
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 355..362
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 363..374
FT /evidence="ECO:0007829|PDB:3MC2"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 378..386
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 387..396
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 406..414
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 418..422
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 446..455
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 469..472
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 477..481
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 483..488
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 496..499
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 500..504
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 515..517
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 530..534
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 538..548
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 551..555
FT /evidence="ECO:0007829|PDB:3MC2"
FT TURN 561..563
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 571..573
FT /evidence="ECO:0007829|PDB:3MC2"
FT TURN 578..580
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 581..584
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 586..588
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:3MC2"
FT TURN 596..598
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 601..604
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 608..611
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 613..615
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 616..630
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 636..639
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 646..648
FT /evidence="ECO:0007829|PDB:3MC2"
FT STRAND 650..652
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 668..679
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 684..686
FT /evidence="ECO:0007829|PDB:3MC2"
FT HELIX 690..695
FT /evidence="ECO:0007829|PDB:3MC2"
SQ SEQUENCE 700 AA; 76766 MW; 38C991D1021AE548 CRC64;
MRLLICALLC LGTLGLCLAL PEKTIRWCVV SDHEATKCSS FRDNMKKVLP AGGPAVTCVR
KMSHPECIRD ISANKVDAVT VDGALVAEAD LPHHSLKPIM AEYYGSKDDP KTHYYVVAMA
KKGTGFQLNQ LRGKKSCHTG LGWSAGWYVP LSTLLPSGSR ETAAATFFSS SCVPCADGKM
FPSLCQLCAG KGTDKCACSS REPYFGSWGA LKCLQDGTAD VSFVKHLTVF EAMPTKADRD
QYELLCMDNT RRPVEEYEQC YLARVPSHVV VARSVDGKED SIQELLRVAQ EHFGKDKSSP
FQLFGSPHGE DLLFTDAAHG LLRVPRKIDI SLYLGYEFLS AFRNLKRGLE DSQRVKWCAV
GQQERTKCDQ WSAVSGGALA CATEETPEDC IAATMKGEAD AMSLDGGFAY VAGHCGLVPV
LAENYLSTHS SGRLGSKCVN APLEGYYVVA VVKKSDVGIT WKSLQGKKSC HTAVGTSEGW
NVPMGLIYNQ TGSCKFDAFF SRSCAPGSDP DSPLCALCVG GNNPAHMCAA NNAEGYHGSS
GALRCLVEKG DVAFMKHPTV LQNTDGKNPE PWAKGLKHED FELLCLDGTR KPVTEAQSCH
LARVPNRAVF SRKDKADFVR RILFNQQELF GRNGFEYMMF QMFESSAKDL LFSDDTECLS
NLQNKTTYKT YLGPQYLTLM DNFRQCLSSE LLDACTFHKY
