ATRN1_MOUSE
ID ATRN1_MOUSE Reviewed; 1378 AA.
AC Q6A051; Q3UHB0; Q68HV2; Q80VI3; Q8BKS4; Q8K0P5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Attractin-like protein 1;
DE Flags: Precursor;
GN Name=Atrnl1; Synonyms=Alp, Atrnl, Kiaa0534;
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=C57BL/6J;
RA Duke-Cohan J.S.;
RT "Identification of full-length mouse attractin-like protein (Atrnl).";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 690-1237 (ISOFORM 2).
RC STRAIN=C57BL/6J;
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), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1002-1378 (ISOFORM 1).
RC STRAIN=Czech II, and FVB/N; TISSUE=Kidney, and Mammary tumor;
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 INTERACTION WITH MC4R.
RX PubMed=14531729; DOI=10.1042/bj20031241;
RA Haqq A.M., Rene P., Kishi T., Khong K., Lee C.E., Liu H., Friedman J.M.,
RA Elmquist J.K., Cone R.D.;
RT "Characterization of a novel binding partner of the melanocortin-4
RT receptor: attractin-like protein.";
RL Biochem. J. 376:595-605(2003).
RN [6]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=18064672; DOI=10.1002/dvg.20351;
RA Walker W.P., Aradhya S., Hu C.-L., Shen S., Zhang W., Azarani A., Lu X.,
RA Barsh G.S., Gunn T.M.;
RT "Genetic analysis of attractin homologs.";
RL Genesis 45:744-756(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 play a role in melanocortin signaling pathways that
CC regulate energy homeostasis. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MC4R. {ECO:0000269|PubMed:14531729}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6A051-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6A051-2; Sequence=VSP_033722, VSP_033723;
CC Name=3;
CC IsoId=Q6A051-3; Sequence=VSP_033720, VSP_033721;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, heart, lung, kidney and
CC liver. In the central nervous system, it is highly expressed in the
CC dentate gyrus, CA1-3 regions of the hippocampus, and the ventral taenia
CC tecta. {ECO:0000269|PubMed:18064672}.
CC -!- DISRUPTION PHENOTYPE: Mice are grossly normal with no alterations of
CC pigmentation, central nervous system pathology or body weight. In
CC contrast, constitutive expression of Atrnl1 in mice lacking Atrn
CC display normal, agouti-banded hairs and significantly delayed onset of
CC spongiform neurodegeneration, indicating that overexpression of Atrnl1
CC compensates for loss of Atrn. {ECO:0000269|PubMed:18064672}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32245.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY688677; AAT99560.1; -; mRNA.
DR EMBL; AK172967; BAD32245.1; ALT_INIT; mRNA.
DR EMBL; AK050882; BAC34442.1; -; mRNA.
DR EMBL; AK147492; BAE27947.1; -; mRNA.
DR EMBL; BC030872; AAH30872.1; -; mRNA.
DR EMBL; BC050020; AAH50020.1; -; mRNA.
DR CCDS; CCDS29928.1; -. [Q6A051-1]
DR RefSeq; NP_852080.3; NM_181415.4. [Q6A051-1]
DR AlphaFoldDB; Q6A051; -.
DR SMR; Q6A051; -.
DR BioGRID; 230494; 1.
DR STRING; 10090.ENSMUSP00000076514; -.
DR GlyGen; Q6A051; 8 sites.
DR PhosphoSitePlus; Q6A051; -.
DR MaxQB; Q6A051; -.
DR PaxDb; Q6A051; -.
DR PeptideAtlas; Q6A051; -.
DR PRIDE; Q6A051; -.
DR ProteomicsDB; 277196; -. [Q6A051-1]
DR ProteomicsDB; 277197; -. [Q6A051-2]
DR ProteomicsDB; 277198; -. [Q6A051-3]
DR Antibodypedia; 52380; 30 antibodies from 12 providers.
DR DNASU; 226255; -.
DR Ensembl; ENSMUST00000077282; ENSMUSP00000076514; ENSMUSG00000054843. [Q6A051-1]
DR GeneID; 226255; -.
DR KEGG; mmu:226255; -.
DR UCSC; uc008iai.2; mouse. [Q6A051-1]
DR UCSC; uc008iaj.1; mouse. [Q6A051-3]
DR CTD; 26033; -.
DR MGI; MGI:2147749; Atrnl1.
DR VEuPathDB; HostDB:ENSMUSG00000054843; -.
DR eggNOG; KOG1388; Eukaryota.
DR GeneTree; ENSGT00940000155790; -.
DR HOGENOM; CLU_003930_0_0_1; -.
DR InParanoid; Q6A051; -.
DR OMA; ACDEWKT; -.
DR OrthoDB; 49565at2759; -.
DR PhylomeDB; Q6A051; -.
DR TreeFam; TF321873; -.
DR BioGRID-ORCS; 226255; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Atrnl1; mouse.
DR PRO; PR:Q6A051; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q6A051; protein.
DR Bgee; ENSMUSG00000054843; Expressed in pigmented layer of retina and 228 other tissues.
DR Genevisible; Q6A051; MM.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IPI:MGI.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd03597; CLECT_attractin_like; 1.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00055; EGF_Lam; 1.
DR Gene3D; 2.120.10.80; -; 2.
DR Gene3D; 2.60.120.290; -; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR034011; Attractin-like_CTLD.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF00053; Laminin_EGF; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF01437; PSI; 2.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00180; EGF_Lam; 1.
DR SMART; SM00423; PSI; 5.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; EGF-like domain;
KW Glycoprotein; Kelch repeat; Laminin EGF-like domain; Lectin; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..51
FT /evidence="ECO:0000255"
FT CHAIN 52..1378
FT /note="Attractin-like protein 1"
FT /id="PRO_0000334651"
FT TOPO_DOM 52..1229
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1230..1250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1251..1378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 52..90
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 92..208
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 206..244
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 315..364
FT /note="Kelch 1"
FT REPEAT 366..414
FT /note="Kelch 2"
FT REPEAT 426..474
FT /note="Kelch 3"
FT REPEAT 479..530
FT /note="Kelch 4"
FT REPEAT 532..590
FT /note="Kelch 5"
FT REPEAT 591..637
FT /note="Kelch 6"
FT DOMAIN 613..656
FT /note="PSI 1"
FT DOMAIN 665..708
FT /note="PSI 2"
FT DOMAIN 714..759
FT /note="PSI 3"
FT DOMAIN 754..872
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 888..938
FT /note="PSI 4"
FT DOMAIN 941..1011
FT /note="PSI 5"
FT DOMAIN 1013..1058
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1059..1107
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 1287..1324
FT /note="Interaction with MC4R"
FT /evidence="ECO:0000269|PubMed:14531729"
FT REGION 1351..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 703
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 777
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 897
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..78
FT /evidence="ECO:0000250"
FT DISULFID 80..89
FT /evidence="ECO:0000250"
FT DISULFID 92..118
FT /evidence="ECO:0000250"
FT DISULFID 210..220
FT /evidence="ECO:0000250"
FT DISULFID 214..232
FT /evidence="ECO:0000250"
FT DISULFID 234..243
FT /evidence="ECO:0000250"
FT DISULFID 775..871
FT /evidence="ECO:0000250"
FT DISULFID 1013..1021
FT /evidence="ECO:0000250"
FT DISULFID 1015..1027
FT /evidence="ECO:0000250"
FT DISULFID 1030..1039
FT /evidence="ECO:0000250"
FT DISULFID 1042..1056
FT /evidence="ECO:0000250"
FT DISULFID 1059..1068
FT /evidence="ECO:0000250"
FT DISULFID 1061..1075
FT /evidence="ECO:0000250"
FT DISULFID 1077..1087
FT /evidence="ECO:0000250"
FT DISULFID 1090..1105
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..561
FT /note="MEPGVRARSGAPQPASPVLWRARPAGGGGASSWLLLDGNSWLLCYGFLYLAL
FT YAQVSQSKPCERTGSCFSGRCVNSTCLCDPGWVGDQCQHCQGRFKLTEPSGYLTDGPIN
FT YKYKTKCTWLIEGYPNAVLRLRFNHFATECSWDHMYVYDGDSIYAPLVAVLSGLIVPEV
FT RGNETVPEVVTTSGYALLHFFSDAAYNLTGFNIFYSINSCPNNCSGHGKCTTSVSVASQ
FT VYCECDKYWKGEACDIPYCKANCGSPDHGYCDLTGEKLCVCNDSWQGPDCSLNVPSTES
FT YWILPNVKPFSPSVGRASHKAVLHGKFMWVIGGYTFNYSSFQMVLNYNLESSIWNVGAV
FT SRGPLQRYGHSLALYQENIFMYGGRMETSDGNVTDELWVFNVRSQSWSTKTPTVLGHSQ
FT QYAVEGHSAHIMELDSRDVVMIVIFGYSAIYGYTSSIQEYHISSNTWLVPETKGAIVQG
FT GYGHTSVYDEVTKSIYVHGGYKALPGNKYGLVDDLYKYEVNTRTWTILKESGFARYLHS
FT AVLINGAMLIFGGNTHNDTSLSNGAKCFSADFLAYDI -> MGWWTTSISTKSTPGL
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033720"
FT VAR_SEQ 1012..1057
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033721"
FT VAR_SEQ 1090..1094
FT /note="CDSEN -> YCQFF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033722"
FT VAR_SEQ 1095..1378
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033723"
FT CONFLICT 47
FT /note="F -> S (in Ref. 1; AAT99560)"
FT /evidence="ECO:0000305"
FT CONFLICT 851
FT /note="R -> K (in Ref. 4; AAH50020)"
FT /evidence="ECO:0000305"
FT CONFLICT 983
FT /note="A -> V (in Ref. 2; BAD32245)"
FT /evidence="ECO:0000305"
FT CONFLICT 1191
FT /note="E -> D (in Ref. 4; AAH50020)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1378 AA; 152467 MW; 28E9AE30440E32A7 CRC64;
MEPGVRARSG APQPASPVLW RARPAGGGGA SSWLLLDGNS WLLCYGFLYL ALYAQVSQSK
PCERTGSCFS GRCVNSTCLC DPGWVGDQCQ HCQGRFKLTE PSGYLTDGPI NYKYKTKCTW
LIEGYPNAVL RLRFNHFATE CSWDHMYVYD GDSIYAPLVA VLSGLIVPEV RGNETVPEVV
TTSGYALLHF FSDAAYNLTG FNIFYSINSC PNNCSGHGKC TTSVSVASQV YCECDKYWKG
EACDIPYCKA NCGSPDHGYC DLTGEKLCVC NDSWQGPDCS LNVPSTESYW ILPNVKPFSP
SVGRASHKAV LHGKFMWVIG GYTFNYSSFQ MVLNYNLESS IWNVGAVSRG PLQRYGHSLA
LYQENIFMYG GRMETSDGNV TDELWVFNVR SQSWSTKTPT VLGHSQQYAV EGHSAHIMEL
DSRDVVMIVI FGYSAIYGYT SSIQEYHISS NTWLVPETKG AIVQGGYGHT SVYDEVTKSI
YVHGGYKALP GNKYGLVDDL YKYEVNTRTW TILKESGFAR YLHSAVLING AMLIFGGNTH
NDTSLSNGAK CFSADFLAYD IACDEWKTLP KPNLHRDVNR FGHSAVVING SMYIFGGFSS
VLLNDILVYK PPNCKAFRDE ELCRNAGPGI KCVWNKNHCE SWESGNTNNI LRAKCPPKTA
ATDDRCYRYA DCASCTANTN GCQWCDDKKC ISASSNCSTS VRNYTKCHIR NEQICNKLTS
CKSCSLNLNC QWDQRQQECQ ALPAHLCGEG WNHVGDACLR INSSRESYDN AKLYCYNLSG
NLASLTTSKE VEFVLDEIQK FTQQKVSPWV GLRKINISYW GWEDMSPFTN TSLQWLPGEP
NDSGFCAYLE RAAVAGLKAN PCTSMADGLV CEKPVVSPNQ NARPCKKPCS LRTSCANCTS
SGMECMWCSS TKRCVDSNAY IISFPYGQCL EWQTATCSPQ NCSGLRTCGQ CLEQPGCGWC
NDPSNTGRGY CIEGSSRGPM KLAGVHNSDV VLDTSLCPKE KNYEWSFIQC PACQCNGHST
CINNNVCEQC KNLTTGRQCQ ECMPGYYGDP TNGGQCTACT CGGHANVCHL HTGKCFCTTK
GIKGDQCQLC DSENRYVGNP LRGTCYYSLL IDYQFTFSLL QEDDRHHTAI NFIANPEQSN
KNLDISINAS NNFNLNITWS VGSTGGTISG EETPIVSKTN IKEYRDSFSY EKFNFRSNPN
ITFYVYVSNF SWPIKIQIAF SQHNTIMDLV QFFVTFFSCF LSLLLVAAVV WKIKQTCWAS
RRREQLLRER QQMASRPFAS VDVALEVGAE QTDFLRGPLE GAPKPIAIEP CAGNRAAVLT
VFLCLPRGSS GAPPPGQSGL AIASALIDIS QQKPSDNKDK TSGVRNRKHL STRQGTCV
