LAMB2_RAT
ID LAMB2_RAT Reviewed; 1801 AA.
AC P15800;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Laminin subunit beta-2;
DE AltName: Full=Laminin chain B3;
DE AltName: Full=Laminin-11 subunit beta;
DE AltName: Full=Laminin-14 subunit beta;
DE AltName: Full=Laminin-15 subunit beta;
DE AltName: Full=Laminin-3 subunit beta;
DE AltName: Full=Laminin-4 subunit beta;
DE AltName: Full=Laminin-7 subunit beta;
DE AltName: Full=Laminin-9 subunit beta;
DE AltName: Full=S-laminin subunit beta;
DE Short=S-LAM beta;
DE Flags: Precursor;
GN Name=Lamb2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=2922051; DOI=10.1038/338229a0;
RA Hunter D.D., Shah V., Merlie J.P., Sanes J.R.;
RT "A laminin-like adhesive protein concentrated in the synaptic cleft of the
RT neuromuscular junction.";
RL Nature 338:229-234(1989).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1088 AND ASN-1351, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
CC -!- FUNCTION: Binding to cells via a high affinity receptor, laminin is
CC thought to mediate the attachment, migration and organization of cells
CC into tissues during embryonic development by interacting with other
CC extracellular matrix components.
CC -!- SUBUNIT: Laminin is a complex glycoprotein, consisting of three
CC different polypeptide chains (alpha, beta, gamma), which are bound to
CC each other by disulfide bonds into a cross-shaped molecule comprising
CC one long and three short arms with globules at each end. Beta-2 is a
CC subunit of laminin-3 (laminin-121 or S-laminin), laminin-4 (laminin-221
CC or S-merosin), laminin-7 (laminin-321 or KS-laminin), laminin-9
CC (laminin-421), laminin-11 (laminin-521), laminin-14 (laminin-423) and
CC laminin-15 (laminin-523).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane.
CC -!- TISSUE SPECIFICITY: Found in the basement membranes (major component).
CC S-laminin is concentrated in the synaptic cleft of the neuromuscular
CC junction.
CC -!- DOMAIN: The alpha-helical domains I and II are thought to interact with
CC other laminin chains to form a coiled coil structure.
CC -!- DOMAIN: Domains VI and IV are globular.
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DR EMBL; X16563; CAA34561.1; -; mRNA.
DR PIR; S03539; MMRTS.
DR RefSeq; NP_037106.1; NM_012974.1.
DR PDB; 5LF2; X-ray; 1.85 A; A/B=523-833.
DR PDBsum; 5LF2; -.
DR AlphaFoldDB; P15800; -.
DR SMR; P15800; -.
DR STRING; 10116.ENSRNOP00000065052; -.
DR GlyGen; P15800; 7 sites, 11 N-linked glycans (4 sites).
DR iPTMnet; P15800; -.
DR PhosphoSitePlus; P15800; -.
DR PaxDb; P15800; -.
DR PRIDE; P15800; -.
DR GeneID; 25473; -.
DR KEGG; rno:25473; -.
DR CTD; 3913; -.
DR RGD; 2988; Lamb2.
DR eggNOG; KOG0994; Eukaryota.
DR InParanoid; P15800; -.
DR PhylomeDB; P15800; -.
DR Reactome; R-RNO-3000157; Laminin interactions.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8874081; MET activates PTK2 signaling.
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR PRO; PR:P15800; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005604; C:basement membrane; ISO:RGD.
DR GO; GO:0043256; C:laminin complex; ISO:RGD.
DR GO; GO:0005608; C:laminin-3 complex; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0043083; C:synaptic cleft; ISO:RGD.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; ISO:RGD.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0014002; P:astrocyte development; ISO:RGD.
DR GO; GO:0048677; P:axon extension involved in regeneration; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0070831; P:basement membrane assembly; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0000904; P:cell morphogenesis involved in differentiation; ISO:RGD.
DR GO; GO:0072274; P:metanephric glomerular basement membrane development; ISO:RGD.
DR GO; GO:0072249; P:metanephric podocyte development; ISO:RGD.
DR GO; GO:0007528; P:neuromuscular junction development; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR GO; GO:0060041; P:retina development in camera-type eye; ISO:RGD.
DR GO; GO:0014044; P:Schwann cell development; ISO:RGD.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0050808; P:synapse organization; ISO:RGD.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; ISO:RGD.
DR CDD; cd00055; EGF_Lam; 13.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013015; Laminin_IV_B.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR Pfam; PF00053; Laminin_EGF; 13.
DR Pfam; PF00055; Laminin_N; 1.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00180; EGF_Lam; 13.
DR SMART; SM00136; LamNT; 1.
DR PROSITE; PS00022; EGF_1; 10.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS01248; EGF_LAM_1; 12.
DR PROSITE; PS50027; EGF_LAM_2; 13.
DR PROSITE; PS51116; LAMININ_IVB; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Basement membrane; Cell adhesion; Coiled coil;
KW Disulfide bond; Extracellular matrix; Glycoprotein;
KW Laminin EGF-like domain; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..35
FT CHAIN 36..1801
FT /note="Laminin subunit beta-2"
FT /id="PRO_0000017070"
FT DOMAIN 46..285
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 286..349
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 350..412
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 413..472
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 473..524
FT /note="Laminin EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 525..555
FT /note="Laminin EGF-like 5; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 564..780
FT /note="Laminin IV type B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00462"
FT DOMAIN 786..833
FT /note="Laminin EGF-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 834..879
FT /note="Laminin EGF-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 880..929
FT /note="Laminin EGF-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 930..988
FT /note="Laminin EGF-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 989..1040
FT /note="Laminin EGF-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1041..1097
FT /note="Laminin EGF-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1098..1145
FT /note="Laminin EGF-like 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1146..1192
FT /note="Laminin EGF-like 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 1193..1412
FT /note="Domain II"
FT REGION 1413..1445
FT /note="Domain alpha"
FT REGION 1446..1801
FT /note="Domain I"
FT REGION 1684..1703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1259..1306
FT /evidence="ECO:0000255"
FT COILED 1475..1529
FT /evidence="ECO:0000255"
FT COILED 1576..1793
FT /evidence="ECO:0000255"
FT MOD_RES 1535
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P55268"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1088
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 1252
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 1502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 286..295
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 288..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 315..324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 327..347
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 350..359
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 352..377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 380..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 392..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 413..426
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 415..441
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 443..452
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 455..470
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 473..487
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 475..494
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 496..505
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 508..522
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 525..537
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 527..544
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 546..555
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 786..798
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 788..805
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 807..816
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 819..831
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 834..846
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 836..853
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 855..864
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 867..877
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 880..889
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 882..896
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 899..908
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 911..927
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 930..946
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 932..957
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 959..968
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 971..986
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 989..1003
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 991..1010
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1013..1022
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1025..1038
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1041..1061
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1043..1068
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1070..1079
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1082..1095
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1098..1110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1100..1117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1119..1128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1131..1143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1146..1158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1148..1165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1167..1176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1179..1190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 1193
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1196
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT DISULFID 1800
FT /note="Interchain"
FT /evidence="ECO:0000305"
FT TURN 529..531
FT /evidence="ECO:0007829|PDB:5LF2"
FT STRAND 532..536
FT /evidence="ECO:0007829|PDB:5LF2"
FT TURN 539..541
FT /evidence="ECO:0007829|PDB:5LF2"
FT STRAND 550..552
FT /evidence="ECO:0007829|PDB:5LF2"
FT STRAND 562..564
FT /evidence="ECO:0007829|PDB:5LF2"
FT STRAND 570..573
FT /evidence="ECO:0007829|PDB:5LF2"
FT HELIX 574..576
FT /evidence="ECO:0007829|PDB:5LF2"
FT STRAND 578..580
FT /evidence="ECO:0007829|PDB:5LF2"
FT STRAND 583..586
FT /evidence="ECO:0007829|PDB:5LF2"
FT STRAND 601..605
FT /evidence="ECO:0007829|PDB:5LF2"
FT STRAND 610..615
FT /evidence="ECO:0007829|PDB:5LF2"
FT STRAND 619..631
FT /evidence="ECO:0007829|PDB:5LF2"
FT STRAND 638..646
FT /evidence="ECO:0007829|PDB:5LF2"
FT TURN 656..659
FT /evidence="ECO:0007829|PDB:5LF2"
FT HELIX 662..665
FT /evidence="ECO:0007829|PDB:5LF2"
FT STRAND 666..671
FT /evidence="ECO:0007829|PDB:5LF2"
FT STRAND 676..679
FT /evidence="ECO:0007829|PDB:5LF2"
FT STRAND 684..686
FT /evidence="ECO:0007829|PDB:5LF2"
FT STRAND 692..702
FT /evidence="ECO:0007829|PDB:5LF2"
FT STRAND 716..725
FT /evidence="ECO:0007829|PDB:5LF2"
FT HELIX 727..729
FT /evidence="ECO:0007829|PDB:5LF2"
FT HELIX 731..734
FT /evidence="ECO:0007829|PDB:5LF2"
FT STRAND 735..737
FT /evidence="ECO:0007829|PDB:5LF2"
FT HELIX 738..749
FT /evidence="ECO:0007829|PDB:5LF2"
FT HELIX 752..756
FT /evidence="ECO:0007829|PDB:5LF2"
FT STRAND 757..759
FT /evidence="ECO:0007829|PDB:5LF2"
FT HELIX 768..780
FT /evidence="ECO:0007829|PDB:5LF2"
FT TURN 790..792
FT /evidence="ECO:0007829|PDB:5LF2"
FT TURN 813..816
FT /evidence="ECO:0007829|PDB:5LF2"
SQ SEQUENCE 1801 AA; 196474 MW; 97AEF32F8F31FA75 CRC64;
MEWASGKPGR GRQGQPVPWE LRLGLLLSVL AATLAQVPSL DVPGCSRGSC YPATGDLLVG
RADRLTASST CGLHSPQPYC IVSHLQDEKK CFLCDSRRPF SARDNPNSHR IQNVVTSFAP
QRRTAWWQSE NGVPMVTIQL DLEAEFHFTH LIMTFKTFRP AAMLVERSAD FGRTWRVYRY
FSYDCGADFP GIPLAPPRRW DDVVCESRYS EIEPSTEGEV IYRVLDPAIP IPDPYSSRIQ
NLLKITNLRV NLTRLHTLGD NLLDPRREIR EKYYYALYEL VIRGNCFCYG HASQCAPAPG
APAHAEGMVH GACICKHNTR GLNCEQCQDF YQDLPWHPAE DGHTHACRKC ECNGHSHSCH
FDMAVYLASG NVSGGVCDGC QHNTAGRHCE LCRPFFYRDP TKDMRDPAAC RPCDCDPMGS
QDGGRCDSHD DPVLGLVSGQ CRCKEHVVGT RCQQCRDGFF GLSASNPRGC QRCQCNSRGT
VPGGTPCDSS SGTCFCKRLV TGDGCDRCLP GHWGLSHDLL GCRPCDCDVG GALDPQCDEA
TGQCPCRPHM IGRRCEQVQP GYFRPFLDHL TWEAEGAHGQ VLEVVERLVT NRETPSWTGV
GFVRLREGQE VEFLVTSLPR AMDYDLLLRW EPQVPEQWAE LELVVQRPGP VSAHSPCGHV
LPRDDRIQGM LHPNTRVLVF PRPVCLEPGL SYKLKLKLTG TGGRAHPETP YSGSGILIDS
LVLQPHVLML EMFSGGDAAA LERRTTFERY RCHEEGLMPS KTPLSEACVP LLISASSLVY
NGALPCQCDP QGSLSSECNP HGGQCRCKPG VVGRRCDACA TGYYGFGPAG CQACQCSPDG
ALSALCEGTS GQCLCRTGAF GLRCDHCQRG QWGFPNCRPC VCNGRADECD AHTGACLGCR
DYTGGEHCER CIAGFHGDPR LPYGGQCRPC PCPEGPGSQR HFATSCHRDG YSQQIVCHCR
AGYTGLRCEA CAPGHFGDPS KPGGRCQLCE CSGNIDPTDP GACDPHTGQC LRCLHHTEGP
HCGHCKPGFH GQAARQSCHR CTCNLLGTDP QRCPSTDLCH CDPSTGQCPC LPHVQGLSCD
RCAPNFWNFT SGRGCQPCAC HPSRARGPTC NEFTGQCHCH AGFGGRTCSE CQELHWGDPG
LQCRACDCDP RGIDKPQCHR STGHCSCRPG VSGVRCDQCA RGFSGVFPAC HPCHACFGDW
DRVVQDLAAR TRRLEQWAQE LQQTGVLGAF ESSFLNLQGK LGMVQAIVAA RNTSAASTAK
LVEATEGLRH EIGKTTERLT QLEAELTDVQ DENFNANHAL SGLERDGLAL NLTLRQLDQH
LDILKHSNFL GAYDSIRHAH SQSTEAERRA NASTFAIPSP VSNSADTRRR AEVLMGAQRE
NFNRQHLANQ QALGRLSTHT HTLSLTGVNE LVCGAPGDAP CATSPCGGAG CRDEDGQPRC
GGLGCSGAAA TADLALGRAR HTQAELQRAL VEGGGILSRV SETRRQAEEA QQRAQAALDK
ANASRGQVEQ ANQELRELIQ NVKDFLSQEG ADPDSIEMVA TRVLDISIPA SPEQIQRLAS
EIAERVRSLA DVDTILAHTM GDVRRAEQLL QDAQRARSRA EGERQKAETV QAALEEAQRA
QGAAQGAIRG AVVDTKNTEQ TLQQVQERMA GTEQSLNSAS ERARQLHALL EALKLKRAGN
SLAASTAEET AGSAQSRARE AEKQLREQVG DQYQTVRALA ERKAEGVLAA QARAEQLRDE
ARGLLQAAQD KLQRLQELEG TYEENERELE VKAAQLDGLE ARMRSVLQAI NLQVQIYNTC
Q
