CADH4_CAEEL
ID CADH4_CAEEL Reviewed; 4328 AA.
AC Q19319; A0A1C3NSI5; G5EE05; Q19785; Q21606;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 4.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Cadherin-4;
DE Flags: Precursor;
GN Name=cdh-4 {ECO:0000312|WormBase:F25F2.2};
GN ORFNames=F25F2.2 {ECO:0000312|WormBase:F25F2.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-2916, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RA Schmitz C., Wacker I., Schwarz V., Hutter H.;
RT "The fat-like cadherin CDH-4 controls axon guidance in the ventral cord of
RT C. elegans.";
RL (In) Proceedings of the 15th international C. elegans meeting, pp.288-288,
RL Los Angeles (2005).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1192 AND ASN-2916, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
RN [5]
RP FUNCTION.
RX PubMed=17213328; DOI=10.1073/pnas.0510527104;
RA Schmitz C., Kinge P., Hutter H.;
RT "Axon guidance genes identified in a large-scale RNAi screen using the
RT RNAi-hypersensitive Caenorhabditis elegans strain nre-1(hd20) lin-
RT 15b(hd126).";
RL Proc. Natl. Acad. Sci. U.S.A. 104:834-839(2007).
RN [6]
RP FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 127-ARG--SER-4328 AND 839-LEU--SER-4328.
RX PubMed=22442082; DOI=10.1523/jneurosci.3094-11.2012;
RA Najarro E.H., Wong L., Zhen M., Carpio E.P., Goncharov A., Garriga G.,
RA Lundquist E.A., Jin Y., Ackley B.D.;
RT "Caenorhabditis elegans flamingo cadherin fmi-1 regulates GABAergic
RT neuronal development.";
RL J. Neurosci. 32:4196-4211(2012).
CC -!- FUNCTION: Potential calcium-dependent cell-adhesion protein that
CC controls axon guidance in the ventral cord.
CC {ECO:0000269|PubMed:17213328, ECO:0000269|PubMed:22442082,
CC ECO:0000269|Ref.3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In larvae and adult, it is expressed in various
CC tissues including pharyngeal muscle, hypodermis and gonad. In the
CC nervous system it is expressed in sensory neurons and motor neurons in
CC the ventral cord. {ECO:0000269|Ref.3}.
CC -!- DEVELOPMENTAL STAGE: Broadly expressed in the nervous system starting
CC early in development (PubMed:22442082). At the L3 larval stage, broad
CC expression throughout the nervous system ceases, and it is specifically
CC expressed in ventral D-type GABAergic motorneurons (PubMed:22442082).
CC {ECO:0000269|PubMed:22442082}.
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC cadherin domain and rigidify the connections, imparting a strong
CC curvature to the full-length ectodomain. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in irregular
CC accumulation of snb-1-positive synaptic vesicles along the axons of
CC ventral D-type GABAergic motorneurons. {ECO:0000269|PubMed:22442082}.
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DR EMBL; BX284603; SBV53364.1; -; Genomic_DNA.
DR PIR; T20721; T20721.
DR RefSeq; NP_001317871.1; NM_001330837.1.
DR SMR; Q19319; -.
DR BioGRID; 40826; 1.
DR IntAct; Q19319; 1.
DR STRING; 6239.F25F2.2a; -.
DR iPTMnet; Q19319; -.
DR EPD; Q19319; -.
DR PaxDb; Q19319; -.
DR PeptideAtlas; Q19319; -.
DR PRIDE; Q19319; -.
DR EnsemblMetazoa; F25F2.2.1; F25F2.2.1; WBGene00000396.
DR GeneID; 175590; -.
DR KEGG; cel:CELE_F25F2.2; -.
DR UCSC; F25F2.2; c. elegans.
DR CTD; 175590; -.
DR WormBase; F25F2.2; CE51760; WBGene00000396; cdh-4.
DR eggNOG; KOG1219; Eukaryota.
DR HOGENOM; CLU_000042_2_0_1; -.
DR InParanoid; Q19319; -.
DR OrthoDB; 12779at2759; -.
DR PhylomeDB; Q19319; -.
DR Reactome; R-CEL-351906; Apoptotic cleavage of cell adhesion proteins.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-6809371; Formation of the cornified envelope.
DR PRO; PR:Q19319; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000396; Expressed in pharyngeal muscle cell (C elegans) and 14 other tissues.
DR GO; GO:0005911; C:cell-cell junction; 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:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IMP:WormBase.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:WormBase.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0097402; P:neuroblast migration; IMP:WormBase.
DR CDD; cd00110; LamG; 1.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR Pfam; PF00028; Cadherin; 15.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 29.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49313; SSF49313; 27.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00232; CADHERIN_1; 9.
DR PROSITE; PS50268; CADHERIN_2; 27.
DR PROSITE; PS00022; EGF_1; 4.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 3.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell membrane; Developmental protein;
KW Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Metal-binding;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..4328
FT /note="Cadherin-4"
FT /id="PRO_0000250582"
FT TOPO_DOM 24..4072
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 4073..4093
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 4094..4328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 108..153
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 156..275
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 384..492
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 507..608
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 609..720
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 721..826
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 827..934
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 935..1051
FT /note="Cadherin 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1047..1156
FT /note="Cadherin 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1175..1262
FT /note="Cadherin 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1265..1363
FT /note="Cadherin 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1364..1467
FT /note="Cadherin 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1476..1570
FT /note="Cadherin 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1671..1784
FT /note="Cadherin 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 1917..1984
FT /note="Cadherin 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2187..2285
FT /note="Cadherin 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2286..2397
FT /note="Cadherin 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2429..2505
FT /note="Cadherin 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2506..2608
FT /note="Cadherin 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2609..2712
FT /note="Cadherin 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2719..2813
FT /note="Cadherin 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2828..2915
FT /note="Cadherin 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 2913..3011
FT /note="Cadherin 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3012..3113
FT /note="Cadherin 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3114..3216
FT /note="Cadherin 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3217..3326
FT /note="Cadherin 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3335..3428
FT /note="Cadherin 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3429..3554
FT /note="Cadherin 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 3706..3744
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3757..3925
FT /note="Laminin G-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 3929..3966
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 3968..4004
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1246..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4143..4215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4268..4311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1090..1092
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 4207..4209
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 4143..4175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4180..4215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 811
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 899
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 1335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1610
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1895
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2059
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2367
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2844
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 2916
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498,
FT ECO:0000269|PubMed:12754521, ECO:0000269|PubMed:17761667"
FT CARBOHYD 2941
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3083
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 3727
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 4043
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 3710..3721
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3715..3732
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3734..3743
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3898..3925
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 3933..3944
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3938..3954
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3956..3965
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3972..3983
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3977..3992
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 3994..4003
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT MUTAGEN 127..4328
FT /note="Missing: In lq83; ventral D-type GABAergic axon
FT guidance and extension defects. Irregular accumulation of
FT snb-1-positive synaptic vesicles along the axons of ventral
FT D-type GABAergic motorneurons."
FT /evidence="ECO:0000269|PubMed:22442082"
FT MUTAGEN 839..4328
FT /note="Missing: In lq56; irregular accumulation of snb-1-
FT positive synaptic vesicles along the axons of ventral D-
FT type GABAergic motorneurons."
FT /evidence="ECO:0000269|PubMed:22442082"
SQ SEQUENCE 4328 AA; 481264 MW; A355CEC9E5A68362 CRC64;
MKKHRVFHLF LLIFCKAISL VTTSSSTEQI FEFTAPLYNL SVEENSIGSK YARSENSTKI
GVPLPEKDAN CKFRVAEIVG EKSSLFKAHS RQVGDFVFLR IRYKGDNPLN RELKDFYDIL
VKAMCKRRDL SNLETTARIH LRVIDRNDAS PVFLVGEQGY EAEIDDDLEP FSTVLRVEAS
DADIGINSAI YFSLVNRSHD FIVEPVTGWV RSLRHVKPGK YSLKVKSEDR ASRLYYFDEN
EVQPSWTADV LITVRETKPK PRRILVDQRK INPNILNNRQ LAAIITLKDS PNDAIVGLKG
NEKEHWFEVE PEVVGNDGTK ELRWMLYAKN GSQVPKNTNV TLTIGEDYIR RSGFSISKKP
VIPTNETVTI QIERLAEHLI RFLDNEKLTL KTDEMAPIGR ILYRMNVNVE NPDDVSLIRY
SLEYSKSDLP NATLPFAIGS KNGILRVSAK INRSERVYNF KVIASLHGIN EKLAEKDVSI
EILDSNDHAP VFSAKWMRQT PIVIGKPGDV LVKVDATDQD EGENGKIVYK FTSELPLEIN
ANTGEITLVE VPKKGNSWPA TVWAIDLGLP LSRMSALNLM FYKNGTKIPA KPKPIIIQES
ENKHSPVFSS FPEIVEVTED APIGTVVAKL QANDEDTGYN GFIRYVIHDI AGSSHEVLTV
DEQSGEITVA SDLSKLMKEK LEVLDVQLKV SAIDAGTPVK SSVKTMKLRI KDVNNHSPQF
DEVSYYLRIS ENEKPGKDIF KVTANDFDGG NNGKIKFSLG NNQEKSSVIS IDAKTGIVKL
LKSLDREDQD VHTFAIIASD EGFPMRVSVT NLTISVEDVN DNPPKCVVQH SRARIPEDLP
HGAFVSCMAA FDEDIGQNSK LKFLLNSEKV PFRIDHHSGC IFIHAPEYPL DYHKTPFFNL
SIEVADHGDP ILSTSCHLHV ELVDIAHNHL AIEFDDVAKE ASVYENSEIG TEVIMIEAKE
TGDEQKVKAE NLEYRIIGGD GWPHFSIDQK GTVRTTHLLD RETKSAYWIT VEARDSKTDL
YKDPRRRDVL HVFIRILDRN DHRPVAKKPM YIASVAENSP ANVVIVKVEA TDADDVDNDA
AAPLMFKIER GDPQSFFRID LTSGYITTSG IRRLDREKQS EHELWVSICD GGEPQLCSNV
IVIVNVLDEN DNSPTFTQAI HHYSVRSKFA GKLCRIFAVD ADEGENARLT YNITEGDARF
SIDNNGNIIA SEAIHGDESY ALTVQATDHG TPGQQFAATR VVLTANSAGQ KPRKSKNSPP
EISGKKSDYV IPISDADQVG LTVGKLEASD ADGDELWWSI SSGDPDSVFD VRQDTGQLLL
AKKVELLKRG ELRLNISVTD GQAWDHSTVI IQVSRQISQR PKFSASHYQT DVSERVAVGT
QIYTLKASGE SLGTKPLVFN LFSVDDVAME DKIRVEPSSG NVIVMEPLDY EAARRIRAVV
QVQQANMKSF ATFSVNINDE NDNSPYFVGH TAFAFVDESD TVDDVLATVT AFDKDRGENG
IVTYSIVSGN EESLFKIDAK SGEVRLAKPL DPELQHVESI LRIRAIDSAA NSLKDEMSLH
IRNSNEAPET AKFDRKVYQT TLYDSTRPGT PVLVLNALHH GTVSYKLEPN CTFFEVHTLS
GAVHLATWLT KLKHRKSVEC TAIVESTEGQ QDIAKVIAKI IRTNQHSPIF RRQVYRGTIR
ENMPTGSSVL SKSLLPLVVS AIDEDPGSNG LVGYRMLSPK DEQMFSVDQY SGAIRTQMSF
DFEKMKEYSF YVQAFDMGQP PRRSLMPSLI VVTVIDENDE PPRFPSNSLD ISMILPTANG
VSVGGQTAQD MDSVGSLRYF IKDQSVPFSV DSKTGDVLVK DSNGISDMTK LFDLEVFVTD
GKQSASYVMK ISTISTENSK FKFTRNEYHT SLIENTTLPP GSIILSVATI GDKLDHFSIV
NPHEAFFIHP GTGVISSSGI ALDREKSAII RLVVQAKSHE KNPVMARALV VVGIENINDE
TPIFMGTPYD ITIGHSDIGT VVLEPKVIDN DEGDVVTISS ENMPEYFKIV GGKVVLGKKL
PSIEEEDLEF NFKLIAKDNG SVHRVEEPVK IRVVDKARPV FSQNVYTAVI SKESTKKSTV
LVKVMAKSSL QSKSKGLIGY RILDKKSPFS VDFLTGEVRL NNLKMLAETN YTFEVEAREV
TRPKMIAKAQ VEIIVKSGIT THAPVFEKLK YTASTPESTS IGQRLLTIKA TTSDENDTIE
YSLSGSKDIE IHPETGDVTI TGQLDYEKTQ KYDLKLVATS SGKQVSSEAE FIVLIEDVND
EMPEFIRSDV SAKISDSAIT GQFITIMSAT DMDTTNSLDE ESQKLLYKIV DGDETLFNIS
PATGELSLAR PVEQDDLVNE DTKKVLNVSV TDGMFTAYAK LVVEILRSGS MQPPPRFEQS
HYVANALENT IVNKSALLTV AVKGGVPPLQ FSLAPTTSSN SSTSKEAWPV AIDRKTGRIH
VSRVLNYHRD KRYQIPLVVE DATGRRAFST LTLSVIDIND KPPFFVLPFY STSISESAKE
GDTVMMVSAT DDDENDTIEY SLLDGSESQF FSVHPRQGTI TVAKKLEHKA GVTLSLTIKA
TDSANPPHHA TTTVEVNIAS ESVKVPRFSN SHYLFSVMED ADVGNVIGRV QQMETEIDEI
RFTIVPGSEE SDSFLPFSVE RSTGKIIVKS SLDRERKNQW KMTIRADAAG GVHAITTVTV
DIGDVNDNAP AFHGDYERFT ISEDAAVGTS VTIFSAMDRD DSPSGRIRFS LVEENPYFDL
NENSGWLTVA SQLDREKIDH YKLIARATDE GGFNTDLPFT IVVSDVNDSP PQFEKEEFNI
DLHLPSTSPI LHFSIKDDDL SPNNVSQFFI PKGNEEGVFW IDSNNDLLLK RPEIVENKMQ
YQLKVTAFDG VFETSTKVKI NLKSSKDSDI RCPEANKTVI LAENSKKGTV VLGESSLLGP
NVTFKLSDND GNVFVVNFRN GIVKVKESDQ IDYEKNQQLE FHRLTIQDNS EVCKELITVV
IENLNDNRPK IIEKLLKVSI DENLPTSEDA RQYITRIVAE DADFDEIKFR MVDDFGGLFQ
IDDINGVVTV VKPLDSEILG FFNLTVVASD GEFEDKATIL VTVIDQNDNA PTFEKSTYSM
KVMESESIGY ELAHFRASGG DQNETIEYYL KPSDVTSFVN LNAQTGILTL AKPLDFETLS
ALKLTVVAKD SGVPPLETEA QVEISVMDEN DNAPKFEKEK YVGKVKENSK SGEKVLTVKA
LDVDSEHFGA VSYELEIVSE TTTDTPVLPF AINSNGDVLI SQSIDYEKIK KYNLKVIAKD
GGRPPLRSEA LLEIHVEDEN DHAPTFDDCN MTALVQEGEA IGHRLLKFSV SDLDGPKNGA
PFTVEIQGDG AKSFKVNEKL ELLTAKKLEY RKKDKYLLTV IAKDVKGKTT DCPLTIFIRQ
TSRHAPTMKP MKIQINTLQN ELPEGIIGRL KASDEDEEDQ NGLLRFGLVE GSIQSPRAQV
QESRSTHLFR VDPNTGDIWS DHSITQGLHT FNVTVTDSKF NTVSYVEVHV TSIDNDVIDH
AVSIRIRSMS VDEFMRKHVK EFRRIISHHL NLNDDSSIQL ISVQAVPSTE SERRSRRNSM
EDVEILMTAQ RGLGRGYLKP DHIYSRLKND FQNMNDQSQR MRYQLITEMC TTGVCLRGEC
REVIELIEDS WTKVSTDDFS FVSPFHSRSA QCLCPDGFGG KRCEVETNQC AKSPCEQWQL
CIPSVHNSTY ECVCPLGMEG DKCSVPSCQN DGKCLEEAEL SVGGDGYFEI SLSNEIETRM
ELEIELKTTT HNGIIMWSRG KRDFHMLRLV NGTPEYHWNA GTGTGIVTSK TSVVDGQWHR
IAISRRQRRT RMTVDDEDLQ EAFSPIGSTV INLHRYSQKL VLGAKVDDGE LTDGVSACFR
TISVDGMKVL KTRQGMKLFG AQPGCSALTS SPCNDLPCQH AGTCISQGKS HFKCECPSRY
SGNVCEIDLE PCASSPCPTG IQCIPFYNDY LCKCPNGFTG KHCEARGFED HETSSCSKNV
CGTSGQCISI PRHSLESSDF ICNCTGGILQ STPCAEKSDI LSTVLEFLLK AEIVIVILGV
LLLLLVFCLT FITWKCCKKN RDPKYGAHCD VPHMRNTRVL VPVVPPPLPP RGFRNDSSNF
ISTSSVTTSH RPMVQVKPYS SDIRDSRSPS ACGSSKGTRR DPLPSDKFRR VDETANRIRH
SDRKDPRGDV LSSLRDSSDE WMGIDDRIDS SLKYSRAAAG TVIVGDTELM PVINDNDYMT
MKPRKDKNFE REKPPAIPAH ATPLESVLKL GSSSSGEEAP RNALYDDPIS LDSQTFDDID
EEVNIHIS
