UNC5A_HUMAN
ID UNC5A_HUMAN Reviewed; 842 AA.
AC Q6ZN44; B2RXE6; Q8TF26; Q96GP4;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Netrin receptor UNC5A;
DE AltName: Full=Protein unc-5 homolog 1;
DE AltName: Full=Protein unc-5 homolog A;
DE Flags: Precursor;
GN Name=UNC5A; Synonyms=KIAA1976, UNC5H1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-404 (ISOFORM 3), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 302-842 (ISOFORMS 1/2/3).
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 624-728.
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII. The
RT complete sequences of 50 new cDNA clones which code for large proteins.";
RL DNA Res. 8:319-327(2001).
RN [5]
RP INDUCTION.
RX PubMed=12598906; DOI=10.1038/ncb943;
RA Tanikawa C., Matsuda K., Fukuda S., Nakamura Y., Arakawa H.;
RT "p53RDL1 regulates of p53-dependent apoptosis.";
RL Nat. Cell Biol. 5:216-223(2003).
RN [6]
RP DOWN-REGULATION IN CANCER.
RX PubMed=12655055; DOI=10.1073/pnas.0738063100;
RA Thiebault K., Mazelin L., Pays L., Llambi F., Joly M.-O., Scoazec J.-Y.,
RA Saurin J.-C., Romeo G., Mehlen P.;
RT "The netrin-1 receptors UNC5H are putative tumor suppressors controlling
RT cell death commitment.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4173-4178(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-303, DISULFIDE BONDS,
RP GLYCOSYLATION AT ASN-218, AND INTERACTION WITH FLRT2.
RX PubMed=25374360; DOI=10.1016/j.neuron.2014.10.008;
RA Seiradake E., del Toro D., Nagel D., Cop F., Haertl R., Ruff T.,
RA Seyit-Bremer G., Harlos K., Border E.C., Acker-Palmer A., Jones E.Y.,
RA Klein R.;
RT "FLRT structure: balancing repulsion and cell adhesion in cortical and
RT vascular development.";
RL Neuron 84:370-385(2014).
CC -!- FUNCTION: Receptor for netrin required for axon guidance. Functions in
CC the netrin signaling pathway and promotes neurite outgrowth in response
CC to NTN1. Mediates axon repulsion of neuronal growth cones in the
CC developing nervous system in response to netrin. Axon repulsion in
CC growth cones may be mediated by its association with DCC that may
CC trigger signaling for repulsion. It also acts as a dependence receptor
CC required for apoptosis induction when not associated with netrin
CC ligand. {ECO:0000250|UniProtKB:O08721}.
CC -!- SUBUNIT: Homodimer and homooligomer. Interacts with the cytoplasmic
CC part of DCC. Interacts with MAGED1. Interacts with PRKCABP, possibly
CC mediating some interaction with PKC (By similarity). Interacts (via
CC extracellular domain) with FLRT2 (via extracellular domain)
CC (PubMed:25374360). Interacts (via extracellular domain) with FLRT3 (via
CC extracellular domain) (By similarity). {ECO:0000250|UniProtKB:O08721,
CC ECO:0000250|UniProtKB:Q8K1S4, ECO:0000269|PubMed:25374360}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O08721};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:O08721}.
CC Membrane raft {ECO:0000250|UniProtKB:O08721}. Cell projection, neuron
CC projection {ECO:0000250|UniProtKB:O08721}. Note=The interaction with
CC PRKCABP regulates its surface expression and leads to its removal from
CC the surface of neurons and growth cones.
CC {ECO:0000250|UniProtKB:O08721}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6ZN44-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZN44-2; Sequence=VSP_011694, VSP_011695;
CC Name=3;
CC IsoId=Q6ZN44-3; Sequence=VSP_011693;
CC -!- INDUCTION: By p53/TP53. {ECO:0000269|PubMed:12598906}.
CC -!- DOMAIN: The ZU5 domain mediates the interaction with MAGED1, which
CC participates in the induction of apoptosis.
CC {ECO:0000250|UniProtKB:O08721}.
CC -!- PTM: Phosphorylated on cytoplasmic tyrosine residues (By similarity).
CC Phosphorylated by PKC in vitro (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:O08721}.
CC -!- PTM: Proteolytically cleaved by caspases during apoptosis. The cleavage
CC does not take place when the receptor is associated with netrin ligand.
CC Its cleavage by caspases is required to induce apoptosis.
CC {ECO:0000250|UniProtKB:O08721}.
CC -!- MISCELLANEOUS: Down-regulated in multiple cancers including colorectal,
CC breast, ovary, uterus, stomach, lung, or kidney cancers.
CC {ECO:0000269|PubMed:12655055}.
CC -!- SIMILARITY: Belongs to the unc-5 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB85562.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AK131380; BAD18531.1; -; mRNA.
DR EMBL; AC027318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009333; AAH09333.2; -; mRNA.
DR EMBL; BC033727; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC157824; AAI57825.1; -; mRNA.
DR EMBL; AB075856; BAB85562.1; ALT_SEQ; mRNA.
DR CCDS; CCDS34299.1; -. [Q6ZN44-1]
DR RefSeq; NP_588610.2; NM_133369.2. [Q6ZN44-1]
DR PDB; 4V2A; X-ray; 2.40 A; A=1-303.
DR PDBsum; 4V2A; -.
DR AlphaFoldDB; Q6ZN44; -.
DR SMR; Q6ZN44; -.
DR BioGRID; 124683; 11.
DR IntAct; Q6ZN44; 1.
DR STRING; 9606.ENSP00000332737; -.
DR GlyGen; Q6ZN44; 3 sites.
DR iPTMnet; Q6ZN44; -.
DR PhosphoSitePlus; Q6ZN44; -.
DR BioMuta; UNC5A; -.
DR DMDM; 296453000; -.
DR MassIVE; Q6ZN44; -.
DR PaxDb; Q6ZN44; -.
DR PeptideAtlas; Q6ZN44; -.
DR PRIDE; Q6ZN44; -.
DR ProteomicsDB; 67973; -. [Q6ZN44-1]
DR ProteomicsDB; 67974; -. [Q6ZN44-2]
DR ProteomicsDB; 67975; -. [Q6ZN44-3]
DR Antibodypedia; 29143; 110 antibodies from 28 providers.
DR DNASU; 90249; -.
DR Ensembl; ENST00000329542.9; ENSP00000332737.4; ENSG00000113763.12. [Q6ZN44-1]
DR GeneID; 90249; -.
DR KEGG; hsa:90249; -.
DR MANE-Select; ENST00000329542.9; ENSP00000332737.4; NM_133369.3; NP_588610.2.
DR UCSC; uc003mey.4; human. [Q6ZN44-1]
DR CTD; 90249; -.
DR DisGeNET; 90249; -.
DR GeneCards; UNC5A; -.
DR HGNC; HGNC:12567; UNC5A.
DR HPA; ENSG00000113763; Tissue enhanced (brain, pituitary gland).
DR MIM; 607869; gene.
DR neXtProt; NX_Q6ZN44; -.
DR OpenTargets; ENSG00000113763; -.
DR PharmGKB; PA37204; -.
DR VEuPathDB; HostDB:ENSG00000113763; -.
DR eggNOG; KOG1480; Eukaryota.
DR GeneTree; ENSGT00950000182815; -.
DR HOGENOM; CLU_014383_0_0_1; -.
DR InParanoid; Q6ZN44; -.
DR OMA; QKSACTT; -.
DR OrthoDB; 334938at2759; -.
DR PhylomeDB; Q6ZN44; -.
DR TreeFam; TF316767; -.
DR PathwayCommons; Q6ZN44; -.
DR Reactome; R-HSA-373752; Netrin-1 signaling.
DR Reactome; R-HSA-418886; Netrin mediated repulsion signals.
DR Reactome; R-HSA-418889; Caspase activation via Dependence Receptors in the absence of ligand.
DR SignaLink; Q6ZN44; -.
DR SIGNOR; Q6ZN44; -.
DR BioGRID-ORCS; 90249; 13 hits in 1065 CRISPR screens.
DR ChiTaRS; UNC5A; human.
DR GeneWiki; UNC5A; -.
DR GenomeRNAi; 90249; -.
DR Pharos; Q6ZN44; Tbio.
DR PRO; PR:Q6ZN44; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q6ZN44; protein.
DR Bgee; ENSG00000113763; Expressed in endothelial cell and 97 other tissues.
DR ExpressionAtlas; Q6ZN44; baseline and differential.
DR Genevisible; Q6ZN44; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0032589; C:neuron projection membrane; ISS:UniProtKB.
DR GO; GO:0032809; C:neuronal cell body membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005042; F:netrin receptor activity; IBA:GO_Central.
DR GO; GO:0033564; P:anterior/posterior axon guidance; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0038007; P:netrin-activated signaling pathway; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR CDD; cd08800; Death_UNC5A; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 2.20.100.10; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR042155; Death_UNC5A.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR037936; UNC5.
DR InterPro; IPR033772; UPA.
DR InterPro; IPR000906; ZU5_dom.
DR PANTHER; PTHR12582; PTHR12582; 2.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF17217; UPA; 1.
DR Pfam; PF00791; ZU5; 1.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00209; TSP1; 1.
DR SMART; SM00218; ZU5; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF48726; SSF48726; 2.
DR SUPFAM; SSF82895; SSF82895; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50092; TSP1; 1.
DR PROSITE; PS51145; ZU5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cell membrane;
KW Cell projection; Developmental protein; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..842
FT /note="Netrin receptor UNC5A"
FT /id="PRO_0000036068"
FT TOPO_DOM 26..306
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..842
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 44..141
FT /note="Ig-like"
FT DOMAIN 155..234
FT /note="Ig-like C2-type"
FT DOMAIN 242..294
FT /note="TSP type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 441..584
FT /note="ZU5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT DOMAIN 761..841
FT /note="Death"
FT REGION 605..623
FT /note="Interaction with DCC"
FT /evidence="ECO:0000250"
FT SITE 340..341
FT /note="Cleavage; by caspase-3"
FT /evidence="ECO:0000250|UniProtKB:O08721"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0007744|PDB:4V2A"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 65..126
FT /evidence="ECO:0007744|PDB:4V2A"
FT DISULFID 77..124
FT /evidence="ECO:0007744|PDB:4V2A"
FT DISULFID 170..221
FT /evidence="ECO:0007744|PDB:4V2A"
FT DISULFID 254..288
FT /evidence="ECO:0007744|PDB:4V2A"
FT DISULFID 258..293
FT /evidence="ECO:0007744|PDB:4V2A"
FT DISULFID 266..278
FT /evidence="ECO:0007744|PDB:4V2A"
FT VAR_SEQ 1..97
FT /note="MAVRPGLWPALLGIVLAAWLRGSGAQQSATVANPVPGANPDLLPHFLVEPED
FT VYIVKNKPVLLVCKAVPATQIFFKCNGEWVRQVDHVIERSTDGSS -> MAGTSERSLI
FT SSISQPKAIECFEVKKKAFLTHGRYHGSGATPPKTKDPKPETFCGQT (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011693"
FT VAR_SEQ 296..301
FT /note="TASGPE -> SESSLP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011694"
FT VAR_SEQ 302..842
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011695"
FT CONFLICT 97
FT /note="S -> N (in Ref. 1; BAD18531)"
FT /evidence="ECO:0000305"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:4V2A"
FT STRAND 61..69
FT /evidence="ECO:0007829|PDB:4V2A"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:4V2A"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:4V2A"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:4V2A"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:4V2A"
FT STRAND 100..108
FT /evidence="ECO:0007829|PDB:4V2A"
FT HELIX 110..115
FT /evidence="ECO:0007829|PDB:4V2A"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:4V2A"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:4V2A"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:4V2A"
FT STRAND 158..163
FT /evidence="ECO:0007829|PDB:4V2A"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:4V2A"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:4V2A"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:4V2A"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:4V2A"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:4V2A"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:4V2A"
FT STRAND 216..224
FT /evidence="ECO:0007829|PDB:4V2A"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:4V2A"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:4V2A"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:4V2A"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:4V2A"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:4V2A"
SQ SEQUENCE 842 AA; 92932 MW; 7B209042977FE524 CRC64;
MAVRPGLWPA LLGIVLAAWL RGSGAQQSAT VANPVPGANP DLLPHFLVEP EDVYIVKNKP
VLLVCKAVPA TQIFFKCNGE WVRQVDHVIE RSTDGSSGLP TMEVRINVSR QQVEKVFGLE
EYWCQCVAWS SSGTTKSQKA YIRIAYLRKN FEQEPLAKEV SLEQGIVLPC RPPEGIPPAE
VEWLRNEDLV DPSLDPNVYI TREHSLVVRQ ARLADTANYT CVAKNIVARR RSASAAVIVY
VDGSWSPWSK WSACGLDCTH WRSRECSDPA PRNGGEECQG TDLDTRNCTS DLCVHTASGP
EDVALYVGLI AVAVCLVLLL LVLILVYCRK KEGLDSDVAD SSILTSGFQP VSIKPSKADN
PHLLTIQPDL STTTTTYQGS LCPRQDGPSP KFQLTNGHLL SPLGGGRHTL HHSSPTSEAE
EFVSRLSTQN YFRSLPRGTS NMTYGTFNFL GGRLMIPNTG ISLLIPPDAI PRGKIYEIYL
TLHKPEDVRL PLAGCQTLLS PIVSCGPPGV LLTRPVILAM DHCGEPSPDS WSLRLKKQSC
EGSWEDVLHL GEEAPSHLYY CQLEASACYV FTEQLGRFAL VGEALSVAAA KRLKLLLFAP
VACTSLEYNI RVYCLHDTHD ALKEVVQLEK QLGGQLIQEP RVLHFKDSYH NLRLSIHDVP
SSLWKSKLLV SYQEIPFYHI WNGTQRYLHC TFTLERVSPS TSDLACKLWV WQVEGDGQSF
SINFNITKDT RFAELLALES EAGVPALVGP SAFKIPFLIR QKIISSLDPP CRRGADWRTL
AQKLHLDSHL SFFASKPSPT AMILNLWEAR HFPNGNLSQL AAAVAGLGQP DAGLFTVSEA
EC
