PCDH1_HUMAN
ID PCDH1_HUMAN Reviewed; 1060 AA.
AC Q08174; Q8IUP2;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Protocadherin-1;
DE AltName: Full=Cadherin-like protein 1;
DE AltName: Full=Protocadherin-42;
DE Short=PC42;
DE Flags: Precursor;
GN Name=PCDH1;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [MRNA] OF 10-1060 (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 980-1060 (ISOFORM 2), AND VARIANT PRO-25.
RC TISSUE=Brain;
RX PubMed=8508762; DOI=10.1002/j.1460-2075.1993.tb05878.x;
RA Sano K., Tanihara H., Heimark R.L., Obata S., Davidson M., St John T.,
RA Taketani S., Suzuki S.;
RT "Protocadherins: a large family of cadherin-related molecules in central
RT nervous system.";
RL EMBO J. 12:2249-2256(1993).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-949 AND SER-962, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-305; ASN-813 AND ASN-818.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-918; SER-962 AND SER-984, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1173 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May be involved in cell-cell interaction processes and in
CC cell adhesion.
CC -!- SUBCELLULAR LOCATION: Cell junction. Cell membrane {ECO:0000305};
CC Single-pass type I membrane protein {ECO:0000305}. Note=Found at cell-
CC cell boundaries and probably at cell-matrix boundaries.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q08174-1; Sequence=Displayed;
CC Name=2; Synonyms=PC42-8;
CC IsoId=Q08174-2; Sequence=VSP_000703;
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain and neuro-glial
CC cells.
CC -!- DEVELOPMENTAL STAGE: Highest expression in adults.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-23 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36419.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AC094107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61902.1; -; Genomic_DNA.
DR EMBL; BC035812; AAH35812.1; -; mRNA.
DR EMBL; L11369; AAA36418.1; -; mRNA.
DR EMBL; L11370; AAA36419.1; ALT_SEQ; mRNA.
DR CCDS; CCDS4267.1; -. [Q08174-2]
DR CCDS; CCDS43375.1; -. [Q08174-1]
DR RefSeq; NP_001265542.1; NM_001278613.1.
DR RefSeq; NP_001265544.1; NM_001278615.1.
DR RefSeq; NP_002578.2; NM_002587.4. [Q08174-1]
DR RefSeq; NP_115796.2; NM_032420.3. [Q08174-2]
DR PDB; 6BX7; X-ray; 2.85 A; A=58-503.
DR PDB; 6MGA; X-ray; 3.15 A; A=58-503.
DR PDB; 6PIM; X-ray; 3.05 A; A=271-503.
DR PDB; 6VFP; X-ray; 3.20 A; A=58-498.
DR PDBsum; 6BX7; -.
DR PDBsum; 6MGA; -.
DR PDBsum; 6PIM; -.
DR PDBsum; 6VFP; -.
DR AlphaFoldDB; Q08174; -.
DR SMR; Q08174; -.
DR BioGRID; 111130; 110.
DR IntAct; Q08174; 14.
DR MINT; Q08174; -.
DR STRING; 9606.ENSP00000287008; -.
DR GlyGen; Q08174; 6 sites.
DR iPTMnet; Q08174; -.
DR PhosphoSitePlus; Q08174; -.
DR BioMuta; PCDH1; -.
DR DMDM; 215273864; -.
DR CPTAC; CPTAC-1310; -.
DR EPD; Q08174; -.
DR jPOST; Q08174; -.
DR MassIVE; Q08174; -.
DR MaxQB; Q08174; -.
DR PaxDb; Q08174; -.
DR PeptideAtlas; Q08174; -.
DR PRIDE; Q08174; -.
DR ProteomicsDB; 58575; -. [Q08174-1]
DR ProteomicsDB; 58576; -. [Q08174-2]
DR Antibodypedia; 27376; 321 antibodies from 28 providers.
DR DNASU; 5097; -.
DR Ensembl; ENST00000287008.8; ENSP00000287008.3; ENSG00000156453.14. [Q08174-2]
DR Ensembl; ENST00000394536.4; ENSP00000378043.3; ENSG00000156453.14. [Q08174-1]
DR GeneID; 5097; -.
DR KEGG; hsa:5097; -.
DR MANE-Select; ENST00000287008.8; ENSP00000287008.3; NM_032420.5; NP_115796.2. [Q08174-2]
DR UCSC; uc003llp.4; human. [Q08174-1]
DR CTD; 5097; -.
DR DisGeNET; 5097; -.
DR GeneCards; PCDH1; -.
DR HGNC; HGNC:8655; PCDH1.
DR HPA; ENSG00000156453; Low tissue specificity.
DR MIM; 603626; gene.
DR neXtProt; NX_Q08174; -.
DR OpenTargets; ENSG00000156453; -.
DR PharmGKB; PA32994; -.
DR VEuPathDB; HostDB:ENSG00000156453; -.
DR eggNOG; ENOG502QWB7; Eukaryota.
DR GeneTree; ENSGT00940000155521; -.
DR HOGENOM; CLU_006480_5_3_1; -.
DR InParanoid; Q08174; -.
DR OMA; NASYKHI; -.
DR OrthoDB; 97260at2759; -.
DR PhylomeDB; Q08174; -.
DR TreeFam; TF320624; -.
DR PathwayCommons; Q08174; -.
DR SignaLink; Q08174; -.
DR BioGRID-ORCS; 5097; 69 hits in 1079 CRISPR screens.
DR ChiTaRS; PCDH1; human.
DR GeneWiki; PCDH1; -.
DR GenomeRNAi; 5097; -.
DR Pharos; Q08174; Tbio.
DR PRO; PR:Q08174; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q08174; protein.
DR Bgee; ENSG00000156453; Expressed in lower esophagus mucosa and 176 other tissues.
DR ExpressionAtlas; Q08174; baseline and differential.
DR Genevisible; Q08174; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005911; C:cell-cell junction; TAS:ProtInc.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR InterPro; IPR013585; Protocadherin.
DR Pfam; PF00028; Cadherin; 6.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF08374; Protocadherin; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 6.
DR PROSITE; PS50268; CADHERIN_2; 7.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell junction;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..57
FT /evidence="ECO:0000255"
FT CHAIN 58..1060
FT /note="Protocadherin-1"
FT /id="PRO_0000354078"
FT TOPO_DOM 58..852
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 853..873
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 874..1060
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 58..168
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 169..280
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 281..387
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 396..506
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 507..612
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 613..715
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 718..844
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 884..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 884..898
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1041
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 918
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 949
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 962
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 984
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 813
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 818
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VAR_SEQ 1034..1060
FT /note="VGQPFQLSTPQPLPHPYHGAIWTEVWE -> LPHRRVTFSATSQAQELQDPS
FT QHSYYDSGLEESETPSSKSSSGPRLGPLALPEDHYERTTPDGSIGEMEHPENDLRPLPD
FT VAMTGTCTRECSEFGHSDTCWMPGQSSPSRRTKSSALKLSTFVPYQDRGGQEPAGAGSP
FT SPPEDRNTKTAPVRLLPSYSAFSHSSHDSCKDSATLEEIPLTQTSDFPPAATPASAQTA
FT KREIYL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8508762"
FT /id="VSP_000703"
FT VARIANT 15
FT /note="L -> F (in dbSNP:rs12517385)"
FT /id="VAR_047530"
FT VARIANT 25
FT /note="H -> P (in dbSNP:rs12515587)"
FT /evidence="ECO:0000269|PubMed:8508762"
FT /id="VAR_047531"
FT VARIANT 514
FT /note="A -> T (in dbSNP:rs3822357)"
FT /id="VAR_047532"
FT CONFLICT 147
FT /note="G -> A (in Ref. 4; AAA36419)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="S -> T (in Ref. 4; AAA36419)"
FT /evidence="ECO:0000305"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:6BX7"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:6VFP"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:6BX7"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:6BX7"
FT TURN 103..106
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:6BX7"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:6BX7"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:6VFP"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 150..159
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 169..178
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:6BX7"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:6BX7"
FT HELIX 211..214
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:6BX7"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 245..258
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 261..271
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 279..290
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:6BX7"
FT HELIX 310..312
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:6BX7"
FT HELIX 324..329
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:6BX7"
FT TURN 334..336
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:6BX7"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 351..361
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 368..378
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 386..390
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 413..420
FT /evidence="ECO:0007829|PDB:6BX7"
FT HELIX 425..428
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 439..444
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:6MGA"
FT STRAND 453..462
FT /evidence="ECO:0007829|PDB:6BX7"
FT TURN 466..468
FT /evidence="ECO:0007829|PDB:6VFP"
FT STRAND 472..479
FT /evidence="ECO:0007829|PDB:6BX7"
FT STRAND 487..495
FT /evidence="ECO:0007829|PDB:6BX7"
FT MOD_RES Q08174-2:1173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CONFLICT Q08174-2:1156
FT /note="V -> M (in Ref. 4; AAA36418)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1060 AA; 114743 MW; 0F4F24F3EE607D04 CRC64;
MDSGAGGRRC PEAALLILGP PRMEHLRHSP GPGGQRLLLP SMLLALLLLL APSPGHATRV
VYKVPEEQPP NTLIGSLAAD YGFPDVGHLY KLEVGAPYLR VDGKTGDIFT TETSIDREGL
RECQNQLPGD PCILEFEVSI TDLVQNGSPR LLEGQIEVQD INDNTPNFAS PVITLAIPEN
TNIGSLFPIP LASDRDAGPN GVASYELQAG PEAQELFGLQ VAEDQEEKQP QLIVMGNLDR
ERWDSYDLTI KVQDGGSPPR ASSALLRVTV LDTNDNAPKF ERPSYEAELS ENSPIGHSVI
QVKANDSDQG ANAEIEYTFH QAPEVVRRLL RLDRNTGLIT VQGPVDREDL STLRFSVLAK
DRGTNPKSAR AQVVVTVKDM NDNAPTIEIR GIGLVTHQDG MANISEDVAE ETAVALVQVS
DRDEGENAAV TCVVAGDVPF QLRQASETGS DSKKKYFLQT TTPLDYEKVK DYTIEIVAVD
SGNPPLSSTN SLKVQVVDVN DNAPVFTQSV TEVAFPENNK PGEVIAEITA SDADSGSNAE
LVYSLEPEPA AKGLFTISPE TGEIQVKTSL DREQRESYEL KVVAADRGSP SLQGTATVLV
NVLDCNDNDP KFMLSGYNFS VMENMPALSP VGMVTVIDGD KGENAQVQLS VEQDNGDFVI
QNGTGTILSS LSFDREQQST YTFQLKAVDG GVPPRSAYVG VTINVLDEND NAPYITAPSN
TSHKLLTPQT RLGETVSQVA AEDFDSGVNA ELIYSIAGGN PYGLFQIGSH SGAITLEKEI
ERRHHGLHRL VVKVSDRGKP PRYGTALVHL YVNETLANRT LLETLLGHSL DTPLDIDIAG
DPEYERSKQR GNILFGVVAG VVAVALLIAL AVLVRYCRQR EAKSGYQAGK KETKDLYAPK
PSGKASKGNK SKGKKSKSPK PVKPVEDEDE AGLQKSLKFN LMSDAPGDSP RIHLPLNYPP
GSPDLGRHYR SNSPLPSIQL QPQSPSASKK HQVVQDLPPA NTFVGTGDTT STGSEQYSDY
SYRTNPPKYP SKQVGQPFQL STPQPLPHPY HGAIWTEVWE
