MCTP1_HUMAN
ID MCTP1_HUMAN Reviewed; 999 AA.
AC Q6DN14; Q6DN13; Q8N2W1; Q8NBA2; Q96LX0; Q9H6E8;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Multiple C2 and transmembrane domain-containing protein 1;
GN Name=MCTP1;
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 [MRNA] (ISOFORMS 1 AND 2), AND COFACTOR.
RX PubMed=15528213; DOI=10.1074/jbc.m407305200;
RA Shin O.H., Han W., Wang Y., Sudhof T.C.;
RT "Evolutionarily conserved multiple C2 domain proteins with two
RT transmembrane regions (MCTPs) and unusual Ca2+ binding properties.";
RL J. Biol. Chem. 280:1641-1651(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 639-999 (ISOFORM 3), AND VARIANT LYS-612.
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT LYS-612.
RC TISSUE=Ovary;
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).
CC -!- FUNCTION: Calcium sensor which is essential for the stabilization of
CC normal baseline neurotransmitter release and for the induction and
CC long-term maintenance of presynaptic homeostatic plasticity.
CC {ECO:0000250|UniProtKB:A1ZBD6}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041,
CC ECO:0000269|PubMed:15528213};
CC Note=Binds Ca(2+) via the C2 domains in absence of phospholipids.
CC {ECO:0000269|PubMed:15528213};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:D4ABL6}; Multi-pass membrane
CC protein {ECO:0000255}. Recycling endosome
CC {ECO:0000250|UniProtKB:D4ABL6}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:A1ZBD6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=MCTP1L;
CC IsoId=Q6DN14-1; Sequence=Displayed;
CC Name=2; Synonyms=MCTP1S;
CC IsoId=Q6DN14-2; Sequence=VSP_026656, VSP_026657;
CC Name=3;
CC IsoId=Q6DN14-3; Sequence=VSP_026656, VSP_026657, VSP_026658,
CC VSP_026659;
CC Name=4;
CC IsoId=Q6DN14-4; Sequence=VSP_026656, VSP_026657, VSP_026660,
CC VSP_026661;
CC Name=5;
CC IsoId=Q6DN14-5; Sequence=VSP_026655;
CC -!- SIMILARITY: Belongs to the MCTP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY656715; AAT73058.1; -; mRNA.
DR EMBL; AY656716; AAT73059.1; -; mRNA.
DR EMBL; AK025997; BAB15311.1; -; mRNA.
DR EMBL; AK057694; BAB71547.1; -; mRNA.
DR EMBL; AK091330; BAC03637.1; -; mRNA.
DR EMBL; AC008534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC008573; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC012312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC099507; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030005; AAH30005.1; -; mRNA.
DR CCDS; CCDS34203.1; -. [Q6DN14-1]
DR CCDS; CCDS47247.1; -. [Q6DN14-2]
DR CCDS; CCDS75275.1; -. [Q6DN14-3]
DR RefSeq; NP_001002796.1; NM_001002796.3. [Q6DN14-2]
DR RefSeq; NP_001284706.1; NM_001297777.1. [Q6DN14-3]
DR RefSeq; NP_078993.4; NM_024717.5. [Q6DN14-1]
DR AlphaFoldDB; Q6DN14; -.
DR SMR; Q6DN14; -.
DR BioGRID; 122875; 6.
DR IntAct; Q6DN14; 1.
DR STRING; 9606.ENSP00000424126; -.
DR iPTMnet; Q6DN14; -.
DR PhosphoSitePlus; Q6DN14; -.
DR BioMuta; MCTP1; -.
DR DMDM; 300669650; -.
DR EPD; Q6DN14; -.
DR jPOST; Q6DN14; -.
DR MassIVE; Q6DN14; -.
DR MaxQB; Q6DN14; -.
DR PaxDb; Q6DN14; -.
DR PeptideAtlas; Q6DN14; -.
DR PRIDE; Q6DN14; -.
DR ProteomicsDB; 66243; -. [Q6DN14-1]
DR ProteomicsDB; 66244; -. [Q6DN14-2]
DR ProteomicsDB; 66245; -. [Q6DN14-3]
DR ProteomicsDB; 66246; -. [Q6DN14-4]
DR ProteomicsDB; 66247; -. [Q6DN14-5]
DR Antibodypedia; 2751; 62 antibodies from 13 providers.
DR DNASU; 79772; -.
DR Ensembl; ENST00000312216.12; ENSP00000308957.8; ENSG00000175471.20. [Q6DN14-2]
DR Ensembl; ENST00000429576.6; ENSP00000391639.2; ENSG00000175471.20. [Q6DN14-3]
DR Ensembl; ENST00000505078.5; ENSP00000426417.1; ENSG00000175471.20. [Q6DN14-5]
DR Ensembl; ENST00000505208.5; ENSP00000426438.1; ENSG00000175471.20. [Q6DN14-4]
DR Ensembl; ENST00000515393.6; ENSP00000424126.1; ENSG00000175471.20. [Q6DN14-1]
DR GeneID; 79772; -.
DR KEGG; hsa:79772; -.
DR MANE-Select; ENST00000515393.6; ENSP00000424126.1; NM_024717.7; NP_078993.4.
DR UCSC; uc003kku.4; human. [Q6DN14-1]
DR CTD; 79772; -.
DR DisGeNET; 79772; -.
DR GeneCards; MCTP1; -.
DR HGNC; HGNC:26183; MCTP1.
DR HPA; ENSG00000175471; Tissue enhanced (bone).
DR MIM; 616296; gene.
DR neXtProt; NX_Q6DN14; -.
DR OpenTargets; ENSG00000175471; -.
DR PharmGKB; PA142671472; -.
DR VEuPathDB; HostDB:ENSG00000175471; -.
DR eggNOG; KOG1030; Eukaryota.
DR GeneTree; ENSGT00940000156031; -.
DR HOGENOM; CLU_011170_1_1_1; -.
DR InParanoid; Q6DN14; -.
DR OMA; DCGPTLE; -.
DR PhylomeDB; Q6DN14; -.
DR TreeFam; TF323373; -.
DR PathwayCommons; Q6DN14; -.
DR SignaLink; Q6DN14; -.
DR BioGRID-ORCS; 79772; 26 hits in 1081 CRISPR screens.
DR ChiTaRS; MCTP1; human.
DR GenomeRNAi; 79772; -.
DR Pharos; Q6DN14; Tbio.
DR PRO; PR:Q6DN14; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q6DN14; protein.
DR Bgee; ENSG00000175471; Expressed in secondary oocyte and 165 other tissues.
DR ExpressionAtlas; Q6DN14; baseline and differential.
DR Genevisible; Q6DN14; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:HGNC-UCL.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:HGNC-UCL.
DR GO; GO:0019722; P:calcium-mediated signaling; NAS:HGNC-UCL.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0045806; P:negative regulation of endocytosis; ISS:UniProtKB.
DR GO; GO:1902883; P:negative regulation of response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; ISS:UniProtKB.
DR GO; GO:0046928; P:regulation of neurotransmitter secretion; ISS:UniProtKB.
DR Gene3D; 2.60.40.150; -; 3.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR013583; PRibTrfase_C.
DR Pfam; PF00168; C2; 3.
DR Pfam; PF08372; PRT_C; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR SMART; SM00239; C2; 3.
DR SUPFAM; SSF49562; SSF49562; 3.
DR PROSITE; PS50004; C2; 3.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cytoplasmic vesicle; Endoplasmic reticulum;
KW Endosome; Membrane; Metal-binding; Reference proteome; Repeat; Synapse;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..999
FT /note="Multiple C2 and transmembrane domain-containing
FT protein 1"
FT /id="PRO_0000294471"
FT TRANSMEM 811..831
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 914..934
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 242..360
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 452..569
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 603..724
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..223
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 277
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 277
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 332
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 338
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 486
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 486
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 492
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 539
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 539
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 541
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 541
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 547
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 642
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 642
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 648
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 694
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 694
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 696
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 696
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 702
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT VAR_SEQ 1..484
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026655"
FT VAR_SEQ 1..221
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:15528213"
FT /id="VSP_026656"
FT VAR_SEQ 222..240
FT /note="RSPAESRAPETGEEHGSSQ -> MLDSCKLKSACNLPFICNK (in
FT isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:15528213"
FT /id="VSP_026657"
FT VAR_SEQ 405..450
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026658"
FT VAR_SEQ 813..852
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026659"
FT VAR_SEQ 813..821
FT /note="LFLFVVWNF -> ALYGTFINV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026660"
FT VAR_SEQ 822..999
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026661"
FT VARIANT 612
FT /note="R -> K (in dbSNP:rs9885412)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_033189"
FT CONFLICT 195
FT /note="H -> R (in Ref. 1; AAT73058)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="P -> A (in Ref. 1; AAT73058)"
FT /evidence="ECO:0000305"
FT CONFLICT 727
FT /note="K -> R (in Ref. 2; BAB15311)"
FT /evidence="ECO:0000305"
FT CONFLICT 907
FT /note="N -> S (in Ref. 2; BAB15311)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 999 AA; 111624 MW; 7AF1FC0ACDB3F599 CRC64;
MEPRAAAAGE PEPPAASSSF QARLWKNLQL GVGRSKGGGG GRAGGPERRT ADTPSPSPPP
PVGTGNAPAR GSGAGSRWSG FKKRKQVLDR VFSSSQPNLC CSSPEPLEPG GAGRAEQGST
LRRRIREHLL PAVKGPAAAS GAAGGTPPGG RSPDSAPSSS SASSSLSSSP QPPPRGDRAR
DEGARRQGPG AHLCHQKSSS LPGTACLEQL LEPPPPPAEP ARSPAESRAP ETGEEHGSSQ
KIINTAGTSN AEVPLADPGM YQLDITLRRG QSLAARDRGG TSDPYVKFKI GGKEVFRSKI
IHKNLNPVWE EKACILVDHL REPLYIKVFD YDFGLQDDFM GSAFLDLTQL ELNRPTDVTL
TLKDPHYPDH DLGIILLSVI LTPKEGESRD VTMLMRKSWK RSSKELSENE VVGSYFSVKS
LFWRTCGRPA LPVLGFCRAE LQNPYCKNVQ FQTQSLRLSD LHRKSHLWRG IVSITLIEGR
DLKAMDSNGL SDPYVKFRLG HQKYKSKIMP KTLNPQWREQ FDFHLYEERG GVIDITAWDK
DAGKRDDFIG RCQVDLSALS REQTHKLELQ LEEGEGHLVL LVTLTASATV SISDLSVNSL
EDQKEREEIL KRYSPLRIFH NLKDVGFLQV KVIRAEGLMA ADVTGKSDPF CVVELNNDRL
LTHTVYKNLN PEWNKVFTFN IKDIHSVLEV TVYDEDRDRS ADFLGKVAIP LLSIQNGEQK
AYVLKNKQLT GPTKGVIYLE IDVIFNAVKA SLRTLIPKEQ KYIEEENRLS KQLLLRNFIR
MKRCVMVLVN AAYYVNSCFD WDSPPRSLAA FVLFLFVVWN FELYMIPLVL LLLLTWNYFL
IISGKDNRQR DTVVEDMLED EEEEDDKDDK DSEKKGFINK IYAIQEVCVS VQNILDEVAS
FGERIKNTFN WTVPFLSWLA IVALCVFTAI LYCIPLRYIV LVWGINKFTK KLRSPYAIDN
NELLDFLSRV PSDVQVVQYQ ELKPDPSHSP YKRKKNNLG