TRPC4_MOUSE
ID TRPC4_MOUSE Reviewed; 974 AA.
AC Q9QUQ5; Q62350; Q9QUQ9; Q9QZC0;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Short transient receptor potential channel 4;
DE Short=TrpC4;
DE AltName: Full=Capacitative calcium entry channel Trp4;
DE AltName: Full=Receptor-activated cation channel TRP4;
GN Name=Trpc4; Synonyms=Trrp4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
RC TISSUE=Brain;
RA Zhu X., Boulay G., Jiang M., Birnbaumer L.;
RT "Trp4 is involved in capacitative calcium entry in murine cells.";
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
RA Qian F., Philipson L.H.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
RC TISSUE=Brain;
RX PubMed=9512398;
RA Mori Y., Takada N., Okada T., Wakamori M., Imoto K., Wanifuchi H., Oka H.,
RA Oba A., Ikenaka K., Kurosaki T.;
RT "Differential distribution of TRP Ca2+ channel isoforms in mouse brain.";
RL NeuroReport 9:507-515(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
RX PubMed=10980202; DOI=10.1074/jbc.m006635200;
RA Tang Y., Tang J., Chen Z., Trost C., Flockerzi V., Li M., Ramesh V.,
RA Zhu M.X.;
RT "Association of mammalian trp4 and phospholipase C isozymes with a PDZ
RT domain-containing protein, NHERF.";
RL J. Biol. Chem. 275:37559-37564(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 505-642.
RC TISSUE=Brain;
RX PubMed=7575478; DOI=10.1042/bj3110041;
RA Petersen C.C.H., Berridge M.J., Borgese M.F., Bennett D.L.;
RT "Putative capacitative calcium entry channels: expression of Drosophila trp
RT and evidence for the existence of vertebrate homologues.";
RL Biochem. J. 311:41-44(1995).
RN [6]
RP FUNCTION.
RX PubMed=11175743; DOI=10.1038/35055019;
RA Freichel M., Suh S.H., Pfeifer A., Schweig U., Trost C., Weissgerber P.,
RA Biel M., Philipp S., Freise D., Droogmans G., Hofmann F., Flockerzi V.,
RA Nilius B.;
RT "Lack of an endothelial store-operated Ca2+ current impairs agonist-
RT dependent vasorelaxation in TRP4-/- mice.";
RL Nat. Cell Biol. 3:121-127(2001).
RN [7]
RP SUBUNIT.
RX PubMed=19070363; DOI=10.1016/j.ceca.2008.11.002;
RA Lepage P.K., Lussier M.P., McDuff F.O., Lavigne P., Boulay G.;
RT "The self-association of two N-terminal interaction domains plays an
RT important role in the tetramerization of TRPC4.";
RL Cell Calcium 45:251-259(2009).
RN [8]
RP INTERACTION WITH TRPC4AP.
RX PubMed=20458742; DOI=10.1002/jcp.22221;
RA Mace K.E., Lussier M.P., Boulay G., Terry-Powers J.L., Parfrey H.,
RA Perraud A.L., Riches D.W.H.;
RT "TRUSS, TNF-R1, and TRPC ion channels synergistically reverse endoplasmic
RT reticulum Ca2+ storage reduction in response to m1 muscarinic acetylcholine
RT receptor signaling.";
RL J. Cell. Physiol. 225:444-453(2010).
RN [9]
RP INTERACTION WITH PLSCR1.
RX PubMed=32110987; DOI=10.3390/cells9030547;
RA Guo J., Li J., Xia L., Wang Y., Zhu J., Du J., Lu Y., Liu G., Yao X.,
RA Shen B.;
RT "Transient Receptor Potential Canonical 5-Scramblase Signaling Complex
RT Mediates Neuronal Phosphatidylserine Externalization and Apoptosis.";
RL Cells 9:0-0(2020).
CC -!- FUNCTION: Thought to form a receptor-activated non-selective calcium
CC permeant cation channel. Probably is operated by a phosphatidylinositol
CC second messenger system activated by receptor tyrosine kinases or G-
CC protein coupled receptors. Acts as a cell-cell contact-dependent
CC endothelial calcium entry channel. Has also been shown to be calcium-
CC selective (By similarity). May also be activated by intracellular
CC calcium store depletion. Trpc4 deficient mice lack a store-operated
CC calcium entry in endothelial cells. {ECO:0000250,
CC ECO:0000269|PubMed:11175743}.
CC -!- SUBUNIT: Homotetramer (PubMed:19070363). Heterotetramer with TRPC1
CC and/or TRPC5 (By similarity). Isoform alpha but not isoform beta
CC interacts with ITPR1, ITPR2 and ITPR3 (By similarity). Interacts with
CC SLC9A3R1/NHERF (By similarity). Interacts with MX1 and RNF24 (By
CC similarity). Interacts (via CIRB domain) with SESTD1 (via the spectrin
CC 1 repeat) and SPTBN5 (via C-terminus) (By similarity). Interacts with
CC CDH5 and CTNNB1 (By similarity). Interacts (via protein 4.1-binding
CC domain) with EPB41L2 (By similarity). Interacts with TRPC4AP
CC (PubMed:20458742). Interacts with PLSCR1 (PubMed:32110987).
CC {ECO:0000250|UniProtKB:Q9UBN4, ECO:0000269|PubMed:19070363,
CC ECO:0000269|PubMed:20458742, ECO:0000269|PubMed:32110987}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Alpha;
CC IsoId=Q9QUQ5-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q9QUQ5-2; Sequence=VSP_006570;
CC -!- TISSUE SPECIFICITY: Abundantly expressed in brain (hippocampal CA1
CC pyramidal neurons, dentate gyrus granule cells, and cerebral cortical
CC neurons, and in the septal nuclei and the mitral layer of olfactory
CC bulb). Lower levels are detected in other tissues.
CC -!- SIMILARITY: Belongs to the transient receptor (TC 1.A.4) family. STrpC
CC subfamily. TRPC4 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF011543; AAD10167.1; -; mRNA.
DR EMBL; U50922; AAC05179.1; -; mRNA.
DR EMBL; AF190646; AAF01469.1; -; mRNA.
DR EMBL; U50921; AAC05178.1; -; mRNA.
DR EMBL; AF019663; AAD10168.1; -; mRNA.
DR EMBL; X90697; CAA62230.1; -; mRNA.
DR CCDS; CCDS17350.1; -. [Q9QUQ5-1]
DR CCDS; CCDS79904.1; -. [Q9QUQ5-2]
DR PIR; S59128; S59128.
DR RefSeq; NP_001240611.1; NM_001253682.1. [Q9QUQ5-2]
DR RefSeq; NP_058680.1; NM_016984.3. [Q9QUQ5-1]
DR RefSeq; XP_006501359.1; XM_006501296.3. [Q9QUQ5-1]
DR PDB; 5Z96; EM; 3.28 A; A/B/C/D=1-755.
DR PDB; 6JZO; EM; 3.28 A; A/B/C/D=1-755.
DR PDB; 7CQP; X-ray; 1.90 A; C=785-812.
DR PDBsum; 5Z96; -.
DR PDBsum; 6JZO; -.
DR PDBsum; 7CQP; -.
DR AlphaFoldDB; Q9QUQ5; -.
DR SMR; Q9QUQ5; -.
DR BioGRID; 204330; 6.
DR DIP; DIP-40848N; -.
DR IntAct; Q9QUQ5; 5.
DR MINT; Q9QUQ5; -.
DR STRING; 10090.ENSMUSP00000029311; -.
DR BindingDB; Q9QUQ5; -.
DR ChEMBL; CHEMBL1741219; -.
DR GuidetoPHARMACOLOGY; 489; -.
DR iPTMnet; Q9QUQ5; -.
DR PhosphoSitePlus; Q9QUQ5; -.
DR SwissPalm; Q9QUQ5; -.
DR MaxQB; Q9QUQ5; -.
DR PaxDb; Q9QUQ5; -.
DR PRIDE; Q9QUQ5; -.
DR ProteomicsDB; 300131; -. [Q9QUQ5-1]
DR ProteomicsDB; 300132; -. [Q9QUQ5-2]
DR Antibodypedia; 8254; 306 antibodies from 34 providers.
DR DNASU; 22066; -.
DR Ensembl; ENSMUST00000029311; ENSMUSP00000029311; ENSMUSG00000027748. [Q9QUQ5-1]
DR Ensembl; ENSMUST00000200048; ENSMUSP00000143593; ENSMUSG00000027748. [Q9QUQ5-2]
DR GeneID; 22066; -.
DR KEGG; mmu:22066; -.
DR UCSC; uc008pfd.2; mouse. [Q9QUQ5-1]
DR UCSC; uc008pff.2; mouse. [Q9QUQ5-2]
DR CTD; 7223; -.
DR MGI; MGI:109525; Trpc4.
DR VEuPathDB; HostDB:ENSMUSG00000027748; -.
DR eggNOG; KOG3609; Eukaryota.
DR GeneTree; ENSGT01050000244831; -.
DR InParanoid; Q9QUQ5; -.
DR OMA; QSPDEKC; -.
DR PhylomeDB; Q9QUQ5; -.
DR TreeFam; TF313147; -.
DR Reactome; R-MMU-3295583; TRP channels.
DR BioGRID-ORCS; 22066; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Trpc4; mouse.
DR PRO; PR:Q9QUQ5; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9QUQ5; protein.
DR Bgee; ENSMUSG00000027748; Expressed in lateral septal nucleus and 96 other tissues.
DR ExpressionAtlas; Q9QUQ5; baseline and differential.
DR Genevisible; Q9QUQ5; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0034704; C:calcium channel complex; ISO:MGI.
DR GO; GO:0034703; C:cation channel complex; IBA:GO_Central.
DR GO; GO:0005901; C:caveola; IDA:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0030863; C:cortical cytoskeleton; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; IPI:MGI.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0045296; F:cadherin binding; ISO:MGI.
DR GO; GO:0005262; F:calcium channel activity; ISO:MGI.
DR GO; GO:0070679; F:inositol 1,4,5 trisphosphate binding; IDA:BHF-UCL.
DR GO; GO:0015279; F:store-operated calcium channel activity; ISO:MGI.
DR GO; GO:0070509; P:calcium ion import; ISO:MGI.
DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; ISO:MGI.
DR GO; GO:0014051; P:gamma-aminobutyric acid secretion; IMP:MGI.
DR GO; GO:0006828; P:manganese ion transport; IBA:GO_Central.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IMP:MGI.
DR GO; GO:0106129; P:positive regulation of store-operated calcium entry; ISO:MGI.
DR GO; GO:0099605; P:regulation of action potential firing rate; ISO:MGI.
DR GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR013555; TRP_dom.
DR InterPro; IPR005460; TRPC4_channel.
DR InterPro; IPR002153; TRPC_channel.
DR PANTHER; PTHR10117; PTHR10117; 1.
DR PANTHER; PTHR10117:SF25; PTHR10117:SF25; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF08344; TRP_2; 1.
DR PRINTS; PR01097; TRNSRECEPTRP.
DR PRINTS; PR01645; TRPCHANNEL4.
DR SMART; SM00248; ANK; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat; Calcium; Calcium channel;
KW Calcium transport; Cell membrane; Coiled coil; Ion channel; Ion transport;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..974
FT /note="Short transient receptor potential channel 4"
FT /id="PRO_0000215315"
FT TOPO_DOM 1..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..362
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 363..383
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 384..436
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 437..457
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 458..469
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..511
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 533..599
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 621..974
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 31..60
FT /note="ANK 1"
FT REPEAT 69..97
FT /note="ANK 2"
FT REPEAT 98..124
FT /note="ANK 3"
FT REPEAT 141..170
FT /note="ANK 4"
FT REGION 87..172
FT /note="Multimerization domain"
FT REGION 254..304
FT /note="Multimerization domain"
FT REGION 615..974
FT /note="Binds to ITPR1, ITPR2 and ITPR3"
FT /evidence="ECO:0000250"
FT REGION 765..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..974
FT /note="PDZ-binding domain"
FT /evidence="ECO:0000250"
FT COILED 223..260
FT /evidence="ECO:0000255"
FT MOD_RES 956
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000250|UniProtKB:Q9UBN4"
FT MOD_RES 969
FT /note="Phosphotyrosine; by FYN"
FT /evidence="ECO:0000250|UniProtKB:Q9UBN4"
FT VAR_SEQ 781..864
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:10980202,
FT ECO:0000303|PubMed:9512398, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.2"
FT /id="VSP_006570"
FT CONFLICT 780
FT /note="E -> K (in Ref. 3; AAF01469)"
FT /evidence="ECO:0000305"
FT CONFLICT 890
FT /note="R -> L (in Ref. 3; AAF01469)"
FT /evidence="ECO:0000305"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 31..39
FT /evidence="ECO:0007829|PDB:5Z96"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 45..53
FT /evidence="ECO:0007829|PDB:5Z96"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:5Z96"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:6JZO"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:5Z96"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 111..116
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 145..151
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 155..162
FT /evidence="ECO:0007829|PDB:5Z96"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 190..203
FT /evidence="ECO:0007829|PDB:5Z96"
FT TURN 206..210
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 216..231
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 238..257
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 264..268
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 287..294
FT /evidence="ECO:0007829|PDB:5Z96"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 305..314
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 326..338
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 340..345
FT /evidence="ECO:0007829|PDB:5Z96"
FT TURN 346..348
FT /evidence="ECO:0007829|PDB:5Z96"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:5Z96"
FT TURN 354..360
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 362..383
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 401..422
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 427..431
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 433..456
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 473..489
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 491..498
FT /evidence="ECO:0007829|PDB:5Z96"
FT TURN 500..502
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 503..517
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 520..541
FT /evidence="ECO:0007829|PDB:5Z96"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:5Z96"
FT STRAND 551..556
FT /evidence="ECO:0007829|PDB:5Z96"
FT STRAND 560..563
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 564..573
FT /evidence="ECO:0007829|PDB:5Z96"
FT TURN 574..578
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 581..584
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 591..609
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 612..627
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 635..644
FT /evidence="ECO:0007829|PDB:5Z96"
FT STRAND 646..650
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 655..657
FT /evidence="ECO:0007829|PDB:5Z96"
FT STRAND 658..661
FT /evidence="ECO:0007829|PDB:6JZO"
FT HELIX 693..724
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 733..754
FT /evidence="ECO:0007829|PDB:5Z96"
FT HELIX 792..799
FT /evidence="ECO:0007829|PDB:7CQP"
FT HELIX 801..807
FT /evidence="ECO:0007829|PDB:7CQP"
SQ SEQUENCE 974 AA; 111575 MW; 2D0BB2F235F5F8D1 CRC64;
MAQFYYKRNV NAPYRDRIPL RIVRAESELS PSEKAYLNAV EKGDYASVKK SLEEAEIYFK
ININCIDPLG RTALLIAIEN ENLELIELLL SFNVYVGDAL LHAIRKEVVG AVELLLNHKK
PSGEKQVPPI LLDKQFSEFT PDITPIILAA HTNNYEIIKL LVQKGVSVPR PHEVRCNCVE
CVSSSDVDSL RHSRSRLNIY KALASPSLIA LSSEDPFLTA FQLSWELQEL SKVENEFKSE
YEELSRQCKQ FAKDLLDQTR SSRELEIILN YRDDNSLIEE QSGNDLARLK LAIKYRQKEF
VAQPNCQQLL ASRWYDEFPG WRRRHWAVKM VTCFIIGLLF PVFSVCYLIA PKSPLGLFIR
KPFIKFICHT ASYLTFLFLL LLASQHIDRS DLNRQGPPPT IVEWMILPWV LGFIWGEIKQ
MWDGGLQDYI HDWWNLMDFV MNSLYLATIS LKIVAFVKYS ALNPRESWDM WHPTLVAEAL
FAIANIFSSL RLISLFTANS HLGPLQISLG RMLLDILKFL FIYCLVLLAF ANGLNQLYFY
YEETKGLSCK GIRCEKQNNA FSTLFETLQS LFWSIFGLIN LYVTNVKAQH EFTEFVGATM
FGTYNVISLV VLLNMLIAMM NNSYQLIADH ADIEWKFART KLWMSYFEEG GTLPTPFNVI
PSPKSLWYLV KWIWTHLCKK KMRRKPESFG TIGRRAADNL RRHHQYQEVM RNLVKRYVAA
MIREAKTEEG LTEENVKELK QDISSFRFEV LGLLRGSKLS TIQSANAASS ADSDEKSQSE
GNGKDKRKNL SLFDLTTLIH PRSAAIASER HNLSNGSALV VQEPPREKQR KVNFVADIKN
FGLFHRRSKQ NAAEQNANQI FSVSEEITRQ QAAGALERNI ELESKGLASR GDRSIPGLNE
QCVLVDHRER NTDTLGLQVG KRVCSTFKSE KVVVEDTVPI IPKEKHAHEE DSSIDYDLSP
TDTAAHEDYV TTRL
