TTYH1_HUMAN
ID TTYH1_HUMAN Reviewed; 450 AA.
AC Q9H313; B0VJY3; B0VJY4; B0VJY5; B2VAL9; Q5U682; Q68A17; Q6L750; Q6ZTE5;
AC Q8WUU2;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Protein tweety homolog 1;
DE Short=hTTY1;
GN Name=TTYH1;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10950931; DOI=10.1006/geno.2000.6259;
RA Campbell H.D., Kamei M., Claudianos C., Woollatt E., Sutherland G.R.,
RA Suzuki Y., Hida M., Sugano S., Young I.G.;
RT "Human and mouse homologues of the Drosophila melanogaster tweety (tty)
RT gene: a novel gene family encoding predicted transmembrane proteins.";
RL Genomics 68:89-92(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND FUNCTION (ISOFORM 3).
RX PubMed=15010458; DOI=10.1074/jbc.m313813200;
RA Suzuki M., Mizuno A.;
RT "A novel human Cl(-) channel family related to Drosophila flightless
RT locus.";
RL J. Biol. Chem. 279:22461-22468(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Sugiyama A., Inoue H., Oka M.;
RT "Homo sapiens mRNA.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
RC TISSUE=Cerebellum;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Brain, and Placenta;
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 [8]
RP TISSUE SPECIFICITY.
RX PubMed=17116230; DOI=10.1111/j.1471-4159.2006.04237.x;
RA Matthews C.A., Shaw J.E., Hooper J.A., Young I.G., Crouch M.F.,
RA Campbell H.D.;
RT "Expression and evolution of the mammalian brain gene Ttyh1.";
RL J. Neurochem. 100:693-707(2007).
CC -!- FUNCTION: Probable chloride channel. May be involved in cell adhesion
CC (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Isoform 3 may be a Ca(2+)-independent and swelling-activated
CC chloride channel, possibly involved in regulation of cell volume.
CC -!- INTERACTION:
CC Q9H313; O15354: GPR37; NbExp=2; IntAct=EBI-20793786, EBI-15639515;
CC Q9H313-4; P13473-2: LAMP2; NbExp=3; IntAct=EBI-17671298, EBI-21591415;
CC Q9H313-4; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-17671298, EBI-5280197;
CC Q9H313-4; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-17671298, EBI-2623095;
CC Q9H313-4; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-17671298, EBI-2852148;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9H313-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H313-2; Sequence=VSP_029760;
CC Name=3; Synonyms=TTYH1s;
CC IsoId=Q9H313-3; Sequence=VSP_029759;
CC Name=4;
CC IsoId=Q9H313-4; Sequence=VSP_029753, VSP_029757, VSP_029760;
CC Name=5;
CC IsoId=Q9H313-5; Sequence=VSP_029754, VSP_029755, VSP_029756,
CC VSP_029758;
CC -!- TISSUE SPECIFICITY: Expressed in brain, eye, ovary and testis, and at
CC lower levels in muscle, placenta, liver and lung.
CC {ECO:0000269|PubMed:17116230}.
CC -!- SIMILARITY: Belongs to the tweety family. {ECO:0000305}.
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DR EMBL; AF177909; AAG02580.1; -; mRNA.
DR EMBL; AB162930; BAD20189.1; -; mRNA.
DR EMBL; AB188496; BAD37142.1; -; mRNA.
DR EMBL; AK126690; BAC86645.1; -; mRNA.
DR EMBL; AK289468; BAF82157.1; -; mRNA.
DR EMBL; CU207370; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU467002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW72240.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW72242.1; -; Genomic_DNA.
DR EMBL; BC011347; AAH11347.1; -; mRNA.
DR EMBL; BC019358; AAH19358.1; -; mRNA.
DR CCDS; CCDS12893.1; -. [Q9H313-1]
DR CCDS; CCDS33106.1; -. [Q9H313-3]
DR CCDS; CCDS56102.1; -. [Q9H313-2]
DR RefSeq; NP_001005367.1; NM_001005367.2. [Q9H313-3]
DR RefSeq; NP_001188390.1; NM_001201461.1. [Q9H313-2]
DR RefSeq; NP_065710.1; NM_020659.3. [Q9H313-1]
DR PDB; 7P5J; EM; 4.00 A; A/B=2-450.
DR PDBsum; 7P5J; -.
DR AlphaFoldDB; Q9H313; -.
DR SMR; Q9H313; -.
DR BioGRID; 121494; 536.
DR IntAct; Q9H313; 10.
DR MINT; Q9H313; -.
DR STRING; 9606.ENSP00000365714; -.
DR TCDB; 1.A.48.1.2; the anion channel tweety (tweety) family.
DR GlyGen; Q9H313; 4 sites.
DR iPTMnet; Q9H313; -.
DR PhosphoSitePlus; Q9H313; -.
DR BioMuta; TTYH1; -.
DR DMDM; 74718142; -.
DR EPD; Q9H313; -.
DR jPOST; Q9H313; -.
DR MassIVE; Q9H313; -.
DR PaxDb; Q9H313; -.
DR PeptideAtlas; Q9H313; -.
DR PRIDE; Q9H313; -.
DR ProteomicsDB; 80648; -. [Q9H313-1]
DR ProteomicsDB; 80649; -. [Q9H313-2]
DR ProteomicsDB; 80650; -. [Q9H313-3]
DR ProteomicsDB; 80651; -. [Q9H313-4]
DR ProteomicsDB; 80652; -. [Q9H313-5]
DR Antibodypedia; 32911; 169 antibodies from 25 providers.
DR DNASU; 57348; -.
DR Ensembl; ENST00000301194.8; ENSP00000301194.4; ENSG00000167614.14. [Q9H313-2]
DR Ensembl; ENST00000376530.8; ENSP00000365713.3; ENSG00000167614.14. [Q9H313-1]
DR Ensembl; ENST00000376531.3; ENSP00000365714.3; ENSG00000167614.14. [Q9H313-3]
DR Ensembl; ENST00000611133.4; ENSP00000480177.1; ENSG00000276887.4. [Q9H313-2]
DR Ensembl; ENST00000611471.1; ENSP00000484881.1; ENSG00000275650.4. [Q9H313-3]
DR Ensembl; ENST00000611711.4; ENSP00000484774.1; ENSG00000276887.4. [Q9H313-1]
DR Ensembl; ENST00000614387.1; ENSP00000484077.1; ENSG00000276887.4. [Q9H313-4]
DR Ensembl; ENST00000614458.4; ENSP00000484835.1; ENSG00000276887.4. [Q9H313-3]
DR Ensembl; ENST00000616929.4; ENSP00000479779.1; ENSG00000276537.4. [Q9H313-2]
DR Ensembl; ENST00000619450.4; ENSP00000480769.1; ENSG00000275650.4. [Q9H313-1]
DR Ensembl; ENST00000619453.4; ENSP00000484548.1; ENSG00000276537.4. [Q9H313-3]
DR Ensembl; ENST00000619591.4; ENSP00000481601.1; ENSG00000275650.4. [Q9H313-2]
DR Ensembl; ENST00000620133.4; ENSP00000483288.1; ENSG00000276887.4. [Q9H313-5]
DR Ensembl; ENST00000620298.4; ENSP00000481138.1; ENSG00000276537.4. [Q9H313-1]
DR Ensembl; ENST00000622771.1; ENSP00000482372.1; ENSG00000276537.4. [Q9H313-4]
DR GeneID; 57348; -.
DR KEGG; hsa:57348; -.
DR MANE-Select; ENST00000376530.8; ENSP00000365713.3; NM_020659.4; NP_065710.1.
DR UCSC; uc002qfq.4; human. [Q9H313-1]
DR CTD; 57348; -.
DR DisGeNET; 57348; -.
DR GeneCards; TTYH1; -.
DR HGNC; HGNC:13476; TTYH1.
DR HPA; ENSG00000167614; Tissue enhanced (brain, testis).
DR MIM; 605784; gene.
DR neXtProt; NX_Q9H313; -.
DR OpenTargets; ENSG00000167614; -.
DR PharmGKB; PA37778; -.
DR VEuPathDB; HostDB:ENSG00000167614; -.
DR eggNOG; KOG4433; Eukaryota.
DR GeneTree; ENSGT00950000183060; -.
DR HOGENOM; CLU_023758_0_1_1; -.
DR InParanoid; Q9H313; -.
DR OMA; SYSPSIW; -.
DR OrthoDB; 725378at2759; -.
DR PhylomeDB; Q9H313; -.
DR TreeFam; TF319025; -.
DR PathwayCommons; Q9H313; -.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels. [Q9H313-3]
DR SignaLink; Q9H313; -.
DR BioGRID-ORCS; 57348; 30 hits in 1070 CRISPR screens.
DR ChiTaRS; TTYH1; human.
DR GenomeRNAi; 57348; -.
DR Pharos; Q9H313; Tbio.
DR PRO; PR:Q9H313; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9H313; protein.
DR Bgee; ENSG00000167614; Expressed in ventricular zone and 100 other tissues.
DR ExpressionAtlas; Q9H313; baseline and differential.
DR Genevisible; Q9H313; HS.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0031527; C:filopodium membrane; IEA:Ensembl.
DR GO; GO:0032433; C:filopodium tip; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030868; C:smooth endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0005254; F:chloride channel activity; TAS:Reactome.
DR GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IBA:GO_Central.
DR GO; GO:0005381; F:iron ion transmembrane transporter activity; NAS:UniProtKB.
DR GO; GO:0072320; F:volume-sensitive chloride channel activity; IDA:FlyBase.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0031589; P:cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:0006821; P:chloride transport; IDA:FlyBase.
DR GO; GO:0046847; P:filopodium assembly; IEA:Ensembl.
DR GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
DR GO; GO:0006826; P:iron ion transport; NAS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:Ensembl.
DR CDD; cd07912; Tweety_N; 1.
DR InterPro; IPR006990; Tweety.
DR PANTHER; PTHR12424; PTHR12424; 1.
DR Pfam; PF04906; Tweety; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane; Chloride;
KW Chloride channel; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..450
FT /note="Protein tweety homolog 1"
FT /id="PRO_0000312239"
FT TOPO_DOM 1..43
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..214
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..240
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..390
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 428..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D3A9"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..212
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029753"
FT VAR_SEQ 1..85
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_029754"
FT VAR_SEQ 86..101
FT /note="GGGCVTWSCIVALLAG -> MEKVRLWRGSESRAAI (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_029755"
FT VAR_SEQ 140..142
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_029756"
FT VAR_SEQ 213
FT /note="R -> M (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029757"
FT VAR_SEQ 376..450
FT /note="DYGAALRGLCEDALEGLLFLLLFSLLSAGALATALCSLPRAWALFPPSDDYD
FT DTDDDDPFNPQESKRFVQWQSSI -> VKPLPSQFLLPRGASVSTHRTTSSFSLDPCHC
FT A (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_029758"
FT VAR_SEQ 423..450
FT /note="SDDYDDTDDDDPFNPQESKRFVQWQSSI -> RNPSALCSGSRLSEPLLPAG
FT LEPGSPLRSFPGCRRRPH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15010458, ECO:0000303|PubMed:15489334"
FT /id="VSP_029759"
FT VAR_SEQ 437
FT /note="P -> PQ (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_029760"
FT CONFLICT 380
FT /note="A -> S (in Ref. 2; BAD20189)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 450 AA; 49051 MW; AD3DA4569F083657 CRC64;
MGAPPGYRPS AWVHLLHQLP RADFQLRPVP SVFAPQEQEY QQALLLVAAL AGLGLGLSLI
FIAVYLIRFC CCRPPEPPGS KIPSPGGGCV TWSCIVALLA GCTGIGIGFY GNSETSDGVS
QLSSALLHAN HTLSTIDHLV LETVERLGEA VRTELTTLEE VLEPRTELVA AARGARRQAE
AAAQQLQGLA FWQGVPLSPL QVAENVSFVE EYRWLAYVLL LLLELLVCLF TLLGLAKQSK
WLVIVMTVMS LLVLVLSWGS MGLEAATAVG LSDFCSNPDP YVLNLTQEET GLSSDILSYY
LLCNRAVSNP FQQRLTLSQR ALANIHSQLL GLEREAVPQF PSAQKPLLSL EETLNVTEGN
FHQLVALLHC RSLHKDYGAA LRGLCEDALE GLLFLLLFSL LSAGALATAL CSLPRAWALF
PPSDDYDDTD DDDPFNPQES KRFVQWQSSI
