TP4AP_HUMAN
ID TP4AP_HUMAN Reviewed; 797 AA.
AC Q8TEL6; E1P5Q0; E1P5Q1; Q96H82; Q9BVB8; Q9H429; Q9UFS6;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Short transient receptor potential channel 4-associated protein {ECO:0000305};
DE Short=Trp4-associated protein {ECO:0000303|PubMed:20551172};
DE Short=Trpc4-associated protein {ECO:0000303|PubMed:20551172};
DE AltName: Full=Protein TAP1;
DE AltName: Full=TNF-receptor ubiquitous scaffolding/signaling protein {ECO:0000303|PubMed:26038816};
DE Short=Protein TRUSS {ECO:0000303|PubMed:26038816};
GN Name=TRPC4AP {ECO:0000303|PubMed:20551172, ECO:0000312|HGNC:HGNC:16181};
GN Synonyms=C20orf188 {ECO:0000312|HGNC:HGNC:16181}, TRRP4AP;
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] (ISOFORMS 2 AND 3).
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=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix, Muscle, and Prostate;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 238-797 (ISOFORM 1).
RC TISSUE=Mammary cancer;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION, IDENTIFICATION IN A DCX (DDB1-CUL4-X-BOX) E3 UBIQUITIN-PROTEIN
RP LIGASE COMPLEX, AND INTERACTION WITH MYC.
RX PubMed=20551172; DOI=10.1101/gad.1920310;
RA Choi S.H., Wright J.B., Gerber S.A., Cole M.D.;
RT "Myc protein is stabilized by suppression of a novel E3 ligase complex in
RT cancer cells.";
RL Genes Dev. 24:1236-1241(2010).
RN [7]
RP INTERACTION WITH DDB1.
RX PubMed=19966799; DOI=10.1038/nsmb.1719;
RA Li T., Robert E.I., van Breugel P.C., Strubin M., Zheng N.;
RT "A promiscuous alpha-helical motif anchors viral hijackers and substrate
RT receptors to the CUL4-DDB1 ubiquitin ligase machinery.";
RL Nat. Struct. Mol. Biol. 17:105-111(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP SUBCELLULAR LOCATION, UBIQUITINATION, PHOSPHORYLATION, AND INTERACTION WITH
RP HEPATITIS B VIRUS PROTEIN X (MICROBIAL INFECTION).
RX PubMed=26038816; DOI=10.1080/15384101.2015.1056946;
RA Jamal A., Swarnalatha M., Sultana S., Joshi P., Panda S.K., Kumar V.;
RT "The G1 phase E3 ubiquitin ligase TRUSS that gets deregulated in human
RT cancers is a novel substrate of the S-phase E3 ubiquitin ligase Skp2.";
RL Cell Cycle 14:2688-2700(2015).
RN [10]
RP FUNCTION, PATHWAY, AND IDENTIFICATION IN A CRL4 E3 UBIQUITIN-PROTEIN LIGASE
RP COMPLEX.
RX PubMed=29779948; DOI=10.1016/j.cell.2018.04.028;
RA Koren I., Timms R.T., Kula T., Xu Q., Li M.Z., Elledge S.J.;
RT "The eukaryotic proteome is shaped by E3 ubiquitin ligases targeting C-
RT terminal degrons.";
RL Cell 173:1622-1635(2018).
CC -!- FUNCTION: Substrate-recognition component of a DCX (DDB1-CUL4-X-box) E3
CC ubiquitin-protein ligase complex required for cell cycle control
CC (PubMed:20551172, PubMed:29779948). The DCX(TRPC4AP) complex
CC specifically mediates the polyubiquitination and subsequent degradation
CC of MYC as part of the DesCEND (destruction via C-end degrons) pathway
CC (PubMed:20551172, PubMed:29779948). The DesCEND (destruction via C-end
CC degrons) pathway recognizes a C-degron located at the extreme C
CC terminus of target proteins, leading to their ubiquitination and
CC degradation (PubMed:29779948). The DCX(TRPC4AP) complex specifically
CC recognizes proteins with an arginine at the minus 3 position (R-3
CC motif) at the C-terminus, such as MYC, leading to their ubiquitination
CC and degradation (PubMed:29779948). Also participates in the activation
CC of NFKB1 in response to ligation of TNFRSF1A, possibly by linking
CC TNFRSF1A to the IKK signalosome (By similarity). Involved in JNK
CC activation via its interaction with TRAF2 (By similarity). Also
CC involved in elevation of endoplasmic reticulum Ca(2+) storage reduction
CC in response to CHRM1 (By similarity). {ECO:0000250|UniProtKB:Q9JLV2,
CC ECO:0000269|PubMed:20551172, ECO:0000269|PubMed:29779948}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:20551172}.
CC -!- SUBUNIT: Component of the DCX(TRPC4AP) E3 ubiquitin ligase complex, at
CC least composed of CUL4A, DDB1, TRPC4AP/TRUSS and RBX1 (PubMed:20551172,
CC PubMed:19966799). Interacts with MYC (PubMed:20551172). Constitutively
CC associated with TNFRSF1A (By similarity). Directly interacts with
CC TRADD, TRAF2, CHUK, IKBKB and IKBKG (By similarity). Interacts with
CC TRPC1, TRPC4 and TRPC5 (By similarity). {ECO:0000250|UniProtKB:Q9JLV2,
CC ECO:0000269|PubMed:19966799, ECO:0000269|PubMed:20551172}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Hepatitis B virus (HBV)
CC protein X; leading to prevent ubiquitination of TRPC4AP by SKP2.
CC {ECO:0000269|PubMed:26038816}.
CC -!- INTERACTION:
CC Q8TEL6; P62136: PPP1CA; NbExp=2; IntAct=EBI-2559060, EBI-357253;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:26038816}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8TEL6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TEL6-2; Sequence=VSP_003982;
CC Name=3;
CC IsoId=Q8TEL6-3; Sequence=VSP_054231;
CC -!- PTM: Phosphorylated by GSK3B; phosphorylation is required for
CC ubiquitination. {ECO:0000269|PubMed:26038816}.
CC -!- PTM: Ubiquitinated by a SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-
CC protein ligase containing SKP2, leading to its degradation
CC (PubMed:26038816). Phosphorylation by GSK3B is required for
CC ubiquitination (PubMed:26038816). {ECO:0000269|PubMed:26038816}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB84932.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK074106; BAB84932.1; ALT_FRAME; mRNA.
DR EMBL; AB590540; BAJ20695.1; -; mRNA.
DR EMBL; AL132825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76233.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76235.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76229.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76234.1; -; Genomic_DNA.
DR EMBL; BC001323; AAH01323.1; -; mRNA.
DR EMBL; BC008836; AAH08836.2; -; mRNA.
DR EMBL; BC013144; AAH13144.1; -; mRNA.
DR EMBL; AL117480; CAB55953.1; -; mRNA.
DR CCDS; CCDS13246.1; -. [Q8TEL6-1]
DR CCDS; CCDS46591.1; -. [Q8TEL6-3]
DR PIR; T17263; T17263.
DR RefSeq; NP_056453.1; NM_015638.2. [Q8TEL6-1]
DR RefSeq; NP_955400.1; NM_199368.1. [Q8TEL6-3]
DR AlphaFoldDB; Q8TEL6; -.
DR BioGRID; 117569; 82.
DR DIP; DIP-42719N; -.
DR IntAct; Q8TEL6; 41.
DR MINT; Q8TEL6; -.
DR STRING; 9606.ENSP00000252015; -.
DR iPTMnet; Q8TEL6; -.
DR PhosphoSitePlus; Q8TEL6; -.
DR BioMuta; TRPC4AP; -.
DR DMDM; 25091357; -.
DR EPD; Q8TEL6; -.
DR jPOST; Q8TEL6; -.
DR MassIVE; Q8TEL6; -.
DR MaxQB; Q8TEL6; -.
DR PaxDb; Q8TEL6; -.
DR PeptideAtlas; Q8TEL6; -.
DR PRIDE; Q8TEL6; -.
DR ProteomicsDB; 15211; -.
DR ProteomicsDB; 74470; -. [Q8TEL6-1]
DR ProteomicsDB; 74471; -. [Q8TEL6-2]
DR Antibodypedia; 25963; 195 antibodies from 30 providers.
DR DNASU; 26133; -.
DR Ensembl; ENST00000252015.3; ENSP00000252015.2; ENSG00000100991.12. [Q8TEL6-1]
DR Ensembl; ENST00000451813.6; ENSP00000400614.1; ENSG00000100991.12. [Q8TEL6-3]
DR GeneID; 26133; -.
DR KEGG; hsa:26133; -.
DR MANE-Select; ENST00000252015.3; ENSP00000252015.2; NM_015638.3; NP_056453.1.
DR UCSC; uc002xbk.4; human. [Q8TEL6-1]
DR CTD; 26133; -.
DR DisGeNET; 26133; -.
DR GeneCards; TRPC4AP; -.
DR HGNC; HGNC:16181; TRPC4AP.
DR HPA; ENSG00000100991; Low tissue specificity.
DR MIM; 608430; gene.
DR neXtProt; NX_Q8TEL6; -.
DR OpenTargets; ENSG00000100991; -.
DR PharmGKB; PA25730; -.
DR VEuPathDB; HostDB:ENSG00000100991; -.
DR eggNOG; ENOG502QQ1C; Eukaryota.
DR GeneTree; ENSGT00390000018330; -.
DR HOGENOM; CLU_015792_1_0_1; -.
DR InParanoid; Q8TEL6; -.
DR OMA; EMTKGNW; -.
DR OrthoDB; 240503at2759; -.
DR PhylomeDB; Q8TEL6; -.
DR TreeFam; TF329145; -.
DR PathwayCommons; Q8TEL6; -.
DR Reactome; R-HSA-3295583; TRP channels.
DR SignaLink; Q8TEL6; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 26133; 16 hits in 1082 CRISPR screens.
DR ChiTaRS; TRPC4AP; human.
DR GeneWiki; TRPC4AP; -.
DR GenomeRNAi; 26133; -.
DR Pharos; Q8TEL6; Tbio.
DR PRO; PR:Q8TEL6; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q8TEL6; protein.
DR Bgee; ENSG00000100991; Expressed in granulocyte and 199 other tissues.
DR Genevisible; Q8TEL6; HS.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005262; F:calcium channel activity; TAS:Reactome.
DR GO; GO:0019902; F:phosphatase binding; IDA:UniProtKB.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IDA:UniProtKB.
DR GO; GO:0070588; P:calcium ion transmembrane transport; TAS:Reactome.
DR GO; GO:0048820; P:hair follicle maturation; IEA:Ensembl.
DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:0140627; P:ubiquitin-dependent protein catabolic process via the C-end degron rule pathway; IDA:UniProtKB.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR022162; TRPC4AP.
DR PANTHER; PTHR31743; PTHR31743; 1.
DR Pfam; PF12463; DUF3689; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Host-virus interaction;
KW Phosphoprotein; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..797
FT /note="Short transient receptor potential channel 4-
FT associated protein"
FT /id="PRO_0000072641"
FT REGION 2..400
FT /note="Interaction with TNFRSF1A"
FT /evidence="ECO:0000250|UniProtKB:Q9JLV2"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 351..358
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054231"
FT VAR_SEQ 533..797
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_003982"
SQ SEQUENCE 797 AA; 90852 MW; 999A8CA3B0D2CEEE CRC64;
MAAAPVAAGS GAGRGRRSAA TVAAWGGWGG RPRPGNILLQ LRQGQLTGRG LVRAVQFTET
FLTERDKQSK WSGIPQLLLK LHTTSHLHSD FVECQNILKE ISPLLSMEAM AFVTEERKLT
QETTYPNTYI FDLFGGVDLL VEILMRPTIS IRGQKLKISD EMSKDCLSIL YNTCVCTEGV
TKRLAEKNDF VIFLFTLMTS KKTFLQTATL IEDILGVKKE MIRLDEVPNL SSLVSNFDQQ
QLANFCRILA VTISEMDTGN DDKHTLLAKN AQQKKSLSLG PSAAEINQAA LLSIPGFVER
LCKLATRKVS ESTGTASFLQ ELEEWYTWLD NALVLDALMR VANEESEHNQ ASIVFPPPGA
SEENGLPHTS ARTQLPQSMK IMHEIMYKLE VLYVLCVLLM GRQRNQVHRM IAEFKLIPGL
NNLFDKLIWR KHSASALVLH GHNQNCDCSP DITLKIQFLR LLQSFSDHHE NKYLLLNNQE
LNELSAISLK ANIPEVEAVL NTDRSLVCDG KRGLLTRLLQ VMKKEPAESS FRFWQARAVE
SFLRGTTSYA DQMFLLKRGL LEHILYCIVD SECKSRDVLQ SYFDLLGELM KFNVDAFKRF
NKYINTDAKF QVFLKQINSS LVDSNMLVRC VTLSLDRFEN QVDMKVAEVL SECRLLAYIS
QVPTQMSFLF RLINIIHVQT LTQENVSCLN TSLVILMLAR RKERLPLYLR LLQRMEHSKK
YPGFLLNNFH NLLRFWQQHY LHKDKDSTCL ENSSCISFSY WKETVSILLN PDRQSPSALV
SYIEEPYMDI DRDFTEE
