TRI72_HUMAN
ID TRI72_HUMAN Reviewed; 477 AA.
AC Q6ZMU5; Q8N4X6; Q8NBD9;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Tripartite motif-containing protein 72;
DE AltName: Full=Mitsugumin-53;
DE Short=Mg53;
GN Name=TRIM72 {ECO:0000312|HGNC:HGNC:32671}; Synonyms=MG53;
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] {ECO:0000305, ECO:0000312|EMBL:BAD18630.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum {ECO:0000312|EMBL:BAC03506.1}, and
RC Thymus {ECO:0000312|EMBL:BAD18630.1};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH33211.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Muscle {ECO:0000312|EMBL:AAH33211.1};
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 S-NITROSYLATION AT CYS-144, AND MUTAGENESIS OF CYS-144.
RX PubMed=24487118; DOI=10.1016/j.yjmcc.2014.01.010;
RA Kohr M.J., Evangelista A.M., Ferlito M., Steenbergen C., Murphy E.;
RT "S-nitrosylation of TRIM72 at cysteine 144 is critical for protection
RT against oxidation-induced protein degradation and cell death.";
RL J. Mol. Cell. Cardiol. 69:67-74(2014).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 278-470.
RX PubMed=19967786; DOI=10.1002/prot.22647;
RA Park E.Y., Kwon O.B., Jeong B.C., Yi J.S., Lee C.S., Ko Y.G., Song H.K.;
RT "Crystal structure of PRY-SPRY domain of human TRIM72.";
RL Proteins 78:790-795(2010).
CC -!- FUNCTION: Muscle-specific protein that plays a central role in cell
CC membrane repair by nucleating the assembly of the repair machinery at
CC injury sites. Specifically binds phosphatidylserine. Acts as a sensor
CC of oxidation: upon membrane damage, entry of extracellular oxidative
CC environment results in disulfide bond formation and homooligomerization
CC at the injury site. This oligomerization acts as a nucleation site for
CC recruitment of TRIM72-containing vesicles to the injury site, leading
CC to membrane patch formation. Probably acts upstream of the Ca(2+)-
CC dependent membrane resealing process. Required for transport of DYSF to
CC sites of cell injury during repair patch formation. Regulates membrane
CC budding and exocytosis. May be involved in the regulation of the
CC mobility of KCNB1-containing endocytic vesicles (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer; disulfide-linked. Interacts with DYSF and CAV3
CC (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q6ZMU5; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-2341648, EBI-11096309;
CC Q6ZMU5; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-2341648, EBI-747505;
CC Q6ZMU5; Q13503: MED21; NbExp=3; IntAct=EBI-2341648, EBI-394678;
CC Q6ZMU5; Q08AG7: MZT1; NbExp=3; IntAct=EBI-2341648, EBI-2637198;
CC Q6ZMU5; Q13287: NMI; NbExp=3; IntAct=EBI-2341648, EBI-372942;
CC Q6ZMU5; Q08209-2: PPP3CA; NbExp=3; IntAct=EBI-2341648, EBI-11959013;
CC Q6ZMU5; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-2341648, EBI-358489;
CC Q6ZMU5; Q99081: TCF12; NbExp=3; IntAct=EBI-2341648, EBI-722877;
CC Q6ZMU5; Q99081-3: TCF12; NbExp=3; IntAct=EBI-2341648, EBI-11952764;
CC Q6ZMU5; Q6ZMU5: TRIM72; NbExp=3; IntAct=EBI-2341648, EBI-2341648;
CC Q6ZMU5; Q8N720: ZNF655; NbExp=3; IntAct=EBI-2341648, EBI-625509;
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250}.
CC Cytoplasmic vesicle membrane {ECO:0000250}. Note=Tethered to plasma
CC membrane and cytoplasmic vesicles via its interaction with
CC phosphatidylserine. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:14702039};
CC IsoId=Q6ZMU5-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q6ZMU5-2; Sequence=VSP_052318;
CC -!- PTM: Disulfide bond formation at Cys-242 occurs in case of membrane
CC damage that cause the entry of the oxidized milieu of the extracellular
CC space, resulting in homooligomerization. {ECO:0000250}.
CC -!- PTM: S-nitrosylation at Cys-144 stabilizes TRIM72 and protects against
CC oxidation-induced protein degradation and cell death.
CC {ECO:0000269|PubMed:24487118}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC03506.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK090695; BAC03506.1; ALT_INIT; mRNA.
DR EMBL; AK131485; BAD18630.1; -; mRNA.
DR EMBL; AC009088; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033211; AAH33211.1; -; mRNA.
DR CCDS; CCDS32437.1; -. [Q6ZMU5-1]
DR RefSeq; NP_001008275.2; NM_001008274.3. [Q6ZMU5-1]
DR PDB; 3KB5; X-ray; 1.50 A; A=278-470.
DR PDBsum; 3KB5; -.
DR AlphaFoldDB; Q6ZMU5; -.
DR SMR; Q6ZMU5; -.
DR BioGRID; 138920; 43.
DR IntAct; Q6ZMU5; 13.
DR MINT; Q6ZMU5; -.
DR STRING; 9606.ENSP00000312675; -.
DR TCDB; 1.F.1.2.1; the synaptosomal vesicle fusion pore (svf-pore) family.
DR iPTMnet; Q6ZMU5; -.
DR PhosphoSitePlus; Q6ZMU5; -.
DR BioMuta; TRIM72; -.
DR DMDM; 126253816; -.
DR EPD; Q6ZMU5; -.
DR jPOST; Q6ZMU5; -.
DR MassIVE; Q6ZMU5; -.
DR MaxQB; Q6ZMU5; -.
DR PaxDb; Q6ZMU5; -.
DR PeptideAtlas; Q6ZMU5; -.
DR PRIDE; Q6ZMU5; -.
DR ProteomicsDB; 67918; -. [Q6ZMU5-1]
DR ProteomicsDB; 67919; -. [Q6ZMU5-2]
DR Antibodypedia; 14026; 210 antibodies from 31 providers.
DR DNASU; 493829; -.
DR Ensembl; ENST00000322122.8; ENSP00000312675.3; ENSG00000177238.14. [Q6ZMU5-1]
DR Ensembl; ENST00000613872.1; ENSP00000481813.1; ENSG00000177238.14. [Q6ZMU5-2]
DR GeneID; 493829; -.
DR KEGG; hsa:493829; -.
DR MANE-Select; ENST00000322122.8; ENSP00000312675.3; NM_001008274.4; NP_001008275.2.
DR UCSC; uc002ebn.3; human. [Q6ZMU5-1]
DR CTD; 493829; -.
DR DisGeNET; 493829; -.
DR GeneCards; TRIM72; -.
DR HGNC; HGNC:32671; TRIM72.
DR HPA; ENSG00000177238; Group enriched (skeletal muscle, tongue).
DR MIM; 613288; gene.
DR neXtProt; NX_Q6ZMU5; -.
DR OpenTargets; ENSG00000177238; -.
DR PharmGKB; PA144596247; -.
DR VEuPathDB; HostDB:ENSG00000177238; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000161791; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q6ZMU5; -.
DR OMA; VECVEHK; -.
DR OrthoDB; 574602at2759; -.
DR PhylomeDB; Q6ZMU5; -.
DR TreeFam; TF342569; -.
DR PathwayCommons; Q6ZMU5; -.
DR Reactome; R-HSA-445355; Smooth Muscle Contraction.
DR SignaLink; Q6ZMU5; -.
DR BioGRID-ORCS; 493829; 24 hits in 1107 CRISPR screens.
DR ChiTaRS; TRIM72; human.
DR EvolutionaryTrace; Q6ZMU5; -.
DR GenomeRNAi; 493829; -.
DR Pharos; Q6ZMU5; Tbio.
DR PRO; PR:Q6ZMU5; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q6ZMU5; protein.
DR Bgee; ENSG00000177238; Expressed in hindlimb stylopod muscle and 110 other tissues.
DR Genevisible; Q6ZMU5; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; ISS:UniProtKB.
DR GO; GO:0003012; P:muscle system process; ISS:UniProtKB.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0043569; P:negative regulation of insulin-like growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0010832; P:negative regulation of myotube differentiation; IEA:Ensembl.
DR GO; GO:0001778; P:plasma membrane repair; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035038; TRIM72.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR24103:SF11; PTHR24103:SF11; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Coiled coil;
KW Cytoplasmic vesicle; Disulfide bond; Exocytosis; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; S-nitrosylation; Transport; Zinc;
KW Zinc-finger.
FT CHAIN 1..477
FT /note="Tripartite motif-containing protein 72"
FT /id="PRO_0000278130"
FT DOMAIN 271..475
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 14..57
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 81..122
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 135..169
FT /evidence="ECO:0000255"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 144
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:24487118"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A0JPQ4"
FT DISULFID 242
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT VAR_SEQ 270..477
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052318"
FT MUTAGEN 144
FT /note="C->S: No decrease in level upon treatment with
FT hydrogen peroxide."
FT /evidence="ECO:0000269|PubMed:24487118"
FT CONFLICT 192
FT /note="R -> C (in Ref. 1; BAD18630)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="E -> G (in Ref. 1; BAC03506)"
FT /evidence="ECO:0000305"
FT HELIX 279..284
FT /evidence="ECO:0007829|PDB:3KB5"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:3KB5"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:3KB5"
FT TURN 306..309
FT /evidence="ECO:0007829|PDB:3KB5"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:3KB5"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:3KB5"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:3KB5"
FT STRAND 342..350
FT /evidence="ECO:0007829|PDB:3KB5"
FT STRAND 355..363
FT /evidence="ECO:0007829|PDB:3KB5"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:3KB5"
FT HELIX 376..378
FT /evidence="ECO:0007829|PDB:3KB5"
FT STRAND 380..386
FT /evidence="ECO:0007829|PDB:3KB5"
FT TURN 387..389
FT /evidence="ECO:0007829|PDB:3KB5"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:3KB5"
FT STRAND 396..399
FT /evidence="ECO:0007829|PDB:3KB5"
FT STRAND 411..418
FT /evidence="ECO:0007829|PDB:3KB5"
FT TURN 419..422
FT /evidence="ECO:0007829|PDB:3KB5"
FT STRAND 423..428
FT /evidence="ECO:0007829|PDB:3KB5"
FT STRAND 436..441
FT /evidence="ECO:0007829|PDB:3KB5"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:3KB5"
FT TURN 459..463
FT /evidence="ECO:0007829|PDB:3KB5"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:3KB5"
SQ SEQUENCE 477 AA; 52731 MW; 2B4EE9A00318151F CRC64;
MSAAPGLLHQ ELSCPLCLQL FDAPVTAECG HSFCRACLGR VAGEPAADGT VLCPCCQAPT
RPQALSTNLQ LARLVEGLAQ VPQGHCEEHL DPLSIYCEQD RALVCGVCAS LGSHRGHRLL
PAAEAHARLK TQLPQQKLQL QEACMRKEKS VAVLEHQLVE VEETVRQFRG AVGEQLGKMR
VFLAALEGSL DREAERVRGE AGVALRRELG SLNSYLEQLR QMEKVLEEVA DKPQTEFLMK
YCLVTSRLQK ILAESPPPAR LDIQLPIISD DFKFQVWRKM FRALMPALEE LTFDPSSAHP
SLVVSSSGRR VECSEQKAPP AGEDPRQFDK AVAVVAHQQL SEGEHYWEVD VGDKPRWALG
VIAAEAPRRG RLHAVPSQGL WLLGLREGKI LEAHVEAKEP RALRSPERRP TRIGLYLSFG
DGVLSFYDAS DADALVPLFA FHERLPRPVY PFFDVCWHDK GKNAQPLLLV GPEGAEA
