CIA2A_HUMAN
ID CIA2A_HUMAN Reviewed; 160 AA.
AC Q9H5X1; A6NKS1; B2R5F8; B7Z8Z5;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Cytosolic iron-sulfur assembly component 2A {ECO:0000305};
DE AltName: Full=MIP18 family protein FAM96A;
GN Name=CIAO2A {ECO:0000312|HGNC:HGNC:26235};
GN Synonyms=CIA2A {ECO:0000303|PubMed:23891004},
GN FAM96A {ECO:0000312|HGNC:HGNC:26235};
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 1 AND 2).
RC TISSUE=Brain, and Trachea;
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=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
RP FUNCTION, IDENTIFICATION IN THE CIA COMPLEX, AND INTERACTION WITH CIAO1 AND
RP IREB2.
RX PubMed=23891004; DOI=10.1016/j.cmet.2013.06.015;
RA Stehling O., Mascarenhas J., Vashisht A.A., Sheftel A.D., Niggemeyer B.,
RA Roesser R., Pierik A.J., Wohlschlegel J.A., Lill R.;
RT "Human CIA2A-FAM96A and CIA2B-FAM96B integrate iron homeostasis and
RT maturation of different subsets of cytosolic-nuclear iron-sulfur
RT proteins.";
RL Cell Metab. 18:187-198(2013).
RN [7]
RP ERRATUM OF PUBMED:23891004.
RX PubMed=29320706; DOI=10.1016/j.cmet.2017.12.009;
RA Stehling O., Mascarenhas J., Vashisht A.A., Sheftel A.D., Niggemeyer B.,
RA Roesser R., Pierik A.J., Wohlschlegel J.A., Lill R.;
RT "Human CIA2A-FAM96A and CIA2B-FAM96B Integrate Iron Homeostasis and
RT Maturation of Different Subsets of Cytosolic-Nuclear Iron-Sulfur
RT Proteins.";
RL Cell Metab. 27:263-263(2018).
RN [8]
RP FUNCTION, AND INTERACTION WITH APAF1.
RX PubMed=25716227; DOI=10.1002/ijc.29498;
RA Schwamb B., Pick R., Fernandez S.B., Voelp K., Heering J., Doetsch V.,
RA Boesser S., Jung J., Beinoraviciute-Kellner R., Wesely J., Zoernig I.,
RA Hammerschmidt M., Nowak M., Penzel R., Zatloukal K., Joos S., Rieker R.J.,
RA Agaimy A., Soeder S., Reid-Lombardo K.M., Kendrick M.L., Bardsley M.R.,
RA Hayashi Y., Asuzu D.T., Syed S.A., Ordog T., Zoernig M.;
RT "FAM96A is a novel pro-apoptotic tumor suppressor in gastrointestinal
RT stromal tumors.";
RL Int. J. Cancer 137:1318-1329(2015).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 31-157, SUBUNIT, SUBCELLULAR
RP LOCATION, ZINC-BINDING SITES, TISSUE SPECIFICITY, AND INTERACTION WITH
RP CIAO1.
RX PubMed=22683786; DOI=10.1107/s0907444912006592;
RA Chen K.E., Richards A.A., Ariffin J.K., Ross I.L., Sweet M.J., Kellie S.,
RA Kobe B., Martin J.L.;
RT "The mammalian DUF59 protein Fam96a forms two distinct types of domain-
RT swapped dimer.";
RL Acta Crystallogr. D 68:637-648(2012).
CC -!- FUNCTION: Component of the cytosolic iron-sulfur protein assembly (CIA)
CC complex, a multiprotein complex that mediates the incorporation of
CC iron-sulfur cluster into extramitochondrial Fe/S proteins
CC (PubMed:23891004). As a CIA complex component and in collaboration with
CC CIAO1 specifically matures ACO1 and stabilizes IREB2, connecting
CC cytosolic iron-sulfur protein maturation with cellular iron regulation
CC (PubMed:23891004). May play a role in chromosome segregation through
CC establishment of sister chromatid cohesion. May induce apoptosis in
CC collaboration with APAF1 (PubMed:25716227). {ECO:0000250,
CC ECO:0000269|PubMed:23891004, ECO:0000269|PubMed:25716227}.
CC -!- SUBUNIT: Monomer and homodimer (PubMed:22683786). Component of the CIA
CC complex (PubMed:23891004). Interacts with CIAO1 (PubMed:23891004,
CC PubMed:22683786). Interacts with IREB2 (PubMed:23891004). Interacts
CC with APAF1 (PubMed:25716227). {ECO:0000269|PubMed:22683786,
CC ECO:0000269|PubMed:23891004, ECO:0000269|PubMed:25716227}.
CC -!- INTERACTION:
CC Q9H5X1; P02652: APOA2; NbExp=3; IntAct=EBI-752069, EBI-1171525;
CC Q9H5X1; O76071: CIAO1; NbExp=14; IntAct=EBI-752069, EBI-725145;
CC Q9H5X1; Q9NX76: CMTM6; NbExp=3; IntAct=EBI-752069, EBI-1054315;
CC Q9H5X1; Q96BA8: CREB3L1; NbExp=5; IntAct=EBI-752069, EBI-6942903;
CC Q9H5X1; Q9BUN8: DERL1; NbExp=3; IntAct=EBI-752069, EBI-398977;
CC Q9H5X1; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-752069, EBI-12831978;
CC Q9H5X1; O00559: EBAG9; NbExp=3; IntAct=EBI-752069, EBI-8787095;
CC Q9H5X1; Q9Y282: ERGIC3; NbExp=3; IntAct=EBI-752069, EBI-781551;
CC Q9H5X1; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-752069, EBI-3918971;
CC Q9H5X1; P48165: GJA8; NbExp=3; IntAct=EBI-752069, EBI-17458373;
CC Q9H5X1; O15499: GSC2; NbExp=3; IntAct=EBI-752069, EBI-19954058;
CC Q9H5X1; Q9NZI2-2: KCNIP1; NbExp=3; IntAct=EBI-752069, EBI-22452746;
CC Q9H5X1; Q9H400: LIME1; NbExp=3; IntAct=EBI-752069, EBI-2830566;
CC Q9H5X1; Q5EB52: MEST; NbExp=3; IntAct=EBI-752069, EBI-1050204;
CC Q9H5X1; Q04941: PLP2; NbExp=3; IntAct=EBI-752069, EBI-608347;
CC Q9H5X1; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-752069, EBI-11721828;
CC Q9H5X1; Q96GM1: PLPPR2; NbExp=3; IntAct=EBI-752069, EBI-12955265;
CC Q9H5X1; O60831: PRAF2; NbExp=3; IntAct=EBI-752069, EBI-2506064;
CC Q9H5X1; Q6NTF9-3: RHBDD2; NbExp=3; IntAct=EBI-752069, EBI-17589229;
CC Q9H5X1; Q9NVD3-4: SETD4; NbExp=3; IntAct=EBI-752069, EBI-23709068;
CC Q9H5X1; H3BQL7: SIN3A; NbExp=3; IntAct=EBI-752069, EBI-13384308;
CC Q9H5X1; Q6PL24: TMED8; NbExp=6; IntAct=EBI-752069, EBI-11603430;
CC Q9H5X1; Q9UBN6: TNFRSF10D; NbExp=3; IntAct=EBI-752069, EBI-1044859;
CC Q9H5X1; Q15836: VAMP3; NbExp=3; IntAct=EBI-752069, EBI-722343;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22683786}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H5X1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H5X1-2; Sequence=VSP_042683;
CC -!- TISSUE SPECIFICITY: Substantially enriched in macrophages.
CC {ECO:0000269|PubMed:22683786}.
CC -!- SIMILARITY: Belongs to the MIP18 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; AK026528; BAB15496.1; -; mRNA.
DR EMBL; AK304202; BAH14131.1; -; mRNA.
DR EMBL; AK312171; BAG35105.1; -; mRNA.
DR EMBL; AC021541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471082; EAW77661.1; -; Genomic_DNA.
DR EMBL; CH471082; EAW77662.1; -; Genomic_DNA.
DR EMBL; BC008865; AAH08865.1; -; mRNA.
DR CCDS; CCDS10189.1; -. [Q9H5X1-1]
DR CCDS; CCDS45278.1; -. [Q9H5X1-2]
DR RefSeq; NP_001014812.1; NM_001014812.2. [Q9H5X1-2]
DR RefSeq; NP_001276037.1; NM_001289108.1. [Q9H5X1-2]
DR RefSeq; NP_115607.1; NM_032231.5. [Q9H5X1-1]
DR PDB; 2M5H; NMR; -; A=28-160.
DR PDB; 3UX2; X-ray; 1.80 A; A=31-157.
DR PDB; 3UX3; X-ray; 1.80 A; A/B=31-157.
DR PDBsum; 2M5H; -.
DR PDBsum; 3UX2; -.
DR PDBsum; 3UX3; -.
DR AlphaFoldDB; Q9H5X1; -.
DR BMRB; Q9H5X1; -.
DR SMR; Q9H5X1; -.
DR BioGRID; 123939; 191.
DR IntAct; Q9H5X1; 24.
DR MINT; Q9H5X1; -.
DR STRING; 9606.ENSP00000300030; -.
DR ChEMBL; CHEMBL4295943; -.
DR iPTMnet; Q9H5X1; -.
DR MetOSite; Q9H5X1; -.
DR PhosphoSitePlus; Q9H5X1; -.
DR BioMuta; FAM96A; -.
DR DMDM; 20455359; -.
DR EPD; Q9H5X1; -.
DR jPOST; Q9H5X1; -.
DR MassIVE; Q9H5X1; -.
DR MaxQB; Q9H5X1; -.
DR PaxDb; Q9H5X1; -.
DR PeptideAtlas; Q9H5X1; -.
DR PRIDE; Q9H5X1; -.
DR ProteomicsDB; 80937; -. [Q9H5X1-1]
DR ProteomicsDB; 80938; -. [Q9H5X1-2]
DR Antibodypedia; 25761; 114 antibodies from 18 providers.
DR DNASU; 84191; -.
DR Ensembl; ENST00000300030.8; ENSP00000300030.3; ENSG00000166797.11. [Q9H5X1-1]
DR Ensembl; ENST00000380290.7; ENSP00000369644.3; ENSG00000166797.11. [Q9H5X1-2]
DR Ensembl; ENST00000557835.5; ENSP00000454079.1; ENSG00000166797.11. [Q9H5X1-2]
DR GeneID; 84191; -.
DR KEGG; hsa:84191; -.
DR MANE-Select; ENST00000300030.8; ENSP00000300030.3; NM_032231.7; NP_115607.1.
DR UCSC; uc002amt.3; human. [Q9H5X1-1]
DR CTD; 84191; -.
DR DisGeNET; 84191; -.
DR GeneCards; CIAO2A; -.
DR HGNC; HGNC:26235; CIAO2A.
DR HPA; ENSG00000166797; Tissue enhanced (liver).
DR MIM; 618382; gene.
DR neXtProt; NX_Q9H5X1; -.
DR OpenTargets; ENSG00000166797; -.
DR PharmGKB; PA142671829; -.
DR VEuPathDB; HostDB:ENSG00000166797; -.
DR eggNOG; KOG3381; Eukaryota.
DR GeneTree; ENSGT00390000017697; -.
DR HOGENOM; CLU_075876_4_0_1; -.
DR InParanoid; Q9H5X1; -.
DR OMA; YISEGAH; -.
DR OrthoDB; 1408004at2759; -.
DR PhylomeDB; Q9H5X1; -.
DR TreeFam; TF323934; -.
DR PathwayCommons; Q9H5X1; -.
DR SignaLink; Q9H5X1; -.
DR BioGRID-ORCS; 84191; 112 hits in 1077 CRISPR screens.
DR ChiTaRS; FAM96A; human.
DR GenomeRNAi; 84191; -.
DR Pharos; Q9H5X1; Tbio.
DR PRO; PR:Q9H5X1; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9H5X1; protein.
DR Bgee; ENSG00000166797; Expressed in ileal mucosa and 185 other tissues.
DR ExpressionAtlas; Q9H5X1; baseline and differential.
DR Genevisible; Q9H5X1; HS.
DR GO; GO:0097361; C:CIA complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:UniProtKB.
DR GO; GO:0106035; P:protein maturation by [4Fe-4S] cluster transfer; IEA:InterPro.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IMP:UniProtKB.
DR Gene3D; 3.30.300.130; -; 1.
DR InterPro; IPR034904; FSCA_dom_sf.
DR InterPro; IPR039796; MIP18.
DR InterPro; IPR002744; MIP18-like.
DR PANTHER; PTHR12377; PTHR12377; 1.
DR Pfam; PF01883; FeS_assembly_P; 1.
DR SUPFAM; SSF117916; SSF117916; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome partition; Cytoplasm;
KW Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..160
FT /note="Cytosolic iron-sulfur assembly component 2A"
FT /id="PRO_0000212689"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="ligand shared between dimeric partners"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="ligand shared between dimeric partners"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="ligand shared between dimeric partners"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="ligand shared between dimeric partners"
FT VAR_SEQ 97..160
FT /note="GLCLRVKLQRCLPFKHKLEIYISEGTHSTEEDINKQINDKERVAAAMENPNL
FT REIVEQCVLEPD -> VGNLHF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042683"
FT HELIX 31..44
FT /evidence="ECO:0007829|PDB:3UX2"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:3UX2"
FT TURN 56..60
FT /evidence="ECO:0007829|PDB:3UX2"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:3UX2"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:3UX2"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:3UX2"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2M5H"
FT HELIX 92..107
FT /evidence="ECO:0007829|PDB:3UX2"
FT STRAND 112..120
FT /evidence="ECO:0007829|PDB:3UX3"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:3UX3"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:3UX2"
FT HELIX 136..144
FT /evidence="ECO:0007829|PDB:3UX2"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:3UX2"
SQ SEQUENCE 160 AA; 18355 MW; 8580E4E397067319 CRC64;
MQRVSGLLSW TLSRVLWLSG LSEPGAARQP RIMEEKALEV YDLIRTIRDP EKPNTLEELE
VVSESCVEVQ EINEEEYLVI IRFTPTVPHC SLATLIGLCL RVKLQRCLPF KHKLEIYISE
GTHSTEEDIN KQINDKERVA AAMENPNLRE IVEQCVLEPD
