RHPN2_HUMAN
ID RHPN2_HUMAN Reviewed; 686 AA.
AC Q8IUC4; B2RCG8; B3KUY8; B4DUS7; Q8N3T7; Q8N9D6; Q8NE33; Q96RU1;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Rhophilin-2;
DE AltName: Full=76 kDa RhoB effector protein;
DE AltName: Full=GTP-Rho-binding protein 2;
DE AltName: Full=p76RBE;
GN Name=RHPN2;
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), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INDUCTION, AND INTERACTION WITH RHOA AND KRT18.
RX PubMed=12473120; DOI=10.1046/j.1432-1033.2002.03343.x;
RA Mircescu H., Steuve S., Savonet V., Degraef C., Mellor H., Dumont J.E.,
RA Maenhaut C., Pirson I.;
RT "Identification and characterization of a novel activated RhoB binding
RT protein containing a PDZ domain whose expression is specifically modulated
RT in thyroid cells by cAMP.";
RL Eur. J. Biochem. 269:6241-6249(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP INTERACTION WITH RHOA, MUTAGENESIS OF 58-GLU-ASN-59; ARG-518 AND
RP 526-LEU-GLY-527, AND VARIANT GLN-70.
RC TISSUE=Kidney;
RX PubMed=12221077; DOI=10.1074/jbc.m203569200;
RA Peck J.W., Oberst M., Bouker K.B., Bowden E., Burbelo P.D.;
RT "The RhoA-binding protein, rhophilin-2, regulates actin cytoskeleton
RT organization.";
RL J. Biol. Chem. 277:43924-43932(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Korkmaz K.S., Korkmaz C.G., Saatcioglu F.;
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Hippocampus, Placenta, and Uterus;
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 MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-686 (ISOFORM 1).
RC TISSUE=Amygdala;
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 514-595.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the PDZ domain of human rhophilin-2.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Binds specifically to GTP-Rho. May function in a Rho pathway
CC to limit stress fiber formation and/or increase the turnover of F-actin
CC structures in the absence of high levels of RhoA activity.
CC {ECO:0000269|PubMed:12221077}.
CC -!- SUBUNIT: Interacts with GTP-bound RhoA and RhoB. Interacts with both
CC GTP- and GDP-bound RhoA. According to PubMed:12473120, it does not
CC interact with RhoA. Interacts with KRT18. {ECO:0000269|PubMed:12221077,
CC ECO:0000269|PubMed:12473120}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:12473120}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IUC4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IUC4-2; Sequence=VSP_055548;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in prostate,
CC trachea, stomach, colon, thyroid and pancreas. Expressed at lower level
CC in brain, spinal cord, kidney, placenta and liver.
CC {ECO:0000269|PubMed:12221077, ECO:0000269|PubMed:12473120}.
CC -!- INDUCTION: By thyrotropin (TSH). Regulated by the cAMP pathway.
CC {ECO:0000269|PubMed:12473120}.
CC -!- SIMILARITY: Belongs to the RHPN family. {ECO:0000305}.
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DR EMBL; AJ347750; CAC87939.1; -; mRNA.
DR EMBL; AF268032; AAK58588.1; -; mRNA.
DR EMBL; AF423421; AAQ04062.1; -; mRNA.
DR EMBL; AK095001; BAC04471.1; -; mRNA.
DR EMBL; AK098246; BAG53600.1; -; mRNA.
DR EMBL; AK300775; BAG62439.1; -; mRNA.
DR EMBL; AK315105; BAG37565.1; -; mRNA.
DR EMBL; AC008521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036447; AAH36447.1; -; mRNA.
DR EMBL; AL831950; CAD38597.1; -; mRNA.
DR CCDS; CCDS12427.1; -. [Q8IUC4-1]
DR RefSeq; NP_149094.3; NM_033103.4. [Q8IUC4-1]
DR PDB; 2VSV; X-ray; 1.82 A; A/B=514-595.
DR PDBsum; 2VSV; -.
DR AlphaFoldDB; Q8IUC4; -.
DR SMR; Q8IUC4; -.
DR BioGRID; 124521; 36.
DR IntAct; Q8IUC4; 8.
DR MINT; Q8IUC4; -.
DR STRING; 9606.ENSP00000254260; -.
DR iPTMnet; Q8IUC4; -.
DR PhosphoSitePlus; Q8IUC4; -.
DR SwissPalm; Q8IUC4; -.
DR BioMuta; RHPN2; -.
DR DMDM; 62288912; -.
DR EPD; Q8IUC4; -.
DR jPOST; Q8IUC4; -.
DR MassIVE; Q8IUC4; -.
DR MaxQB; Q8IUC4; -.
DR PaxDb; Q8IUC4; -.
DR PeptideAtlas; Q8IUC4; -.
DR PRIDE; Q8IUC4; -.
DR ProteomicsDB; 5211; -.
DR ProteomicsDB; 70543; -. [Q8IUC4-1]
DR Antibodypedia; 28974; 142 antibodies from 31 providers.
DR DNASU; 85415; -.
DR Ensembl; ENST00000254260.8; ENSP00000254260.2; ENSG00000131941.8. [Q8IUC4-1]
DR GeneID; 85415; -.
DR KEGG; hsa:85415; -.
DR MANE-Select; ENST00000254260.8; ENSP00000254260.2; NM_033103.5; NP_149094.3.
DR UCSC; uc002nuf.4; human. [Q8IUC4-1]
DR CTD; 85415; -.
DR DisGeNET; 85415; -.
DR GeneCards; RHPN2; -.
DR HGNC; HGNC:19974; RHPN2.
DR HPA; ENSG00000131941; Low tissue specificity.
DR MIM; 617932; gene.
DR neXtProt; NX_Q8IUC4; -.
DR OpenTargets; ENSG00000131941; -.
DR PharmGKB; PA134979284; -.
DR VEuPathDB; HostDB:ENSG00000131941; -.
DR eggNOG; KOG2220; Eukaryota.
DR GeneTree; ENSGT00940000153837; -.
DR HOGENOM; CLU_006514_1_1_1; -.
DR InParanoid; Q8IUC4; -.
DR OMA; MICLAYD; -.
DR OrthoDB; 641122at2759; -.
DR PhylomeDB; Q8IUC4; -.
DR TreeFam; TF323502; -.
DR PathwayCommons; Q8IUC4; -.
DR Reactome; R-HSA-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR SignaLink; Q8IUC4; -.
DR BioGRID-ORCS; 85415; 18 hits in 1080 CRISPR screens.
DR ChiTaRS; RHPN2; human.
DR EvolutionaryTrace; Q8IUC4; -.
DR GeneWiki; RHPN2; -.
DR GenomeRNAi; 85415; -.
DR Pharos; Q8IUC4; Tbio.
DR PRO; PR:Q8IUC4; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8IUC4; protein.
DR Bgee; ENSG00000131941; Expressed in epithelial cell of pancreas and 142 other tissues.
DR ExpressionAtlas; Q8IUC4; baseline and differential.
DR Genevisible; Q8IUC4; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0003094; P:glomerular filtration; IEA:Ensembl.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IDA:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.25.40.280; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR004328; BRO1_dom.
DR InterPro; IPR038499; BRO1_sf.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF03097; BRO1; 1.
DR Pfam; PF02185; HR1; 1.
DR SMART; SM01041; BRO1; 1.
DR SMART; SM00742; Hr1; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF46585; SSF46585; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS51180; BRO1; 1.
DR PROSITE; PS51860; REM_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..686
FT /note="Rhophilin-2"
FT /id="PRO_0000218898"
FT DOMAIN 26..100
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 111..460
FT /note="BRO1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT DOMAIN 515..593
FT /note="PDZ"
FT REGION 46..66
FT /note="Interaction with Rho"
FT MOD_RES 655
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BWR8"
FT VAR_SEQ 1..151
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055548"
FT VARIANT 70
FT /note="R -> Q (in dbSNP:rs28626308)"
FT /evidence="ECO:0000269|PubMed:12221077"
FT /id="VAR_061996"
FT VARIANT 342
FT /note="A -> P (in dbSNP:rs28407794)"
FT /id="VAR_061997"
FT MUTAGEN 58..59
FT /note="EN->AA: Abolishes interaction with RhoA."
FT /evidence="ECO:0000269|PubMed:12221077"
FT MUTAGEN 518
FT /note="R->A: Does not induce actin disassembly but still
FT interacts with RhoA; when associated with A-526 and A-527."
FT /evidence="ECO:0000269|PubMed:12221077"
FT MUTAGEN 526..527
FT /note="LG->AA: Does not induce actin disassembly but still
FT interacts with RhoA; when associated with A-518."
FT /evidence="ECO:0000269|PubMed:12221077"
FT CONFLICT 16
FT /note="E -> K (in Ref. 6; AAH36447)"
FT /evidence="ECO:0000305"
FT CONFLICT 51
FT /note="V -> M (in Ref. 4; BAG53600)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="G -> D (in Ref. 2; AAK58588)"
FT /evidence="ECO:0000305"
FT CONFLICT 207..214
FT /note="VSQQNLLL -> EPAEPGA (in Ref. 2; AAK58588)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="Q -> E (in Ref. 2; AAK58588)"
FT /evidence="ECO:0000305"
FT CONFLICT 261
FT /note="D -> VH (in Ref. 2; AAK58588)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="S -> C (in Ref. 2; AAK58588)"
FT /evidence="ECO:0000305"
FT CONFLICT 326
FT /note="A -> Q (in Ref. 2; AAK58588)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="S -> L (in Ref. 2; AAK58588)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="E -> V (in Ref. 4; BAG37565)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="G -> V (in Ref. 2; AAK58588)"
FT /evidence="ECO:0000305"
FT CONFLICT 412..418
FT /note="HLRRAMA -> TCADHG (in Ref. 2; AAK58588)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="M -> T (in Ref. 9; BAC04471)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="S -> T (in Ref. 2; AAK58588)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="V -> A (in Ref. 2; AAK58588)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="P -> A (in Ref. 2; AAK58588)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="V -> L (in Ref. 2; AAK58588)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="R -> K (in Ref. 2; AAK58588)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="L -> G (in Ref. 2; AAK58588)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="L -> V (in Ref. 2; AAK58588)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="E -> R (in Ref. 2; AAK58588)"
FT /evidence="ECO:0000305"
FT CONFLICT 598
FT /note="S -> P (in Ref. 9; BAC04471)"
FT /evidence="ECO:0000305"
FT CONFLICT 600
FT /note="M -> T (in Ref. 4; BAG37565)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="D -> N (in Ref. 2; AAK58588)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="N -> T (in Ref. 2; AAK58588)"
FT /evidence="ECO:0000305"
FT STRAND 515..519
FT /evidence="ECO:0007829|PDB:2VSV"
FT HELIX 522..524
FT /evidence="ECO:0007829|PDB:2VSV"
FT STRAND 528..535
FT /evidence="ECO:0007829|PDB:2VSV"
FT STRAND 537..541
FT /evidence="ECO:0007829|PDB:2VSV"
FT HELIX 546..549
FT /evidence="ECO:0007829|PDB:2VSV"
FT STRAND 557..561
FT /evidence="ECO:0007829|PDB:2VSV"
FT HELIX 571..579
FT /evidence="ECO:0007829|PDB:2VSV"
FT TURN 580..583
FT /evidence="ECO:0007829|PDB:2VSV"
FT STRAND 586..592
FT /evidence="ECO:0007829|PDB:2VSV"
SQ SEQUENCE 686 AA; 76993 MW; 8D6CA2F9B0405A00 CRC64;
MTDALLPAAP QPLEKENDGY FRKGCNPLAQ TGRSKLQNQR AALNQQILKA VRMRTGAENL
LKVATNSKVR EQVRLELSFV NSDLQMLKEE LEGLNISVGV YQNTEEAFTI PLIPLGLKET
KDVDFAVVLK DFILEHYSED GYLYEDEIAD LMDLRQACRT PSRDEAGVEL LMTYFIQLGF
VESRFFPPTR QMGLLFTWYD SLTGVPVSQQ NLLLEKASVL FNTGALYTQI GTRCDRQTQA
GLESAIDAFQ RAAGVLNYLK DTFTHTPSYD MSPAMLSVLV KMMLAQAQES VFEKISLPGI
RNEFFMLVKV AQEAAKVGEV YQQLHAAMSQ APVKENIPYS WASLACVKAH HYAALAHYFT
AILLIDHQVK PGTDLDHQEK CLSQLYDHMP EGLTPLATLK NDQQRRQLGK SHLRRAMAHH
EESVREASLC KKLRSIEVLQ KVLCAAQERS RLTYAQHQEE DDLLNLIDAP SVVAKTEQEV
DIILPQFSKL TVTDFFQKLG PLSVFSANKR WTPPRSIRFT AEEGDLGFTL RGNAPVQVHF
LDPYCSASVA GAREGDYIVS IQLVDCKWLT LSEVMKLLKS FGEDEIEMKV VSLLDSTSSM
HNKSATYSVG MQKTYSMICL AIDDDDKTDK TKKISKKLSF LSWGTNKNRQ KSASTLCLPS
VGAARPQVKK KLPSPFSLLN SDSSWY
