MIIP_HUMAN
ID MIIP_HUMAN Reviewed; 388 AA.
AC Q5JXC2; C0KL22; Q96HU6; Q9H839; Q9HA00;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Migration and invasion-inhibitory protein;
DE AltName: Full=IGFBP2-binding protein;
DE AltName: Full=Invasion-inhibitory protein 45;
DE Short=IIp45;
GN Name=MIIP; Synonyms=IIP45;
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] (ISOFORMS 1 AND 2), AND VARIANTS ASN-99; SER-142
RP AND GLU-167.
RX PubMed=15867349; DOI=10.1158/0008-5472.can-04-3392;
RA Song S.W., Fuller G.N., Zheng H., Zhang W.;
RT "Inactivation of the invasion inhibitory gene IIp45 by alternative splicing
RT in gliomas.";
RL Cancer Res. 65:3562-3567(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Liu S., Wu Y., Zhang W.;
RT "Molecular cloning and bioinformatic analysis of IIP45 gene.";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ASN-99 AND
RP GLU-167.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-167.
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ASN-99 AND
RP GLU-167.
RC TISSUE=Skin;
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 FUNCTION, REGION, TISSUE SPECIFICITY, AND INTERACTION WITH IGFBP2.
RX PubMed=14617774; DOI=10.1073/pnas.2332186100;
RA Song S.W., Fuller G.N., Khan A., Kong S., Shen W., Taylor E., Ramdas L.,
RA Lang F.F., Zhang W.;
RT "IIp45, an insulin-like growth factor binding protein 2 (IGFBP-2) binding
RT protein, antagonizes IGFBP-2 stimulation of glioma cell invasion.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13970-13975(2003).
RN [8]
RP INDUCTION BY IGFBP2.
RX PubMed=16901920; DOI=10.1677/jme.1.01955;
RA Frommer K.W., Reichenmiller K., Schutt B.S., Hoeflich A., Ranke M.B.,
RA Dodt G., Elmlinger M.W.;
RT "IGF-independent effects of IGFBP-2 on the human breast cancer cell line
RT Hs578T.";
RL J. Mol. Endocrinol. 37:13-23(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141 AND SER-303, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Inhibits glioma cells invasion and down-regulates
CC adhesion- and motility-associated genes such as NFKB2 and ICAM1.
CC Exhibits opposing effects to IGFBP2 on cell invasion.
CC {ECO:0000269|PubMed:14617774}.
CC -!- SUBUNIT: Interacts with IGFBP2. {ECO:0000269|PubMed:14617774}.
CC -!- INTERACTION:
CC Q5JXC2; O75934: BCAS2; NbExp=3; IntAct=EBI-2801965, EBI-1050106;
CC Q5JXC2; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-2801965, EBI-744556;
CC Q5JXC2; P28329-3: CHAT; NbExp=3; IntAct=EBI-2801965, EBI-25837549;
CC Q5JXC2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-2801965, EBI-3867333;
CC Q5JXC2; Q5JVL4: EFHC1; NbExp=3; IntAct=EBI-2801965, EBI-743105;
CC Q5JXC2; P60228: EIF3E; NbExp=3; IntAct=EBI-2801965, EBI-347740;
CC Q5JXC2; P22607: FGFR3; NbExp=3; IntAct=EBI-2801965, EBI-348399;
CC Q5JXC2; O43559: FRS3; NbExp=3; IntAct=EBI-2801965, EBI-725515;
CC Q5JXC2; P06396: GSN; NbExp=3; IntAct=EBI-2801965, EBI-351506;
CC Q5JXC2; P01112: HRAS; NbExp=3; IntAct=EBI-2801965, EBI-350145;
CC Q5JXC2; Q7L273: KCTD9; NbExp=3; IntAct=EBI-2801965, EBI-4397613;
CC Q5JXC2; Q5T749: KPRP; NbExp=3; IntAct=EBI-2801965, EBI-10981970;
CC Q5JXC2; O76011: KRT34; NbExp=3; IntAct=EBI-2801965, EBI-1047093;
CC Q5JXC2; Q9H204: MED28; NbExp=3; IntAct=EBI-2801965, EBI-514199;
CC Q5JXC2; P42568: MLLT3; NbExp=3; IntAct=EBI-2801965, EBI-716132;
CC Q5JXC2; Q70IA6: MOB2; NbExp=3; IntAct=EBI-2801965, EBI-2558739;
CC Q5JXC2; O43482: OIP5; NbExp=3; IntAct=EBI-2801965, EBI-536879;
CC Q5JXC2; P32242: OTX1; NbExp=3; IntAct=EBI-2801965, EBI-740446;
CC Q5JXC2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2801965, EBI-5235340;
CC Q5JXC2; O75716: STK16; NbExp=4; IntAct=EBI-2801965, EBI-749295;
CC Q5JXC2; Q9BT92: TCHP; NbExp=3; IntAct=EBI-2801965, EBI-740781;
CC Q5JXC2; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-2801965, EBI-750487;
CC Q5JXC2; Q08117-2: TLE5; NbExp=3; IntAct=EBI-2801965, EBI-11741437;
CC Q5JXC2; Q15654: TRIP6; NbExp=3; IntAct=EBI-2801965, EBI-742327;
CC Q5JXC2; Q8N6Y0: USHBP1; NbExp=5; IntAct=EBI-2801965, EBI-739895;
CC Q5JXC2; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-2801965, EBI-740727;
CC Q5JXC2; Q9Y649; NbExp=3; IntAct=EBI-2801965, EBI-25900580;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5JXC2-1; Sequence=Displayed;
CC Name=2; Synonyms=IIP45S;
CC IsoId=Q5JXC2-2; Sequence=VSP_032214;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Isoform 1 is expressed in brain but
CC underexpressed in glioma tissues, at protein level. Isoform 2 is not
CC detected in normal organs, but is expressed in gliomas with increasing
CC levels with glioma progression. On the contrary, at protein level,
CC isoform 2 is not detected in gliomas, suggesting that this isoform is
CC unstable in glioma cells. {ECO:0000269|PubMed:14617774}.
CC -!- INDUCTION: Up-regulated by IGFBP2. {ECO:0000269|PubMed:16901920}.
CC -!- PTM: Isoform 2 is degraded by the ubiquitin-proteasome pathway.
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DR EMBL; FJ618905; ACM90320.1; -; mRNA.
DR EMBL; AK022500; BAB14062.1; -; mRNA.
DR EMBL; AK024020; BAB14781.1; -; mRNA.
DR EMBL; AL096840; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471130; EAW71729.1; -; Genomic_DNA.
DR EMBL; BC008068; AAH08068.1; -; mRNA.
DR CCDS; CCDS143.1; -. [Q5JXC2-1]
DR RefSeq; NP_068752.2; NM_021933.3. [Q5JXC2-1]
DR RefSeq; XP_011540197.1; XM_011541895.1. [Q5JXC2-1]
DR RefSeq; XP_011540198.1; XM_011541896.1. [Q5JXC2-1]
DR AlphaFoldDB; Q5JXC2; -.
DR SMR; Q5JXC2; -.
DR BioGRID; 121947; 44.
DR IntAct; Q5JXC2; 41.
DR STRING; 9606.ENSP00000235332; -.
DR iPTMnet; Q5JXC2; -.
DR PhosphoSitePlus; Q5JXC2; -.
DR BioMuta; MIIP; -.
DR DMDM; 296439302; -.
DR EPD; Q5JXC2; -.
DR jPOST; Q5JXC2; -.
DR MassIVE; Q5JXC2; -.
DR MaxQB; Q5JXC2; -.
DR PaxDb; Q5JXC2; -.
DR PeptideAtlas; Q5JXC2; -.
DR PRIDE; Q5JXC2; -.
DR ProteomicsDB; 63443; -. [Q5JXC2-1]
DR ProteomicsDB; 63444; -. [Q5JXC2-2]
DR Antibodypedia; 28442; 120 antibodies from 21 providers.
DR DNASU; 60672; -.
DR Ensembl; ENST00000235332.6; ENSP00000235332.4; ENSG00000116691.11. [Q5JXC2-1]
DR GeneID; 60672; -.
DR KEGG; hsa:60672; -.
DR MANE-Select; ENST00000235332.6; ENSP00000235332.4; NM_021933.4; NP_068752.2.
DR UCSC; uc001ato.3; human. [Q5JXC2-1]
DR CTD; 60672; -.
DR DisGeNET; 60672; -.
DR GeneCards; MIIP; -.
DR HGNC; HGNC:25715; MIIP.
DR HPA; ENSG00000116691; Low tissue specificity.
DR MIM; 608772; gene.
DR neXtProt; NX_Q5JXC2; -.
DR OpenTargets; ENSG00000116691; -.
DR PharmGKB; PA165751598; -.
DR VEuPathDB; HostDB:ENSG00000116691; -.
DR eggNOG; ENOG502RZQ8; Eukaryota.
DR GeneTree; ENSGT00390000003768; -.
DR HOGENOM; CLU_061576_0_0_1; -.
DR InParanoid; Q5JXC2; -.
DR OMA; PHVPRQK; -.
DR OrthoDB; 1259790at2759; -.
DR PhylomeDB; Q5JXC2; -.
DR TreeFam; TF335829; -.
DR PathwayCommons; Q5JXC2; -.
DR SignaLink; Q5JXC2; -.
DR BioGRID-ORCS; 60672; 24 hits in 1075 CRISPR screens.
DR ChiTaRS; MIIP; human.
DR GenomeRNAi; 60672; -.
DR Pharos; Q5JXC2; Tbio.
DR PRO; PR:Q5JXC2; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5JXC2; protein.
DR Bgee; ENSG00000116691; Expressed in granulocyte and 206 other tissues.
DR Genevisible; Q5JXC2; HS.
DR GO; GO:0030336; P:negative regulation of cell migration; IEA:InterPro.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IEA:InterPro.
DR InterPro; IPR031466; MIIP.
DR PANTHER; PTHR34831; PTHR34831; 1.
DR Pfam; PF15734; MIIP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Phosphoprotein; Reference proteome.
FT CHAIN 1..388
FT /note="Migration and invasion-inhibitory protein"
FT /id="PRO_0000324322"
FT REGION 32..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 239..282
FT /note="Interaction with IGFBP2"
FT /evidence="ECO:0000269|PubMed:14617774"
FT REGION 344..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..388
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 141
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 282..388
FT /note="RVSIPLSILEPPHRYHIHRRKSFDASDTLALPRHCLLGWDIFPPKSEKSSAP
FT RNLDLWSSVSAEAQHQKLSGTSSPFHPASPMQMLPPTPTWSVPQVPRPHVPRQKP ->
FT STACWAGTFFLRSLRKAQPPGTWTSGPLYPLRPSTRSCPAPAQALFTRPHQCRCCPRPR
FT PGQCPRSLGPTSHGRSPED (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15867349"
FT /id="VSP_032214"
FT VARIANT 99
FT /note="K -> N (in dbSNP:rs11553925)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15867349"
FT /id="VAR_039729"
FT VARIANT 142
FT /note="P -> S (in dbSNP:rs11588712)"
FT /evidence="ECO:0000269|PubMed:15867349"
FT /id="VAR_039730"
FT VARIANT 167
FT /note="K -> E (in dbSNP:rs2295283)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15867349,
FT ECO:0000269|Ref.5"
FT /id="VAR_039731"
FT VARIANT 247
FT /note="R -> W (in dbSNP:rs2295289)"
FT /id="VAR_059688"
FT VARIANT 288
FT /note="S -> L (in dbSNP:rs35317667)"
FT /id="VAR_059689"
FT VARIANT 381
FT /note="P -> S (in dbSNP:rs34874602)"
FT /id="VAR_059690"
FT CONFLICT 183
FT /note="G -> V (in Ref. 2; BAB14062)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 388 AA; 42824 MW; 31854F9B1669B00C CRC64;
MVEAEELAQL RLLNLELLRQ LWVGQDAVRR SVARAASESS LESSSSYNSE TPSTPETSST
SLSTSCPRGR SSVWGPPDAC RGDLRDVARS GVASLPPAKC QHQESLGRPR PHSAPSLGTS
SLRDPEPSGR LGDPGPQEAQ TPRSILAQQS KLSKPRVTFS EESAVPKRSW RLRPYLGYDW
IAGSLDTSSS ITSQPEAFFS KLQEFRETNK EECICSHPEP QLPGLRESSG SGVEEDHECV
YCYRVNRRLF PVPVDPGTPC RLCRTPRDQQ GPGTLAQPAH VRVSIPLSIL EPPHRYHIHR
RKSFDASDTL ALPRHCLLGW DIFPPKSEKS SAPRNLDLWS SVSAEAQHQK LSGTSSPFHP
ASPMQMLPPT PTWSVPQVPR PHVPRQKP
