CEMIP_MOUSE
ID CEMIP_MOUSE Reviewed; 1361 AA.
AC Q8BI06; E9QJS6; Q6L9J4; Q9EPQ3; Q9EPQ4;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Cell migration-inducing and hyaluronan-binding protein;
DE EC=3.2.1.35 {ECO:0000269|PubMed:24251095};
DE AltName: Full=Protein 12H19.01.T7;
DE Flags: Precursor;
GN Name=Cemip; Synonyms=Kiaa1199 {ECO:0000303|PubMed:14577002};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE OF 901-1293
RP (ISOFORM 1), TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Swiss Webster / NIH;
RX PubMed=11247670; DOI=10.1006/geno.2000.6466;
RA Wines M.E., Lee L., Katari M.S., Zhang L., DeRossi C., Shi Y., Perkins S.,
RA Feldman M., McCombie W.R., Holdener B.C.;
RT "Identification of mesoderm development (mesd) candidate genes by
RT comparative mapping and genome sequence analysis.";
RL Genomics 72:88-98(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=14577002; DOI=10.1007/s10038-003-0079-2;
RA Abe S., Usami S., Nakamura Y.;
RT "Mutations in the gene encoding KIAA1199 protein, an inner-ear protein
RT expressed in Deiters' cells and the fibrocytes, as the cause of
RT nonsyndromic hearing loss.";
RL J. Hum. Genet. 48:564-570(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Vagina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 962-1361 (ISOFORM 1).
RC STRAIN=C57BL/6J; 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 [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18448257; DOI=10.1016/j.neuroscience.2008.03.018;
RA Usami S., Takumi Y., Suzuki N., Oguchi T., Oshima A., Suzuki H., Kitoh R.,
RA Abe S., Sasaki A., Matsubara A.;
RT "The localization of proteins encoded by CRYM, KIAA1199, UBA52, COL9A3, and
RT COL9A1, genes highly expressed in the cochlea.";
RL Neuroscience 154:22-28(2008).
RN [7]
RP FUNCTION IN HYALURONAN DEGRADATION, CATALYTIC ACTIVITY, HYALURONAN-BINDING,
RP AND SUBCELLULAR LOCATION.
RX PubMed=24251095; DOI=10.1016/j.fob.2013.08.003;
RA Yoshida H., Nagaoka A., Nakamura S., Sugiyama Y., Okada Y., Inoue S.;
RT "Murine homologue of the human KIAA1199 is implicated in hyaluronan binding
RT and depolymerization.";
RL FEBS Open Bio 3:352-356(2013).
CC -!- FUNCTION: Mediates depolymerization of hyaluronic acid (HA) via the
CC cell membrane-associated clathrin-coated pit endocytic pathway. Binds
CC to hyaluronic acid. Hydrolyzes high molecular weight hyaluronic acid to
CC produce an intermediate-sized product, a process that may occur through
CC rapid vesicle endocytosis and recycling without intracytoplasmic
CC accumulation or digestion in lysosomes. Involved in hyaluronan
CC catabolism in the dermis of the skin and arthritic synovium. Positively
CC regulates epithelial-mesenchymal transition (EMT), and hence tumor cell
CC growth, invasion and cancer dissemination. In collaboration with
CC HSPA5/BIP, promotes cancer cell migration in a calcium and PKC-
CC dependent manner. May be involved in hearing.
CC {ECO:0000269|PubMed:24251095}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-
CC glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35;
CC Evidence={ECO:0000269|PubMed:24251095};
CC -!- ACTIVITY REGULATION: Activity is up-regulated by histamine.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with EPHA2 and ITPR3. Interacts with HSPA5/BIP; the
CC interaction induces calcium leakage from the endoplasmic reticulum and
CC cell migration. Interacts with clathrin heavy chain/CLTC (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Endoplasmic reticulum {ECO:0000250}. Cell membrane {ECO:0000250}.
CC Membrane, clathrin-coated pit {ECO:0000269|PubMed:18448257,
CC ECO:0000269|PubMed:24251095}. Secreted {ECO:0000250}. Note=Retained in
CC the endoplasmic reticulum (ER) in a HSPA5/BIP-dependent manner.
CC Strongly detected in the cytoplasm of breast carcinoma cells, whereas
CC poorly detected in adjacent normal epithelial cells, stromal cells, or
CC benign breast tissues. Localized in the nucleus and cytoplasm of colon
CC adenocarcinomas (By similarity). Colocalized with clathrin heavy
CC chain/CLTC in clathrin-coated vesicles. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BI06-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BI06-2; Sequence=VSP_009816;
CC Name=3;
CC IsoId=Q8BI06-3; Sequence=VSP_009817;
CC -!- TISSUE SPECIFICITY: Expressed in Deiters' cells and various supporting
CC cells in the organ of Corti including inner phalangeal, border, inner
CC and outer pillar cells (at protein level). Weakly expressed in brain
CC and testis. In ear, it is specifically expressed in inner ear.
CC Expressed in Deiters' cells in the organ of Corti at P0 (postnatal day
CC zero) before the onset of hearing, but disappears by day P7. Also
CC expressed in fibrocytes of the spiral ligament and the spiral limbus
CC through to P21, when the cochlea matures. {ECO:0000269|PubMed:11247670,
CC ECO:0000269|PubMed:14577002, ECO:0000269|PubMed:18448257}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development.
CC {ECO:0000269|PubMed:11247670}.
CC -!- DOMAIN: The signal sequence is essential in mediating its proper
CC translocation, hyaluronic acid (HA) degradation activity and secretion.
CC {ECO:0000250}.
CC -!- PTM: N-glycosylated; glycosylation is not necessary for HA-binding.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CEMIP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH56981.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC29586.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY007814; AAG41061.1; -; mRNA.
DR EMBL; AY007815; AAG41062.1; -; mRNA.
DR EMBL; AB103331; BAD02452.1; -; mRNA.
DR EMBL; AK036809; BAC29586.1; ALT_SEQ; mRNA.
DR EMBL; AC101659; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC056981; AAH56981.1; ALT_INIT; mRNA.
DR CCDS; CCDS21416.1; -. [Q8BI06-1]
DR RefSeq; NP_109653.3; NM_030728.4. [Q8BI06-1]
DR RefSeq; XP_006508416.1; XM_006508353.3. [Q8BI06-1]
DR RefSeq; XP_006508417.1; XM_006508354.3. [Q8BI06-1]
DR RefSeq; XP_017167893.1; XM_017312404.1.
DR AlphaFoldDB; Q8BI06; -.
DR SMR; Q8BI06; -.
DR BioGRID; 219857; 1.
DR IntAct; Q8BI06; 1.
DR STRING; 10090.ENSMUSP00000063277; -.
DR GlyGen; Q8BI06; 6 sites.
DR iPTMnet; Q8BI06; -.
DR PhosphoSitePlus; Q8BI06; -.
DR MaxQB; Q8BI06; -.
DR PaxDb; Q8BI06; -.
DR PRIDE; Q8BI06; -.
DR ProteomicsDB; 281532; -. [Q8BI06-1]
DR ProteomicsDB; 281533; -. [Q8BI06-2]
DR ProteomicsDB; 281534; -. [Q8BI06-3]
DR Antibodypedia; 27890; 230 antibodies from 25 providers.
DR Ensembl; ENSMUST00000064174; ENSMUSP00000063277; ENSMUSG00000052353. [Q8BI06-1]
DR GeneID; 80982; -.
DR KEGG; mmu:80982; -.
DR UCSC; uc009idy.3; mouse. [Q8BI06-2]
DR UCSC; uc009idz.2; mouse. [Q8BI06-1]
DR CTD; 57214; -.
DR MGI; MGI:2443629; Cemip.
DR VEuPathDB; HostDB:ENSMUSG00000052353; -.
DR eggNOG; ENOG502QT0K; Eukaryota.
DR GeneTree; ENSGT00940000153636; -.
DR HOGENOM; CLU_005606_1_0_1; -.
DR InParanoid; Q8BI06; -.
DR OMA; DGHHGKV; -.
DR OrthoDB; 294134at2759; -.
DR PhylomeDB; Q8BI06; -.
DR TreeFam; TF316575; -.
DR Reactome; R-MMU-2142850; Hyaluronan biosynthesis and export.
DR BioGRID-ORCS; 80982; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Cemip; mouse.
DR PRO; PR:Q8BI06; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BI06; protein.
DR Bgee; ENSMUSG00000052353; Expressed in vault of skull and 115 other tissues.
DR Genevisible; Q8BI06; MM.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; ISS:UniProtKB.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032050; F:clathrin heavy chain binding; ISS:UniProtKB.
DR GO; GO:0046923; F:ER retention sequence binding; ISS:UniProtKB.
DR GO; GO:0005540; F:hyaluronic acid binding; IDA:UniProtKB.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IDA:UniProtKB.
DR GO; GO:0030214; P:hyaluronan catabolic process; IDA:UniProtKB.
DR GO; GO:0030212; P:hyaluronan metabolic process; IMP:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISS:UniProtKB.
DR GO; GO:1900020; P:positive regulation of protein kinase C activity; ISS:UniProtKB.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR GO; GO:0007605; P:sensory perception of sound; ISO:MGI.
DR CDD; cd13938; PANDER_like_TMEM2; 1.
DR InterPro; IPR019316; G8_domain.
DR InterPro; IPR039477; ILEI/PANDER_dom.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR039473; TMEM2_PANDER-like.
DR InterPro; IPR025155; WxxW_domain.
DR Pfam; PF10162; G8; 1.
DR Pfam; PF15711; ILEI; 2.
DR Pfam; PF13330; Mucin2_WxxW; 1.
DR SMART; SM01225; G8; 1.
DR SUPFAM; SSF51126; SSF51126; 2.
DR PROSITE; PS51484; G8; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coated pit; Cytoplasm;
KW Endoplasmic reticulum; Glycoprotein; Glycosidase; Hyaluronic acid;
KW Hydrolase; Membrane; Nucleus; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000250"
FT CHAIN 31..1361
FT /note="Cell migration-inducing and hyaluronan-binding
FT protein"
FT /id="PRO_0000021539"
FT DOMAIN 44..166
FT /note="G8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00817"
FT REPEAT 572..594
FT /note="PbH1 1"
FT REPEAT 595..617
FT /note="PbH1 2"
FT REPEAT 719..741
FT /note="PbH1 3"
FT REPEAT 798..819
FT /note="PbH1 4"
FT REGION 295..591
FT /note="Necessary for its endoplasmic reticulum (ER)
FT retention and interaction with HSPA5"
FT /evidence="ECO:0000250"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 889
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 921
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..1155
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11247670"
FT /id="VSP_009816"
FT VAR_SEQ 1137..1361
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009817"
FT CONFLICT 197
FT /note="K -> E (in Ref. 3; BAC29586)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="I -> V (in Ref. 2; BAD02452)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="K -> N (in Ref. 3; BAC29586)"
FT /evidence="ECO:0000305"
FT CONFLICT 880
FT /note="F -> L (in Ref. 3; BAC29586)"
FT /evidence="ECO:0000305"
FT CONFLICT 1268..1270
FT /note="ILQ -> PEF (in Ref. 1; AAG41062)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1361 AA; 153034 MW; ACAFA439574B9E8C CRC64;
MRASGRHDVS LKIVLATGCL LLANFSGASS AVATECPDQS PELQPWSPGH NRDYQVHIGH
GRKLLLTSSA TVHSITISGG GKLVIKDHHE HIVLRTRYIL IDDGGELHAG SALCPFEGNF
SIVLYGRADE NILPDPYYGL KYIGVDKGGT LELHGQKKLS WTFLNKTLHP GGMQEGGYFF
ERSWGHRGVI VHVIDAKLGT VVHSDRFDTY RSKKESERLV QYLNAVPDGR ILSVAVNDEG
SRNLDDTARK AMTKLGSKHF LHLGFRHPWS FITVKGNPSS SVEDHIEYHG HKGSAAARVF
KLFQTEHGEH FNVSSSSEWV QDVEWTEWFD HDKVPQSKGG EKISDLRAAY PGKICNRPID
IQATTMDGVA LSTEVVYKNG QDYRFACYTR GRACRSYRVR FLCGKPVRPK LTVSIDTNVN
STILSLVDNV RSWRPGDTLV VASTDYSMYQ AEEFRVLPCK ACTSTQVKVA GKPQYLHIGE
EIDGVDMRAE VGLLTRNIVV MGEMEDRCYP YTNHICDFFD FDTFGGHIKF ALGFKAAHLE
GVELKYMGQQ LVGQYPIHFH LAGDLDEQGG YDPPTYIRDL SIHHTFSRCI TVHGSNGLLI
KDVVGYNSLG HCFFTEDGPE ERNTFDHCLG LLVKSGTLLP SDRDSRMCKV ITEDSYPGYI
PKPRQDCNAV STFWMANPNN NLINCAAAGS EETGFWFIFH HVPTGPSVGM YSPGYSEHIP
LGKFYNNRAH SNYRAGMIID NGVKTTEASA KDKRPFLSII SARYSPHQDA DPLKPREPAI
IRHFTAYKNQ DHGAWLRGGD VWLDSCRFAD NGIGLTLASG GTFPYDDGSK QEIKNSLFVG
ESGNVGTEMM DNRIWGPGGL DHSGRTLPIG QNFPIRGIQF YDGPINIQNC TFRKFAALEG
RHTSALAFRL NNAWQSCPHN NVTNIAFEDV PITSRVFFGE PGPWFNQLDM DGDKTSVFHD
LDGSVSEYPG SYLTKDDNWL VRHPDCINVP DWRGAICSGR YAQMYIQAYK SSNLRMKIIK
NDFPSHPLYL EGALTRSTHY QQYQPVITLQ KGYTIHWDQT APAELAIWLI NFNKGDWIRV
GLCYPRGTTF SILSDVHNRL LKQTSKTGTF VRTLQMDKVE QSYPGRSHYY WDEDSGLLFL
KLKAQNEREK FAFCSMKGCE RIKIKALLPR NAGISDCTAT AYPRFTERAI VDVPMPRKLF
GAQLKTKDHF LEVKMESSRQ HFFHLRNDFA YIEVDGRRYP CSEDGIQIVV IDGSRGHVVS
HGSFRNAILQ GIPWQLFNYV AAIPDNSIVL MASKGRYITR GPWTRVLEKL GADKGLKLKE
KMAFVGFKGS FRPIWVTLET EDHKAKIFQV VPIPVVRKKK L
