ID   FREM2_MOUSE             Reviewed;        3160 AA.
AC   Q6NVD0; Q4W2Q5; Q5H8C0; Q811G9; Q8C4G5; Q8CD46;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   24-JAN-2024, entry version 147.
DE   RecName: Full=FRAS1-related extracellular matrix protein 2;
DE   AltName: Full=ECM3 homolog;
DE   AltName: Full=NV domain-containing protein 1;
DE   Flags: Precursor;
GN   Name=Frem2; Synonyms=Nv1;
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 1), FUNCTION, TISSUE SPECIFICITY, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=15838507; DOI=10.1038/ng1549;
RA   Jadeja S., Smyth I., Pitera J.E., Taylor M.S., van Haelst M., Bentley E.,
RA   McGregor L., Hopkins J., Chalepakis G., Philip N., Perez Aytes A.,
RA   Watt F.M., Darling S.M., Jackson I., Woolf A.S., Scambler P.J.;
RT   "Identification of a new gene mutated in Fraser syndrome and mouse
RT   myelencephalic blebs.";
RL   Nat. Genet. 37:520-525(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Testis;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2277-3160.
RC   STRAIN=C57BL/6J, and Czech II; TISSUE=Head, and Mammary tumor;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 1-291.
RA   Kiyozumi D., Osada A., Sugimoto N., Weber C.N., Ono Y., Imai T., Okada A.,
RA   Sekiguchi K.;
RT   "QBRICK, a novel cell-adhesive protein expressed in the basement membrane
RT   of the developing hair follicle.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, Kidney, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=30802441; DOI=10.1016/j.exer.2019.02.013;
RA   Zhang X., Wang D., Dongye M., Zhu Y., Chen C., Wang R., Long E., Liu Z.,
RA   Wu X., Lin D., Chen J., Lin Z., Wang J., Li W., Li Y., Li D., Lin H.;
RT   "Loss-of-function mutations in FREM2 disrupt eye morphogenesis.";
RL   Exp. Eye Res. 181:302-312(2019).
CC   -!- FUNCTION: Extracellular matrix protein required for maintenance of the
CC       integrity of the skin epithelium and for maintenance of renal epithelia
CC       (By similarity). Required for epidermal adhesion (PubMed:15838507).
CC       Involved in the development of eyelids and the anterior segment of the
CC       eyeballs (PubMed:30802441). {ECO:0000250|UniProtKB:Q5SZK8,
CC       ECO:0000269|PubMed:15838507, ECO:0000269|PubMed:30802441}.
CC   -!- SUBUNIT: Interacts with FREM1. {ECO:0000250|UniProtKB:Q5SZK8}.
CC   -!- INTERACTION:
CC       Q6NVD0; Q80T14: Fras1; NbExp=2; IntAct=EBI-15594269, EBI-15594303;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q5SZK8};
CC       Single-pass type I membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6NVD0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NVD0-2; Sequence=VSP_015038, VSP_015039;
CC       Name=3;
CC         IsoId=Q6NVD0-3; Sequence=VSP_015037;
CC   -!- TISSUE SPECIFICITY: First expressed from 10 dpc in the mesodermal core
CC       of the branchial arches, developing lens, otic vesicle and limb apical
CC       ectodermal ridge. Later, it is expressed in the vibrissae and vibrissae
CC       pad, eyelids ear and pelage follicles and, at low levels, in the
CC       epidermis (PubMed:15838507). Also expressed in caudal somites and, in
CC       later embryos, in facial, limb and intercostal muscles
CC       (PubMed:15838507). In contrast to Frem1, it is not expressed in the
CC       developing mammary glands or in the caecum (PubMed:15838507).
CC       Restricted to the epithelia in a pattern complementary to that of Frem1
CC       (which is generally expressed in the dermis and mesenchyme)
CC       (PubMed:15838507). In the developing kidney, it is expressed At in the
CC       mesonephric and metanephric epithelia at 11.5 dpc, with a highest
CC       expression at the tips of the developing ureteric buds
CC       (PubMed:15838507). At 12.5 and 13.5 dpc, it is still expressed
CC       throughout the epithelial components of the kidney, including epithelia
CC       fated to form nephrons, which are induced by the ureter tips to
CC       differeintiate from the mesenchymal condensations that surround them
CC       (PubMed:15838507). Expressed in retinal neuron-containing outer
CC       plexiform layer (PubMed:30802441). {ECO:0000269|PubMed:15838507,
CC       ECO:0000269|PubMed:30802441}.
CC   -!- DOMAIN: The Calx-beta domains bind calcium with high affinity and
CC       undergo a major conformational shift upon binding. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Mice display cryptophthalmos, syndactyly and
CC       renal defects. Frem2 corresponds to the X-ray irradiated-induced allele
CC       'myelencephalic blebs' (my). {ECO:0000269|PubMed:15838507}.
CC   -!- SIMILARITY: Belongs to the FRAS1 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; AJ833643; CAH55760.1; -; mRNA.
DR   EMBL; AK031494; BAC27425.1; -; mRNA.
DR   EMBL; AK082256; BAC38448.1; -; mRNA.
DR   EMBL; BC046388; AAH46388.1; -; mRNA.
DR   EMBL; BC068185; AAH68185.1; -; mRNA.
DR   EMBL; AB160988; BAD89016.1; -; mRNA.
DR   CCDS; CCDS17348.1; -. [Q6NVD0-1]
DR   RefSeq; NP_766450.2; NM_172862.3. [Q6NVD0-1]
DR   SMR; Q6NVD0; -.
DR   DIP; DIP-61241N; -.
DR   IntAct; Q6NVD0; 2.
DR   STRING; 10090.ENSMUSP00000088670; -.
DR   GlyCosmos; Q6NVD0; 5 sites, No reported glycans.
DR   GlyGen; Q6NVD0; 6 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6NVD0; -.
DR   PhosphoSitePlus; Q6NVD0; -.
DR   EPD; Q6NVD0; -.
DR   MaxQB; Q6NVD0; -.
DR   PaxDb; 10090-ENSMUSP00000088670; -.
DR   ProteomicsDB; 266859; -. [Q6NVD0-1]
DR   ProteomicsDB; 266860; -. [Q6NVD0-2]
DR   ProteomicsDB; 266861; -. [Q6NVD0-3]
DR   Antibodypedia; 23253; 137 antibodies from 29 providers.
DR   DNASU; 242022; -.
DR   Ensembl; ENSMUST00000091137.6; ENSMUSP00000088670.5; ENSMUSG00000037016.12. [Q6NVD0-1]
DR   GeneID; 242022; -.
DR   KEGG; mmu:242022; -.
DR   UCSC; uc008pex.1; mouse. [Q6NVD0-3]
DR   UCSC; uc008pey.1; mouse. [Q6NVD0-1]
DR   AGR; MGI:2444465; -.
DR   CTD; 341640; -.
DR   MGI; MGI:2444465; Frem2.
DR   VEuPathDB; HostDB:ENSMUSG00000037016; -.
DR   eggNOG; KOG1306; Eukaryota.
DR   eggNOG; KOG2090; Eukaryota.
DR   eggNOG; KOG3597; Eukaryota.
DR   GeneTree; ENSGT00940000155313; -.
DR   HOGENOM; CLU_000394_0_0_1; -.
DR   InParanoid; Q6NVD0; -.
DR   OMA; ILPWELN; -.
DR   OrthoDB; 5470912at2759; -.
DR   PhylomeDB; Q6NVD0; -.
DR   TreeFam; TF316876; -.
DR   BioGRID-ORCS; 242022; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Frem2; mouse.
DR   PRO; PR:Q6NVD0; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q6NVD0; Protein.
DR   Bgee; ENSMUSG00000037016; Expressed in molar tooth and 154 other cell types or tissues.
DR   GO; GO:0005604; C:basement membrane; IDA:BHF-UCL.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; ISO:MGI.
DR   GO; GO:0007154; P:cell communication; IEA:InterPro.
DR   GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR   GO; GO:0001654; P:eye development; IMP:UniProtKB.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0048839; P:inner ear development; IDA:MGI.
DR   GO; GO:0001822; P:kidney development; IMP:MGI.
DR   GO; GO:0002009; P:morphogenesis of an epithelium; IMP:MGI.
DR   Gene3D; 2.60.40.2030; -; 5.
DR   InterPro; IPR038081; CalX-like_sf.
DR   InterPro; IPR003644; Calx_beta.
DR   InterPro; IPR039005; CSPG_rpt.
DR   InterPro; IPR045658; FRAS1-rel_N.
DR   PANTHER; PTHR45739:SF4; FRAS1-RELATED EXTRACELLULAR MATRIX PROTEIN 2; 1.
DR   PANTHER; PTHR45739; MATRIX PROTEIN, PUTATIVE-RELATED; 1.
DR   Pfam; PF16184; Cadherin_3; 12.
DR   Pfam; PF03160; Calx-beta; 5.
DR   Pfam; PF19309; Frem_N; 1.
DR   SMART; SM00237; Calx_beta; 5.
DR   SUPFAM; SSF141072; CalX-like; 5.
DR   PROSITE; PS51854; CSPG; 12.
DR   Genevisible; Q6NVD0; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW   Developmental protein; Glycoprotein; Membrane; Metal-binding;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..3160
FT                   /note="FRAS1-related extracellular matrix protein 2"
FT                   /id="PRO_0000010125"
FT   TOPO_DOM        40..3105
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        3106..3126
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        3127..3160
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          312..406
FT                   /note="CSPG 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          431..530
FT                   /note="CSPG 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          553..664
FT                   /note="CSPG 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          689..796
FT                   /note="CSPG 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          817..908
FT                   /note="CSPG 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          934..1026
FT                   /note="CSPG 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          1055..1157
FT                   /note="CSPG 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          1178..1271
FT                   /note="CSPG 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          1292..1388
FT                   /note="CSPG 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          1409..1501
FT                   /note="CSPG 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          1521..1610
FT                   /note="CSPG 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   REPEAT          1644..1741
FT                   /note="CSPG 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT   DOMAIN          1748..1847
FT                   /note="Calx-beta 1"
FT   DOMAIN          1860..1971
FT                   /note="Calx-beta 2"
FT   DOMAIN          1986..2092
FT                   /note="Calx-beta 3"
FT   DOMAIN          2107..2209
FT                   /note="Calx-beta 4"
FT   DOMAIN          2227..2331
FT                   /note="Calx-beta 5"
FT   REGION          3130..3160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3136..3160
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        351
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1233
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1358
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1573
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1730
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..2851
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_015037"
FT   VAR_SEQ         1..2287
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_015038"
FT   VAR_SEQ         2288..2297
FT                   /note="SGEDYHPVSE -> MVGPGNFRKR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_015039"
FT   CONFLICT        2437
FT                   /note="S -> N (in Ref. 2; BAC27425)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2851
FT                   /note="H -> N (in Ref. 2; BAC27425)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3031
FT                   /note="P -> H (in Ref. 3; AAH46388)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3040
FT                   /note="S -> G (in Ref. 3; AAH46388)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   3160 AA;  350640 MW;  579F20BD79957E06 CRC64;
     MASRARRTAK FSSFQPILAQ SPRLLLLLLL LSLVSYVSTQ AAGPGAALQS LGLSGTSGVP
     TEEAIVVANR GLRVPFGREV WLDPLRDLVL QVQPGDRCTV TVLDNDALAQ RPGHLSPKRF
     ACDYGPGEVR YSHLGARSPS RDRVRLQLRY DAPGGAIVLP LALEVEVVFT QLEIVTRNLP
     LVVEELLGTS NALDDRSLEF AYQPETEECR VGILSGLSAL PRYGELLHYP QVQGGAGDRG
     TSKTLLMDCK AFQELGVRYR HTAPSRSPNR DWLPMVVELH SRGAPEGSPA LKREHFQVLV
     RIRGGAENTA PKPSFVAMMM MEVDQFVLTA LTPDMLAAED AESDPDLLIF NLTSAFQPGQ
     GYLVSTDDRS LPLSSFTQRD LRLLKIAYQP PSEDSDQERL FELELEIVDP EGAASDPFAF
     MVVVKPMNTL APVVTRNTGL ILYEGQYRPL TGPIGSGPQN LVISDEDDLE AVRLEVVAGL
     RHGHLVILGS PSSDSAPKTF TVAELAAGQV VYQHDDKDGS LSDNLVLRMS DGGGRHQVQF
     LFPITLVPVD DQPPVLNANT GLTVAEGETV PIPPLTLSAT DIDSDDSQLV FVLLPPFSSL
     GHLLLRQRHV PQEEQGLWQK QGSFYERTVT EWRQQDITEG KLFYRHSGPH SPGPVMDQFM
     FRVQDNHDPP NQSGIQRFVI RIHPVDRLPP ELGSGCPLRM VVQESQLTPL RKRWLHYTDL
     DTDDRELQYT VTQPPTDTDE NHSPAPLGTL VFTDNPSVVV SHFTQAQVNH HKIAYRPPGQ
     ELGVAARVAQ FQFQVEDRAG NVAPGTFTLY LQPVDNQPPE IVNTGFTVEE KGHHILRETE
     LHVSDVDTDV THISFTLTQA PKHGHMQISG RPLHVGGQFH LEDIKHGRIS YWNSGDESLT
     DSCSLEVSDR HHVVPITLRV NVRPGDREGP MSVLPAGTLE SYLDVLENGA TEVTANIIKG
     AYQGTDDLML TFLLEGPPSY GEILVNGAPA EQFTQRDILE GSVVYAHTSG EIGLLPKADS
     FNLSLSAMSQ EWRIGSSIVQ GVTVWVTILP VDSQAPEISL GEQFVVLEGD KSVISLTHLS
     AEDMDSLKDD LLCTIVIQPT SGYVENISPA PGSEKSRAGV AISAFTLKDL RQGHINYVQS
     VHRGVEPVED RFIFRCSDGI NFSERQIFPI VIIPTNDEQP EMFMREFMVM EGMSLVVNRL
     ILNAADADIP RDDLTFTITR FPTHGHVMNQ LINGTVLVES FTLDQIIESS SIIYEHDDSE
     TQEDSFVIKL TDGKHSVEKM VLIVVIPVDD ETPRMTINNG LEIEIGETKV INNKVLMATD
     LDSDDKSLVY IIRYGPGHGL LQRQKPLGAF ENITLGMNFT QDEVDRNLIQ YVHFGQEGIR
     DLIKFDVTDG TNALIDRYFY VTIGSVDIVF PDVVSKGVSL KEGGKVTLTT DLLSTSDLNS
     PDENLVFTIT RAPMRGHLEC TDRRGLSITS FTQLQLAGNK IYYIHTAEDE VKMDSFEFQV
     TDGRNPVFRT FRISISDVDN KKPVVTIHNL VVSESESKLI TPFELTVEDR DTPDRLLKFI
     VTQVPVHGHL LFNNTRSVMV FTKQDLNENL ISYKHDGTES TEDSFSFTVT DGTHSDFYVF
     PDTVFETRRP QVMKIQVLPV DNSVPQIVVN KGASTLRTLA TGHLGFMITS KILKVEDRDS
     LHFSLRFIVT EAPQHGYLLN LGQGNHSVTQ FTQADIDDMK ICYVLRERAN ATSDMFHFIV
     EDDGGNRLTN QHFRLNWAWI SFEKEYYLIN EDSKFLDIVL TRRGYLGETS FISIGTRDGT
     AEKDRDFKGK AQKQVQFNPG QTRASWRVRI LSDGEHEHSE TFQVVLSEPV LAILEFPTVT
     TVEIIDPGDE STVFIPQSEY SVEEDVGELF IPIRRSGDIS RELMVICYTQ QGTATSTVRT
     SVLSYSDYIS RPEDHSSVIR FDKDEREKMC RILVIDDSLY EEEETFQVLL SMPMGGRIGD
     KFPGANVTIL TDRDDEPAFY FGDTQYSVDE SAGYVELQVW RTGTDLSKPS SVTVRSRKTE
     SLSADAGTDY VGISRNLDFA PGVNMQTVRV VILDDLGRPI LEGIEKFELV LRMPMNAALG
     EPSKATVSIN DSASDLPKMQ FKERVYTCNE NDGRVVAMIY RSGDIQHRSS VRCYTRQGSA
     QVMMDFEERP NTDVSTVTFL PGEMEKPCVL ELMDDAVYED VEELRLVLGT PQGSSAFGAA
     VGEQNETLIK IQDEADKAVI KFGETKFSVT EPSRPGESVV VKIPVIRQGD TSKVSIVRVH
     TKDGSATSGE DYHPVSEEIE FKEGETQHTV EIEVIFDGVR EMREAFTVHL KPDENMVAET
     QATKAIVYIE EIHSMADVTF PSVPHIVSLL IYDDPSKGRE DTGPVSGYPV VCITACNPKY
     PDYEKTGSIC ASENINDTLT RYRWLISAPA GPDGVTSPMR EVDFDTFFTS SKMITLDSIY
     FQPGSRVQCA ARAVNTNGNE GLELMSPIVT IGREEGLCQP RVPGVVGAEP FSAKLRYTGP
     EDPDFANLIK LTVTMPHIDG MLPAISTREL SNFELTLSPD GTRVGNHKCS NLLDYNEVKT
     HHGFLTNATK NPEVIGETYP YQYSVPVRGS STLRFYRNLN LEACLWEFVS YYDMTELLAD
     CGGTIGTDGQ VLNLVQSYVT LRVPLYVSYV FHSPVGVGGW QHFDLKSELR LTFVYDTAIL
     WNHGIGSPPE AELQGSLYPT SMRIGEEGRL AVNFKTEAQF HGLFVLSHPA SFTSSLIVSA
     DHPGLTFSLR LIRSEPTYNQ PVQQWSFVSD FAVRDYSGTY TVKLVPCTTP SNQEYRLPVT
     CNPREPVTFD LDIRFQQVSD PVATEFSLNT HMYLLSKKNL WLSDGSMGFG QESDVAFAEG
     DVIYGRVMVD PVQNLGDSFY CSIEKVFLCT GDDGYVPKYS PANAEYGCLA DSPSLLHRFK
     IVDKAQPETQ ATSFGDVLFN AKLAVDDPEA VLLVNQPGSD GFKVDSTPLF QVALGREWYI
     HTIYTVKSKD NTHRGIGKRS LEYQYHSVVH PGPPQATTKS WKKRAVRSTP SLAGEIGAEN
     NRGTNIQHIS LNRRGKRQVP HGRIPPDGIL PWELNSPSSE VSLVTVLGGL TVGLLTVCLA
     VAAAVMCRNR STKGKDTPKG SGSTEPMMSP QSHYNDSSEV
//