GenomeNet

Database: UniProt
Entry: A0A140T902_HUMAN
LinkDB: A0A140T902_HUMAN
Original site: A0A140T902_HUMAN 
ID   A0A140T902_HUMAN        Unreviewed;      4222 AA.
AC   A0A140T902;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=Tenascin-X {ECO:0000313|Ensembl:ENSP00000387561.1};
GN   Name=TNXB {ECO:0000313|Ensembl:ENSP00000387561.1};
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 {ECO:0000313|Ensembl:ENSP00000387561.1, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000387561.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [2] {ECO:0007829|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [3] {ECO:0000313|Ensembl:ENSP00000387561.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (AUG-2022) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000256|ARBA:ARBA00004498}.
CC   -!- SIMILARITY: Belongs to the tenascin family.
CC       {ECO:0000256|ARBA:ARBA00008673}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; CR753803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR753845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   SMR; A0A140T902; -.
DR   MassIVE; A0A140T902; -.
DR   PeptideAtlas; A0A140T902; -.
DR   Ensembl; ENST00000440248.5; ENSP00000387561.1; ENSG00000231608.9.
DR   HGNC; HGNC:11976; TNXB.
DR   PhylomeDB; A0A140T902; -.
DR   ChiTaRS; TNXB; human.
DR   Proteomes; UP000005640; Unplaced.
DR   CDD; cd00054; EGF_CA; 4.
DR   CDD; cd00063; FN3; 31.
DR   CDD; cd00087; FReD; 1.
DR   Gene3D; 3.90.215.10; Gamma Fibrinogen, chain A, domain 1; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 31.
DR   Gene3D; 2.10.25.10; Laminin; 17.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR041161; EGF_Tenascin.
DR   InterPro; IPR036056; Fibrinogen-like_C.
DR   InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR   InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR   InterPro; IPR020837; Fibrinogen_CS.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR46708; TENASCIN; 1.
DR   PANTHER; PTHR46708:SF3; TENASCIN-X; 1.
DR   Pfam; PF07974; EGF_2; 2.
DR   Pfam; PF18720; EGF_Tenascin; 10.
DR   Pfam; PF00147; Fibrinogen_C; 1.
DR   Pfam; PF00041; fn3; 31.
DR   SMART; SM00181; EGF; 18.
DR   SMART; SM00186; FBG; 1.
DR   SMART; SM00060; FN3; 32.
DR   SUPFAM; SSF56496; Fibrinogen C-terminal domain-like; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 29.
DR   PROSITE; PS00022; EGF_1; 6.
DR   PROSITE; PS01186; EGF_2; 6.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS00514; FIBRINOGEN_C_1; 1.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
DR   PROSITE; PS50853; FN3; 31.
PE   1: Evidence at protein level;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Proteomics identification {ECO:0007829|MaxQB:A0A140T902,
KW   ECO:0007829|PeptideAtlas:A0A140T902};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..4222
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007305400"
FT   DOMAIN          617..648
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          751..841
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          842..932
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1064..1153
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1161..1249
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1263..1352
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1374..1468
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1476..1566
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1574..1669
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1674..1764
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1778..1868
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1883..1971
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          1989..2082
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2097..2185
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2196..2286
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2305..2398
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2408..2502
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2519..2617
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2625..2723
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2733..2830
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2835..2928
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          2938..3035
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          3040..3131
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          3146..3238
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          3242..3333
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          3335..3424
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          3429..3522
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          3531..3625
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          3635..3732
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          3736..3825
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          3826..3912
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          3913..4003
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          3999..4214
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51406"
FT   REGION          27..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          169..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          926..956
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1340..1372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1752..1777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1968..1990
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2281..2304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2495..2542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2922..2958
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3514..3537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3614..3640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        940..956
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3621..3640
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        621..631
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        638..647
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   4222 AA;  456160 MW;  CE5277F33A46F355 CRC64;
     MMPAQYALTS SLVLLVLLST ARAGPFSSRS NVTLPAPRPP PQPGGHTVGA GVGSPSSQLY
     EHTVEGGEKQ VVFTHRINLP PSTGCGCPPG TEPPVLASEV QALRVRLEIL EELVKGLKEQ
     CTGGCCPASA QAGTGQTDVR TLCSLHGVFD LSRCTCSCEP GWGGPTCSDP TDAEIPPSSP
     PSASGSCPDD CNDQGRCVRG RCVCFPGYTG PSCGWPSCPG DCQGRGRCVQ GVCVCRAGFS
     GPDCSQRSCP RGCSQRGRCE GGRCVCDPGY TGDDCGMRSC PRGCSQRGRC ENGRCVCNPG
     YTGEDCGVRS CPRGCSQRGR CKDGRCVCDP GYTGEDCGTR SCPWDCGEGG RCVDGRCVCW
     PGYTGEDCST RTCPRDCRGR GRCEDGECIC DTGYSGDDCG VRSCPGDCNQ RGRCEDGRCV
     CWPGYTGTDC GSRACPRDCR GRGRCENGVC VCNAGYSGED CGVRSCPGDC RGRGRCESGR
     CMCWPGYTGR DCGTRACPGD CRGRGRCVDG RCVCNPGFTG EDCGSRRCPG DCRGHGLCED
     GVCVCDAGYS GEDCSTRSCP GGCRGRGQCL DGRCVCEDGY SGEDCGVRQC PNDCSQHGVC
     QDGVCICWEG YVSEDCSIRT CPSNCHGRGR CEEGRCLCDP GYTGPTCATR MCPADCRGRG
     RCVQGVCLCH VGYGGEDCGQ EEPPASACPG GCGPRELCRA GQCVCVEGFR GPDCAIQTCP
     GDCRGRGECH DGSCVCKDGY AGEDCGEEVP TIEGMRMHLL EETTVRTEWT PAPGPVDAYE
     IQFIPTTEGA SPPFTARVPS SASAYDQRGL APGQEYQVTV RALRGTSWGL PASKTITTMI
     DGPQDLRVVA VTPTTLELGW LRPQAEVDRF VVSYVSAGNQ RVRLEVPPEA DGTLLTDLMP
     GVEYVVTVTA ERGRAVSYPA SVRANTGSSP LGLLGTTDEP PPSGPSTTQG AQAPLLQQRP
     QELGELRVLG RDETGRLRVV WTAQPDTFAY FQLRMRVPEG PGAHEEVLPG DVRQALVPPP
     PPGTPYELSL HGVPPGGKPS DPIIYQGIMD KDEEKPGKSS GPPRLGELTV TDRTSDSLLL
     RWTVPEGEFD SFVIQYKDRD GQPQVVPVEG PQRSAVITSL DPGRKYKFVL YGFVGKKRHG
     PLVAEAKILP QSDPSPGTPP RLGNLWVTDP TPDSLHLSWT VPEGQFDTFM VQYRDRDGRP
     QVVPVEGPER SFVVSSLDPD HKYRFTLFGI ANKKRYGPLT ADGTTAPERK EEPPHPEFLE
     QPLLGELTVT GVTPDSLRLS WTVAQGPFDS FMVQYKDAQG QPQAVPVAGD ENEVTVPGLD
     PDRKYKMNLY GLRGRQRVGP ESVVAKTAPQ EDVDETPSPT ELGTEAPESP EEPLLGELTV
     TGSSPDSLSL FWTVPQGSFD SFTVQYKDRD GRPRAVRVGG KESEVTVGGL EPGHKYKMHL
     YGLHEGQRVG PVSAVGVTAP QQEETPPATE SPLEPRLGEL TVTDVTPNSV GLSWTVPEGQ
     FDSFIVQYKD KDGQPQVVPV AADQREVTVY NLEPERKYKM NMYGLHDGQR MGPLSVVIVT
     APLPPAPATE ASKPPLEPRL GELTVTDITP DSVGLSWTVP EGEFDSFVVQ YKDRDGQPQV
     VPVAADQREV TIPDLEPSRK YKFLLFGIQD GKRRSPVSVE AKTVARGDAS PGAPPRLGEL
     WVTDPTPDSL RLSWTVPEGQ FDSFVVQFKD KDGPQVVPVE GHERSVTVTP LDAGRKYRFL
     LYGLLGKKRH GPLTADGTTE ARSAMDDTGT KRPPKPRLGE ELQVTTVTQN SVGLSWTVPE
     GQFDSFVVQY KDRDGQPQVV PVEGSLREVS VPGLDPAHRY KLLLYGLHHG KRVGPISAVA
     ITAGREETET ETTAPTPPAP EPHLGELTVE EATSHTLHLS WMVTEGEFDS FEIQYTDRDG
     QLQMVRIGGD RNDITLSGLE SDHRYLVTLY GFSDGKHVGP VHVEALTVPE EEKPSEPPTA
     TPEPPIKPRL GELTVTDATP DSLSLSWTVP EGQFDHFLVQ YRNGDGQPKA VRVPGHEEGV
     TISGLEPDHK YKMNLYGFHG GQRMGPVSVV GVTAAEEETP SPTEPSMEAP EPAEEPLLGE
     LTVTGSSPDS LSLSWTVPQG RFDSFTVQYK DRDGRPQVVR VGGEESEVTV GGLEPGRKYK
     MHLYGLHEGR RVGPVSAVGV TAPEEESPDA PLAKLRLGQM TVRDITSDSL SLSWTVPEGQ
     FDHFLVQFKN GDGQPKAVRV PGHEDGVTIS GLEPDHKYKM NLYGFHGGQR VGPVSAVGLT
     APGKDEEMAP ASTEPPTPEP PIKPRLEELT VTDATPDSLS LSWTVPEGQF DHFLVQYKNG
     DGQPKATRVP GHEDRVTISG LEPDNKYKMN LYGFHGGQRV GPVSAIGVTA AEEETPSPTE
     PSMEAPEPPE EPLLGELTVT GSSPDSLSLS WTVPQGRFDS FTVQYKDRDG RPQVVRVGGE
     ESEVTVGGLE PGRKYKMHLY GLHEGRRVGP VSTVGVTAPQ EDVDETPSPT EPGTEAPEPP
     EEPLLGELTV TGSSPDSLSL SWTVPQGRFD SFTVQYKDRD GRPQAVRVGG QESKVTVRGL
     EPGRKYKMHL YGLHEGRRLG PVSAVGVTED EAETTQAVPT MTPEPPIKPR LGELTMTDAT
     PDSLSLSWTV PEGQFDHFLV QYRNGDGQPK AVRVPGHEDG VTISGLEPDH KYKMNLYGFH
     GGQRVGPISV IGVTAAEEET PSPTELSTEA PEPPEEPLLG ELTVTGSSPD SLSLSWTIPQ
     GHFDSFTVQY KDRDGRPQVM RVRGEESEVT VGGLEPGRKY KMHLYGLHEG RRVGPVSTVG
     VTVPTTTPEP PNKPRLGELT VTDATPDSLS LSWMVPEGQF DHFLVQYRNG DGQPKVVRVP
     GHEDGVTISG LEPDHKYKMN LYGFHGGQRV GPISVIGVTA AEEETPAPTE PSTEAPEPPE
     EPLLGELTVT GSSPDSLSLS WTIPQGRFDS FTVQYKDRDG RPQVVRVRGE ESEVTVGGLE
     PGCKYKMHLY GLHEGQRVGP VSAVGVTVPT MTPEPPIKPR LGELTVTDAT PDSLSLSWMV
     PEGQFDHFLV QYRNGDGQPK AVRVPGHEDG VTISGLEPDH KYKMNLYGFH GGQRVGPVSA
     IGVTEEETPS PTEPSTEAPE APEEPLLGEL TVTGSSPDSL SLSWTIPQGR FDSFTVQYKD
     RDGQPQVVRV RGEESEVTVG GLEPGRKYKM HLYGLHEGQR VGPVSTVGIT APLPTPLPVE
     PRLGELAVAA VTSDSVGLSW TVAQGPFDSF LVQYRDAQGQ PQAVPVSGDL RAVAVSGLDP
     ARKYKFLLFG LQNGKRHGPV PVEARTAPDT KPSPRLGELT VTDATPDSVG LSWTVPEGEF
     DSFVVQYKDK DGRLQVVPVA ANQREVTVQG LEPSRKYRFL LYGLSGRKRL GPISADSTTA
     PLEKELPPHL GELTVAEETS SSLRLSWTVA QGPFDSFVVQ YRDTDGQPRA VPVAADQRTV
     TVEDLEPGKK YKFLLYGLLG GKRLGPVSAL GMTAPEEDTP APELAPEAPE PPEEPRLGVL
     TVTDTTPDSM RLSWSVAQGP FDSFVVQYED TNGQPQALLV DGDQSKILIS GLEPSTPYRF
     LLYGLHEGKR LGPLSAEGTT GLAPAGQTSE ESRPRLSQLS VTDVTTSSLR LNWEAPPGAF
     DSFLLRFGVP SPSTLEPHPR PLLQRELMVP GTRHSAVLRD LRSGTLYSLT LYGLRGPHKA
     DSIQGTARTL SPVLESPRDL QFSEIRETSA KVNWMPPPSR ADSFKVSYQL ADGGEPQSVQ
     VDGQARTQKL QGLIPGARYE VTVVSVRGFE ESEPLTGFLT TVPDGPTQLR ALNLTEGFAV
     LHWKPPQNPV DTYDIQVTAP GAPPLQAETP GSAVDYPLHD LVLHTNYTAT VRGLRGPNLT
     SPASITFTTG LEAPRDLEAK EVTPRTALLT WTEPPVRPAG YLLSFHTPGG QTQEILLPGG
     ITSHQLLGLF PSTSYNARLQ ATWGQSLLPP VSTSFTTGGL RIPFPRDCGE EMQNGAGASR
     TSTIFLNGNR ERPLNVFCDM ETDGGGWLVF QRRMDGQTDF WRDWEDYAHG FGNISGEFWL
     GNEALHSLTQ AGDYSMRVDL RAGDEAVFAQ YDSFHVDSAA EYYRLHLEGY HGTAGDSMSY
     HSGSVFSARD RDPNSLLISC AVSYRGAWWY RNCHYANLNG LYGSTVDHQG VSWYHWKGFE
     FSVPFTEMKL RPRNFRSPAG GG
//
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