COCA1_MOUSE
ID COCA1_MOUSE Reviewed; 3120 AA.
AC Q60847; P70322;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Collagen alpha-1(XII) chain;
DE Flags: Precursor;
GN Name=Col12a1;
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 5), AND ALTERNATIVE SPLICING (ISOFORMS
RP 1 AND 3).
RC STRAIN=C57BL/6J, and Swiss Webster; TISSUE=Skin;
RX PubMed=8601036; DOI=10.1002/aja.1002040409;
RA Boehme K., Li Y., Oh P.S., Olsen B.R.;
RT "Primary structure of the long and short splice variants of mouse collagen
RT XII and their tissue-specific expression during embryonic development.";
RL Dev. Dyn. 204:432-445(1995).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3047-3120, AND ALTERNATIVE SPLICING (ISOFORMS
RP 2 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Skin fibroblast;
RX PubMed=10419532; DOI=10.1074/jbc.274.31.22053;
RA Kania A.M., Reichenberger E., Baur S.T., Karimbux N.Y., Taylor R.W.,
RA Olsen B.R., Nishimura I.;
RT "Structural variation of type XII collagen at its carboxyl-terminal NC1
RT domain generated by tissue-specific alternative splicing.";
RL J. Biol. Chem. 274:22053-22059(1999).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=21670218; DOI=10.1083/jcb.201010010;
RA Izu Y., Sun M., Zwolanek D., Veit G., Williams V., Cha B., Jepsen K.J.,
RA Koch M., Birk D.E.;
RT "Type XII collagen regulates osteoblast polarity and communication during
RT bone formation.";
RL J. Cell Biol. 193:1115-1130(2011).
CC -!- FUNCTION: Type XII collagen interacts with type I collagen-containing
CC fibrils, the COL1 domain could be associated with the surface of the
CC fibrils, and the COL2 and NC3 domains may be localized in the
CC perifibrillar matrix. {ECO:0000250}.
CC -!- SUBUNIT: Trimer of identical chains each containing 190 kDa of non-
CC triple-helical sequences. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=The final tissue form of collagen XII may contain homotrimers
CC or any combination of the various isoforms.;
CC Name=1; Synonyms=XIIA-1;
CC IsoId=Q60847-1; Sequence=Displayed;
CC Name=2; Synonyms=ER#K, XIIA-2;
CC IsoId=Q60847-2; Sequence=VSP_001151, VSP_001152;
CC Name=3; Synonyms=XIIB-1;
CC IsoId=Q60847-3; Sequence=VSP_001150;
CC Name=4; Synonyms=XIIB-2;
CC IsoId=Q60847-4; Sequence=VSP_001150, VSP_001151, VSP_001152;
CC Name=5;
CC IsoId=Q60847-5; Sequence=VSP_023404, VSP_023405;
CC -!- TISSUE SPECIFICITY: Highest expression in tendons, perichondrium, skin,
CC cornea, sclera, blood vessels, and periosteum.
CC -!- DEVELOPMENTAL STAGE: The long NC3 XIIA isoforms are predominant at
CC early stages (ED7 and 11); at later stages of development (ED15 and 17)
CC the short NC3 XIIB forms become the major forms. As the short NC3 forms
CC become the major product, the long splice variant continues to be
CC expressed in several tissues, even after birth. The long NC1 isoforms,
CC XIIA-1 and XIIB-1, peak in 15-day old embryos and decrease in 17-day
CC old ones. The expression of the short NC1 form XIIB-2 remains constant
CC throughout late stages of embryonic development (ED15 and ED17).
CC -!- PTM: The triple-helical tail is stabilized by disulfide bonds at each
CC end. {ECO:0000250}.
CC -!- PTM: Hydroxylation on proline residues within the sequence motif, GXPG,
CC is most likely to be 4-hydroxy as this fits the requirement for 4-
CC hydroxylation in vertebrates. {ECO:0000250}.
CC -!- PTM: O-glycosylation of isoform 2; glycosaminoglycan of chondroitin-
CC sulfate type. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Animals have fragile bones with a disorganized
CC collagen fiber arrangement, decreased expression of bone matrix
CC proteins, and decreased bone-forming activity associated with delayed
CC terminal differentiation. They have also decreased grip strength, a
CC delay in fiber-type transition, and a deficiency in passive force
CC generation, while the muscle seemed more resistant to eccentric
CC contraction-induced force drop, indicating a role for a matrix-based
CC passive force-transducing elastic element in the generation of the
CC weakness. {ECO:0000269|PubMed:21670218}.
CC -!- SIMILARITY: Belongs to the fibril-associated collagens with interrupted
CC helices (FACIT) family. {ECO:0000305}.
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DR EMBL; U25652; AAA99719.1; -; mRNA.
DR EMBL; AC157477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC166055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U57095; AAB07047.1; -; mRNA.
DR CCDS; CCDS72284.1; -. [Q60847-2]
DR PIR; C44479; C44479.
DR PIR; D44479; D44479.
DR RefSeq; NP_001277237.1; NM_001290308.1. [Q60847-2]
DR SMR; Q60847; -.
DR BioGRID; 198807; 3.
DR ComplexPortal; CPX-2978; Collagen type XII trimer.
DR STRING; 10090.ENSMUSP00000071662; -.
DR GlyGen; Q60847; 8 sites.
DR iPTMnet; Q60847; -.
DR PhosphoSitePlus; Q60847; -.
DR CPTAC; non-CPTAC-3417; -.
DR EPD; Q60847; -.
DR jPOST; Q60847; -.
DR MaxQB; Q60847; -.
DR PaxDb; Q60847; -.
DR PeptideAtlas; Q60847; -.
DR PRIDE; Q60847; -.
DR ProteomicsDB; 283780; -. [Q60847-1]
DR ProteomicsDB; 283781; -. [Q60847-2]
DR ProteomicsDB; 283782; -. [Q60847-3]
DR ProteomicsDB; 283783; -. [Q60847-4]
DR ProteomicsDB; 283784; -. [Q60847-5]
DR Antibodypedia; 2124; 101 antibodies from 20 providers.
DR DNASU; 12816; -.
DR Ensembl; ENSMUST00000071750; ENSMUSP00000071662; ENSMUSG00000032332. [Q60847-2]
DR GeneID; 12816; -.
DR KEGG; mmu:12816; -.
DR UCSC; uc009qus.2; mouse. [Q60847-2]
DR CTD; 1303; -.
DR MGI; MGI:88448; Col12a1.
DR VEuPathDB; HostDB:ENSMUSG00000032332; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000154923; -.
DR HOGENOM; CLU_000467_0_0_1; -.
DR InParanoid; Q60847; -.
DR OMA; KAEIQKC; -.
DR OrthoDB; 67372at2759; -.
DR PhylomeDB; Q60847; -.
DR TreeFam; TF329914; -.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 12816; 0 hits in 68 CRISPR screens.
DR ChiTaRS; Col12a1; mouse.
DR PRO; PR:Q60847; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q60847; protein.
DR Bgee; ENSMUSG00000032332; Expressed in diaphysis of femur and 182 other tissues.
DR ExpressionAtlas; Q60847; baseline and differential.
DR Genevisible; Q60847; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0035987; P:endodermal cell differentiation; IBA:GO_Central.
DR CDD; cd00063; FN3; 18.
DR Gene3D; 2.60.40.10; -; 18.
DR Gene3D; 3.40.50.410; -; 4.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF00041; fn3; 18.
DR Pfam; PF00092; VWA; 4.
DR SMART; SM00060; FN3; 18.
DR SMART; SM00210; TSPN; 1.
DR SMART; SM00327; VWA; 4.
DR SUPFAM; SSF49265; SSF49265; 10.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF53300; SSF53300; 4.
DR PROSITE; PS50853; FN3; 18.
DR PROSITE; PS50234; VWFA; 4.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell adhesion; Collagen; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydroxylation; Proteoglycan;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..3120
FT /note="Collagen alpha-1(XII) chain"
FT /id="PRO_0000005784"
FT DOMAIN 27..117
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 140..316
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 336..426
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 440..616
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 634..723
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 725..816
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 817..905
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 907..998
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1000..1087
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1089..1179
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1199..1371
FT /note="VWFA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1387..1475
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1476..1567
FT /note="Fibronectin type-III 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1568..1658
FT /note="Fibronectin type-III 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1659..1754
FT /note="Fibronectin type-III 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1757..1851
FT /note="Fibronectin type-III 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1852..1937
FT /note="Fibronectin type-III 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1938..2028
FT /note="Fibronectin type-III 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2029..2119
FT /note="Fibronectin type-III 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2120..2208
FT /note="Fibronectin type-III 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2209..2296
FT /note="Fibronectin type-III 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 2325..2498
FT /note="VWFA 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 2522..2714
FT /note="Laminin G-like"
FT DOMAIN 2749..2800
FT /note="Collagen-like 1"
FT DOMAIN 2804..2854
FT /note="Collagen-like 2"
FT DOMAIN 2855..2899
FT /note="Collagen-like 3"
FT DOMAIN 2943..2992
FT /note="Collagen-like 4"
FT REGION 1074..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2293..2313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2453..2748
FT /note="Nonhelical region (NC3)"
FT REGION 2749..2900
FT /note="Triple-helical region (COL2) with 1 imperfection"
FT REGION 2752..2898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2901..2943
FT /note="Nonhelical region (NC2)"
FT REGION 2933..3072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2944..3046
FT /note="Triple-helical region (COL1) with 2 imperfections"
FT REGION 3047..3120
FT /note="Nonhelical region (NC1)"
FT REGION 3094..3120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 862..864
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 2781..2783
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 2897..2899
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 1076..1099
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2299..2313
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2780..2799
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2826..2840
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2942..2956
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3020..3038
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3098..3114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2946
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 2949
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 2952
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 2961
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 2967
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 2970
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 2973
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 2985
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 3002
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 3005
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 3016
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 3025
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 3028
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 3031
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT CARBOHYD 700
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 798
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 889
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 981
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1765
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 25..1186
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_001150"
FT VAR_SEQ 3063..3068
FT /note="EPYVPE -> GMLLPS (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:8601036"
FT /id="VSP_023404"
FT VAR_SEQ 3063..3065
FT /note="EPY -> GSG (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_001151"
FT VAR_SEQ 3066..3120
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_001152"
FT VAR_SEQ 3069..3120
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:8601036"
FT /id="VSP_023405"
FT CONFLICT 245
FT /note="A -> G (in Ref. 1; AAA99719)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="K -> KTQPK (in Ref. 1; AAA99719)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="I -> T (in Ref. 1; AAA99719)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="K -> E (in Ref. 1; AAA99719)"
FT /evidence="ECO:0000305"
FT CONFLICT 611
FT /note="E -> V (in Ref. 1; AAB07047/AAA99719)"
FT /evidence="ECO:0000305"
FT CONFLICT 690
FT /note="N -> S (in Ref. 1; AAA99719)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="S -> P (in Ref. 1; AAA99719)"
FT /evidence="ECO:0000305"
FT CONFLICT 954
FT /note="P -> N (in Ref. 1; AAA99719)"
FT /evidence="ECO:0000305"
FT CONFLICT 1079
FT /note="G -> R (in Ref. 1; AAA99719)"
FT /evidence="ECO:0000305"
FT CONFLICT 1271
FT /note="Y -> N (in Ref. 1; AAA99719)"
FT /evidence="ECO:0000305"
FT CONFLICT 1472
FT /note="T -> A (in Ref. 1; AAA99719)"
FT /evidence="ECO:0000305"
FT CONFLICT 1524
FT /note="G -> E (in Ref. 1; AAA99719)"
FT /evidence="ECO:0000305"
FT CONFLICT 1773
FT /note="V -> I (in Ref. 1; AAA99719)"
FT /evidence="ECO:0000305"
FT CONFLICT 1831
FT /note="D -> G (in Ref. 1; AAA99719)"
FT /evidence="ECO:0000305"
FT CONFLICT 1939
FT /note="A -> S (in Ref. 1; AAA99719)"
FT /evidence="ECO:0000305"
FT CONFLICT 2005
FT /note="N -> Y (in Ref. 1; AAA99719)"
FT /evidence="ECO:0000305"
FT CONFLICT 2428..2429
FT /note="PK -> R (in Ref. 1; AAA99719)"
FT /evidence="ECO:0000305"
FT CONFLICT 2432
FT /note="V -> G (in Ref. 1; AAA99719)"
FT /evidence="ECO:0000305"
FT CONFLICT 2515
FT /note="L -> Q (in Ref. 1; AAA99719)"
FT /evidence="ECO:0000305"
FT CONFLICT 2551..2552
FT /note="SY -> DS (in Ref. 1; AAA99719)"
FT /evidence="ECO:0000305"
FT CONFLICT 2861..2864
FT /note="Missing (in Ref. 1; AAA99719)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3120 AA; 340214 MW; C4D9264E3C5C8CB5 CRC64;
MQTRLPRALA ALGVALLLSS IEAEVDPPSD LNFKIIDENT VHMSWERPVD PIVGYRITVD
PTTDGPTKEF TLAASTTETL LSDLIPETQY VVTITSYNEV EESVPVIGQL TIQTGGPTKP
GEKKPGKTEI QKCSVSAWTD LVFLVDGSWS VGRNNFKYIL DFIVALVSAF DIGEEKTRVG
VVQYSSDTRT EFNLNQYYRR EDLLAAVKKI PYKGGNTMTG DAIDYLVKNT FTESAGSRAG
FPKVAIIITD GKSQDEVEIP ARELRNIGVE VFSLGIKAAD AKELKQIAST PSLNHVFNVA
NFDAIVDIQN EIISQVCSGV DEQLGELVSG EEVIEPPSNL VVTELSSKYI RLSWDPSPSA
VTGYKILLTP MAAGSRHHAL SVGPQTTTLN VRDLTADTEY QISVFAMKGL TSSEPTSVME
KTQPMKVQVE CSRGVDIKAD IVFLVDGSYS IGIANFVKVR AFLEVLAKSF EISPNRVQIS
LVQYSRDPHT EFTLKEFNRV EDIIKAINTF PYRGGSTNTG KAMTYVREKI FVPNKGSRSN
VPKVMILITD GKSSDAFRDP AIKLRNSDVE IFAVGVKDAV RSELEAIASP PAETHVFTVE
DFDAFQRISF ELTQSICLRI EQELAAIKKK AYVPPKDLRF TQVTANSFKA EWSPPGDNVF
SYHVTYKDAN GDDEVTVVEP ASSTSVVLNN LRPETLYLVN VTAEYEDGFS VPITGEETTA
EVKGVPRNLK VTDETTDSFK LTWSQAPGRV LRYRIRYRPV SGGESKEVST PANQRRKTLE
NLTPDTKYEI SVIAEYSSGP GSPLTGNAAT EEVRGNPRDL RVSDATTSTL KLSWSRAPGK
VKQYLVTYTP AAGGETQEVT VRGDTTTTML RKLKEGTQYD LSVTALYASG AGEALSGKGS
TLEERGSPQN LVTKDITDTS IGAYWTSAPG MVRGYRVSWK SLYDDIEAGE TTLPGDAIHT
MIENLQPETK YKISVFATYS SGEGEPVTGD ATTELSQDSK ILRVDEETEH TMRVTWKAAP
GKVVNYRVVY RPQGGGRQMV AKVPPTVTST VLKRLQPQTT YDITVLPMYK TGEGKLRQGS
GTTASRFKSP RNLKTSDPTM SSFRVTWEPA PGEVKGYKVT FHPTGDDRRL GELVLGPYDN
TVVLEELRAG TTYRVNVFGM FDGGESLPLV GQEMTTLSDT TVTPFLSSGM DCLTRAEADI
VLLVDGSWSI GRANFRTVRS FISRIVEVFE IGPKRVQIAL AQYSGDPRTE WQLNAHRDKK
SLLQAVANLP YKGGNTLTGM ALNFIRQQSF KTQAGMRPRA RKIGVLITDG KSQDDVEAPS
KKLKDEGVEL FAIGIKNADE VELKMIATDP DDTHAYNVAD FESLSKIVDD LTINLCNSVK
GPGDLEAPTN LVISERTHRS FRVSWTPPSD SVDRYKVEYY PVSGGKRQEF YVSRLDTSTV
LKDLKPETDY VVNVYSVVED EYSEPLKGTE KTLPVPVVSL NIYDVGPTTM HVQWQPVGGA
TGYTVSYQPT RSPEGTKPKE MRVGPTVNDV QLTGLLPNTE YEVTVQAVLY DLTSEPAKAR
EVTLPLPRPQ DVKLRDVTHS TMNVVWEPVL GKVRKYIVRY KTPDEEFKEV EVDRSRASTI
LKDLSSQTQY TVSVSAVYDE GTSPPATAYD TTRRVPAPTN LQFTEVTPES FRGTWDHGAS
DVSLYRITWA PVGNPDKMET ILNGDENTLV FENLNPNTPY EVSITAIYPD ESESEDLSGT
ERTLRLIPLT TQAPKSGPRN LQVYNATSNS LTVKWDPASG RVQKYRITYQ PSTGEGNEQT
ITVGGRQNSV LLQKLKPDTP YTITVYSQYP DGEGGRMTGR GKTKPLNTVR NLRVYDPSTS
SLSVRWDHAE GNPRQYKLFY APTSGGPEEL VPIPGNTNYA ILRNLQPDTP YTITVVPVYT
EGDGGRTSDT GRTLVRGLAR NIQVYNPTPN SLDVRWDPAP GPVQQYRIVY SPVAGTRPSE
SIVVPGNTRT VHLERLIPDT PYSVNIVALY SDGEGNPSPS QGRTLPRSGP RNIRVFGETT
NSLSVAWDHA DGPVQQYRII YSPTVGDPID EYTTVPGRRN NVILQPLQPD TPYKITVIAI
YEDGDGGHLT GNGRTVGLLP PQNIHIFDEW YTRFRVSWDP SPSPVLGYKI VYKPVGSNEP
MEAFVGEVTS YTLHNLNPST TYDVSVYAQY DSGLSVPLTD QGTTLYLNVT DLKTYQVGWD
TFCVKWSPHR AATSYRLKLS PADGTRGQEI TVRGSETSHC FTGLSPEAEY GVTVFVQTPN
LEGPGVPIKE QTTVKPTEAP TEPPTPSPPP TIPPARDVCK GAKADIVFLT DASWSIGDDN
FNKVVKFIFN TVGAFDEVNP AGIQVSFVQY SDEVKSEFKL NTYNDKALAL GALQNIRYRG
GNTRTGKALT FIKEKVLTWE SGMRKNVPKV LVVVTDGRSQ DEVKKAAFVI QQSGFSVFVV
GVADVDYNEL ANIASKPSER HVFIVDDFES FEKIEDNLIT FVCETATSSC PLIYLDGYTS
PGFKMLEAYN LTEKNFASVQ GVSLESGSFP SYSAYRLQKN AFINQPTAEL HPNGLPPSYT
IILLFRLLPE TPSDPFAIWQ ITDRDYRPQV GVIADPSSKT LSFFNKDTRG EVQTVTFDTD
EVKTLFYGSF HKVHIVVTSK SVKIYIDCYE IIEKDIKEAG NITTDGYEIL GKLLKGERKS
ATFQIQSFDI VCSPVWTSRD RCCDIPSRRD EAKCPALPNA CTCTQDSVGP PGPPGPAGGP
GAKGPRGERG INGAVGPPGP RGDTGPPGPQ GPPGPQGPNG LSIPGEQGRQ GMKGDAGEPG
LPGRTGTPGL PGPPGPMGPP GDRGFTGKDG AMGPRGPPGP PGSPGSPGVT GPSGKPGKPG
DHGRPGQSGL KGEKGDRGDI ASQNMMRAVA RQVCEQLISG QMSRFNQMLN QIPNDYHSSR
NQPGPPGPPG PPGSAGARGE PGPGGRPGFP GTPGMQGPPG ERGLPGEKGE RGTGSQGPRG
PPGPPGPQGE SRTGPPGSTG SRGPPGPPGR PGNSGIRGPP GPPGYCDSSQ CASIPYNGQG
YPEPYVPEGG AYLPEREPFI VPVEPERTAE YEDDYGADEP DQQHPDHMRW RRALRPGPAE
