FA5_MOUSE
ID FA5_MOUSE Reviewed; 2183 AA.
AC O88783; Q3UTQ2; Q3UV80;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Coagulation factor V;
DE AltName: Full=Activated protein C cofactor;
DE Contains:
DE RecName: Full=Coagulation factor V heavy chain;
DE Contains:
DE RecName: Full=Coagulation factor V light chain;
DE Flags: Precursor;
GN Name=F5;
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], CLEAVAGE BY ACTIVATED PROTEIN C, AND
RP MUTAGENESIS OF ARG-333 AND ARG-532.
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=9616155;
RA Yang T.L., Cui J., Rehumtulla A., Yang A., Moussalli M., Kaufman R.J.,
RA Ginsburg D.;
RT "The structure and function of murine factor V and its inactivation by
RT protein C.";
RL Blood 91:4593-4599(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1012.
RC STRAIN=C57BL/6J; TISSUE=Bone, Cerebellum, and Olfactory bulb;
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-841.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, 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).
CC -!- FUNCTION: Central regulator of hemostasis. It serves as a critical
CC cofactor for the prothrombinase activity of factor Xa that results in
CC the activation of prothrombin to thrombin.
CC -!- ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250}.
CC -!- SUBUNIT: Factor Va, the activated form of factor V, is composed of a
CC heavy chain and a light chain, non-covalently bound. The interaction
CC between the two chains is calcium-dependent. Forms heterodimer with
CC SERPINA5 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- DOMAIN: Domain B contains 32 X 9 AA tandem repeats, and 1 X 17 AA
CC repeats.
CC -!- PTM: Thrombin activates factor V proteolytically to the active
CC cofactor, factor Va (formation of a heavy chain at the N-terminus and a
CC light chain at the C-terminus). {ECO:0000250}.
CC -!- PTM: Sulfation is required for efficient thrombin cleavage and
CC activation and for full procoagulant activity. {ECO:0000250}.
CC -!- PTM: Activated protein C inactivates factor V and factor Va by
CC proteolytic degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE23393.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U52925; AAC99553.1; -; mRNA.
DR EMBL; AK137521; BAE23393.1; ALT_INIT; mRNA.
DR EMBL; AK139240; BAE23928.1; -; mRNA.
DR CCDS; CCDS35754.1; -.
DR PIR; T42764; T42764.
DR RefSeq; NP_032002.1; NM_007976.3.
DR AlphaFoldDB; O88783; -.
DR SMR; O88783; -.
DR BioGRID; 199574; 4.
DR IntAct; O88783; 2.
DR MINT; O88783; -.
DR STRING; 10090.ENSMUSP00000083204; -.
DR GlyGen; O88783; 8 sites.
DR iPTMnet; O88783; -.
DR PhosphoSitePlus; O88783; -.
DR MaxQB; O88783; -.
DR PaxDb; O88783; -.
DR PeptideAtlas; O88783; -.
DR PRIDE; O88783; -.
DR ProteomicsDB; 266826; -.
DR Antibodypedia; 863; 395 antibodies from 31 providers.
DR DNASU; 14067; -.
DR Ensembl; ENSMUST00000086040; ENSMUSP00000083204; ENSMUSG00000026579.
DR GeneID; 14067; -.
DR KEGG; mmu:14067; -.
DR UCSC; uc007dic.1; mouse.
DR CTD; 2153; -.
DR MGI; MGI:88382; F5.
DR VEuPathDB; HostDB:ENSMUSG00000026579; -.
DR eggNOG; ENOG502QSUG; Eukaryota.
DR GeneTree; ENSGT00940000158556; -.
DR HOGENOM; CLU_000948_0_0_1; -.
DR InParanoid; O88783; -.
DR OMA; GDYWEPS; -.
DR OrthoDB; 454773at2759; -.
DR PhylomeDB; O88783; -.
DR TreeFam; TF329807; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-5694530; Cargo concentration in the ER.
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR BioGRID-ORCS; 14067; 1 hit in 60 CRISPR screens.
DR ChiTaRS; F5; mouse.
DR PRO; PR:O88783; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; O88783; protein.
DR Bgee; ENSMUSG00000026579; Expressed in choroid plexus epithelium and 95 other tissues.
DR Genevisible; O88783; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0031091; C:platelet alpha granule; IDA:MGI.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0008015; P:blood circulation; IMP:MGI.
DR GO; GO:0007596; P:blood coagulation; IDA:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0032571; P:response to vitamin K; IEA:Ensembl.
DR GO; GO:0031638; P:zymogen activation; ISO:MGI.
DR CDD; cd00057; FA58C; 2.
DR Gene3D; 2.60.40.420; -; 5.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR024715; Factor_5/8-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR Pfam; PF07732; Cu-oxidase_3; 3.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR PIRSF; PIRSF000354; Factors_V_VIII; 1.
DR SMART; SM00231; FA58C; 2.
DR SUPFAM; SSF49503; SSF49503; 6.
DR SUPFAM; SSF49785; SSF49785; 2.
DR PROSITE; PS01285; FA58C_1; 2.
DR PROSITE; PS01286; FA58C_2; 2.
DR PROSITE; PS50022; FA58C_3; 2.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
PE 1: Evidence at protein level;
KW Blood coagulation; Calcium; Copper; Disulfide bond; Glycoprotein;
KW Hemostasis; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Signal; Sulfation; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..2183
FT /note="Coagulation factor V"
FT /id="PRO_0000358718"
FT CHAIN 20..736
FT /note="Coagulation factor V heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000358719"
FT PROPEP 737..1533
FT /note="Activation peptide (connecting region)"
FT /evidence="ECO:0000250"
FT /id="PRO_0000358720"
FT CHAIN 1534..2183
FT /note="Coagulation factor V light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000358721"
FT DOMAIN 30..328
FT /note="F5/8 type A 1"
FT DOMAIN 30..192
FT /note="Plastocyanin-like 1"
FT DOMAIN 202..328
FT /note="Plastocyanin-like 2"
FT DOMAIN 347..682
FT /note="F5/8 type A 2"
FT DOMAIN 347..524
FT /note="Plastocyanin-like 3"
FT DOMAIN 534..682
FT /note="Plastocyanin-like 4"
FT REPEAT 892..911
FT /note="1-1"
FT REPEAT 1175..1183
FT /note="2-1"
FT REPEAT 1184..1192
FT /note="2-2"
FT REPEAT 1193..1201
FT /note="2-3"
FT REPEAT 1202..1210
FT /note="2-4"
FT REPEAT 1211..1219
FT /note="2-5"
FT REPEAT 1220..1228
FT /note="2-6"
FT REPEAT 1229..1237
FT /note="2-7"
FT REPEAT 1238..1246
FT /note="2-8"
FT REPEAT 1247..1255
FT /note="2-9"
FT REPEAT 1256..1264
FT /note="2-10"
FT REPEAT 1265..1273
FT /note="2-11"
FT REPEAT 1274..1282
FT /note="2-12"
FT REPEAT 1283..1291
FT /note="2-13"
FT REPEAT 1292..1299
FT /note="2-14"
FT REPEAT 1300..1308
FT /note="2-15"
FT REPEAT 1309..1316
FT /note="2-16"
FT REPEAT 1317..1325
FT /note="2-17"
FT REPEAT 1326..1334
FT /note="2-18"
FT REPEAT 1335..1341
FT /note="2-19"
FT REPEAT 1342..1350
FT /note="2-20"
FT REPEAT 1351..1359
FT /note="2-21"
FT REPEAT 1360..1368
FT /note="2-22"
FT REPEAT 1369..1377
FT /note="2-23"
FT REPEAT 1378..1386
FT /note="2-24"
FT REPEAT 1387..1395
FT /note="2-25"
FT REPEAT 1396..1404
FT /note="2-26"
FT REPEAT 1405..1413
FT /note="2-27"
FT REPEAT 1414..1422
FT /note="2-28"
FT REPEAT 1423..1431
FT /note="2-29"
FT REPEAT 1432..1440
FT /note="2-30"
FT REPEAT 1441..1449
FT /note="2-31"
FT REPEAT 1452..1461
FT /note="2-32"
FT DOMAIN 1538..1866
FT /note="F5/8 type A 3"
FT DOMAIN 1538..1711
FT /note="Plastocyanin-like 5"
FT DOMAIN 1721..1866
FT /note="Plastocyanin-like 6"
FT DOMAIN 1866..2020
FT /note="F5/8 type C 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 2025..2180
FT /note="F5/8 type C 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT REGION 691..1533
FT /note="B"
FT /evidence="ECO:0000250"
FT REGION 884..904
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..908
FT /note="1 X 17 AA tandem repeats"
FT REGION 947..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1059..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1175..1461
FT /note="32 X 9 AA approximate tandem repeats of [TNP]-L-S-P-
FT D-L-S-Q-T"
FT REGION 1204..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1403..1462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1007..1022
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1113..1134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1802
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT BINDING 1804
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000250"
FT SITE 333..334
FT /note="Cleavage; by activated protein C"
FT /evidence="ECO:0000250"
FT SITE 532..533
FT /note="Cleavage; by activated protein C"
FT /evidence="ECO:0000250"
FT SITE 706..707
FT /note="Cleavage; by activated protein C"
FT /evidence="ECO:0000250"
FT SITE 736..737
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250"
FT SITE 1004..1005
FT /note="Cleavage; by activated protein C"
FT /evidence="ECO:0000250"
FT SITE 1029..1030
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250"
FT SITE 1533..1534
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250"
FT MOD_RES 638
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P12259"
FT MOD_RES 692
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 725
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 841
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT CARBOHYD 959
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 972
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1811
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1866..2020
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DISULFID 2025..2180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT MUTAGEN 333
FT /note="R->Q: Does not affect pro-coagulant function.
FT Partially resistant to inactivation by activated protein
FT C."
FT /evidence="ECO:0000269|PubMed:9616155"
FT MUTAGEN 532
FT /note="R->Q: Does not affect pro-coagulant function.
FT Partially resistant to inactivation by activated protein
FT C."
FT /evidence="ECO:0000269|PubMed:9616155"
SQ SEQUENCE 2183 AA; 247230 MW; BF0A8AA723F60317 CRC64;
MLLVCPCFFL LVVLGTRWAG WGSHQAEAAQ LRQFYVAAQG ILWNYHPEPT DPSLNSIPSF
KKIVYREYEQ YFKKEKPRSS NSGLLGPTLY AEVGDVIKVH FRNKADKPLS IHPQGIKYSK
FSEGASYADH TFPAERKDDA VAPGEEYTYE WIVSEDSGPT PDDPPCLTHI YYSYENLTQD
FNSGLIGPLL ICKKGTLTED GTQKMFDKQH VLLFAVFDES KSRSQSPSLM YTINGFVNKT
MPDITVCAHD HVSWHLIGMS SGPELFSIHF NGQVLEQNQH KVSTVTLVSA TSTTANMTMS
PEGRWIVSSL IPKHYQAGMQ AYIDIKNCPK KTRSPKTLTR EQRRYMKRWE YFIAAEEVIW
NYAPVIPANM DKIYRSQHLD NFSNQIGKHY KKVIYRQYEE ETFTKRTDNP SIKQSGILGP
VIRAQVRDTL KIVFKNMASR PYSIYPHGVT FSPYEDGINS SSTSGSHTTI RPVQPGETFT
YKWNILEFDE PTENDAQCLT RPYYSDVDVT RDIASGLIGL LLICKSRSLD QRGVQRVADI
EQQAVFAVFD ENKSWYIEDN INKFCENPDE VKRDDPKFYE SNIMSTINGY VPESISTLGF
CFDDTVQWHF CSVGTHDDIL TIHFTGHSFI YGRRHEDTLT LFPMRGESVT VTMDNVGTWM
LTTMNSNPKR RNLRLRFRDV KCNRDYDNED SYEIYEPPAP TSMTTRRIHD SLENEFGIDN
EDDDYQYLLA SSLGIRSFKN SSLNPEENEF NLTALALENS SEFISPSTDR VVDSNSSRIL
SKIINNNLKD FQRTLPGSGA TVAGTLLRNL IGLDENFVLN SSTEHRSSSY HENDMENPQS
NITMVYLLPL GPKGSGNREQ DKPKTIKTGR PHMMKHRFSW MKAPAGKTGR HSNPKNSYSG
MKSEEDIPSE LIPLKQKITS KFLNRRWRVA SEKGSYEIIA ANGEDTDVDK LTNSPQNQNI
TVPRGESTSH TNTTRKPSDL PTFSGVGHKS PHVRQEEENS GFQKRQLFIR TRKKKKNKKL
ALHSPLSPRG FDPLRGHNHS PFPDRRLLNH SLLLHKSNET ALSPDLNQTS PSMSTDRSLP
DYNQYSKNDT EQMSSSLDLY QSVPAEEHSP TFPAQDPDQT HSTTDPSYRS SPPELSQGLD
YDLSHDFYPD DIGLTSFFPD QSQKSSFSSD DDQAIPSSDL SLFTISPELD QTIIYPDLDQ
LLLSPEDNQK TSSPDLGQVP LSPDDNQKTS SPDLGQVSLS PDDNQKTSSP DLGQVPLSLD
DNQKTTSPDL GQVPLSPDDN QMITSPDLGQ VPLSSDNQKT SSPDLGQVPL FPEDNQNYFL
DLSQVPLSSD QNQETSSTDL LTLSPDFGQT VLSPDLDQLP LPSDNSQVTV SPDLSLLTLS
PDFNEIILAP DLGQVTLSPD LIQTNPALNH GHKASSADPD QASYPPDSGQ ASSLPELNRT
LPHPDLTHIP PPSPSPTLNN TSLSRKFNPL VVVGLSRVDG DDVEIVPSEE PERIDEDYAE
DDFVTYNDPY RTDTRTDVNS SRNPDTIAAW YLRGHGGHKK FYYIAAEEIT WNYAEFAQSE
MDHEDTGHTP KDTTYKKVVF RKYLDSTFTS RDPRAEYEEH LGILGPVIRA EVDDVIQVRF
KNLASRPYSL HAHGLSYEKS SEGKTYEDES PEWFQEDDAV QPNSSYTYVW HATKRSGPEN
PGSACRAWAY YSAVNVERDI HSGLIGPLLI CRKGTLHMER NLPMDMREFV LLFMVFDEKK
SWYYEKSKGS RRIESPEEKN AHKFYAINGM IYNLPGLRMY EQEWVRLHLL NMGGSRDIHV
VHFHGQTLLD NRTKQHQLGV WPLLPGSFKT LEMKASKPGW WLLDTEVGEN QVAGMQTPFL
IIDKECKMPM GLSTGVISDS QIKASEYLTY WEPRLARLNN AGSYNAWSIE KTALDFPIKP
WIQVDMQKEV VVTGIQTQGA KHYLKSCFTT EFQVAYSSDQ TNWQIFRGKS GKSVMYFTGN
SDGSTIKENR LDPPIVARYI RIHPTKSYNR PTLRLELQGC EVNGCSTPLG LEDGRIQDKQ
ITASSFKKSW WGDYWEPSLA RLNAQGRVNA WQAKANNNKQ WLQVDLLKIK KVTAIVTQGC
KSLSSEMYVK SYSIQYSDQG VAWKPYRQKS SMVDKIFEGN SNTKGHMKNF FNPPIISRFI
RIIPKTWNQS IALRLELFGC DIY
