ID   SIAL_HUMAN              Reviewed;         317 AA.
AC   P21815;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 4.
DT   27-MAR-2024, entry version 175.
DE   RecName: Full=Integrin-binding sialoprotein {ECO:0000303|PubMed:36261010};
DE   AltName: Full=Bone sialoprotein 2 {ECO:0000305};
DE   AltName: Full=Bone sialoprotein II;
DE            Short=BSP II;
DE   AltName: Full=Cell-binding sialoprotein;
DE   Flags: Precursor;
GN   Name=IBSP; Synonyms=BNSP;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLY-213; GLY-219 AND VAL-268.
RX   PubMed=2404984; DOI=10.1016/s0021-9258(19)39982-x;
RA   Fisher L.W., McBride O.W., Termine J.D., Young M.F.;
RT   "Human bone sialoprotein. Deduced protein sequence and chromosomal
RT   localization.";
RL   J. Biol. Chem. 265:2347-2351(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-195; GLY-213; GLY-219
RP   AND ASP-270.
RX   PubMed=8406493; DOI=10.1006/geno.1993.1340;
RA   Kerr J.M., Fisher L.W., Termine J.D., Wang M.G., McBride W., Young M.F.;
RT   "The human bone sialoprotein gene (IBSP): genomic localization and
RT   characterization.";
RL   Genomics 17:408-415(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-195; GLY-213 AND
RP   ASP-270.
RX   PubMed=8061918; DOI=10.1016/0945-053x(94)90027-2;
RA   Kim R.H., Shapiro H.S., Li J.J., Wrana J.L., Sodek J.;
RT   "Characterization of the human bone sialoprotein (BSP) gene and its
RT   promoter sequence.";
RL   Matrix Biol. 14:31-40(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RX   PubMed=3597437; DOI=10.1016/s0021-9258(18)47991-4;
RA   Fisher L.W., Hawkins G.R., Tuross N., Termine J.D.;
RT   "Purification and partial characterization of small proteoglycans I and II,
RT   bone sialoproteins I and II, and osteonectin from the mineral compartment
RT   of developing human bone.";
RL   J. Biol. Chem. 262:9702-9708(1987).
RN   [6]
RP   PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP   SPECIFICITY, GLYCOSYLATION AT THR-119; THR-122; THR-227; THR-228; THR-229;
RP   THR-238 AND THR-239, STRUCTURE OF CARBOHYDRATE, VARIANT GLY-213, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=11459848; DOI=10.1074/jbc.m105689200;
RA   Wuttke M., Muller S., Nitsche D.P., Paulsson M., Hanisch F.G., Maurer P.;
RT   "Structural characterization of human recombinant and bone-derived bone
RT   sialoprotein. Functional implications for cell attachment and
RT   hydroxyapatite binding.";
RL   J. Biol. Chem. 276:36839-36848(2001).
RN   [7]
RP   FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=1818768; DOI=10.1007/bf02555854;
RA   Bianco P., Fisher L.W., Young M.F., Termine J.D., Robey P.G.;
RT   "Expression of bone sialoprotein (BSP) in developing human tissues.";
RL   Calcif. Tissue Int. 49:421-426(1991).
RN   [8]
RP   FUNCTION, AND DOMAIN.
RX   PubMed=10640428; DOI=10.1006/excr.1999.4765;
RA   Byzova T.V., Kim W., Midura R.J., Plow E.F.;
RT   "Activation of integrin alpha(V)beta(3) regulates cell adhesion and
RT   migration to bone sialoprotein.";
RL   Exp. Cell Res. 254:299-308(2000).
RN   [9]
RP   PHOSPHORYLATION AT SER-31, SULFATION AT TYR-313 AND TYR-314, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=11669636; DOI=10.1021/bi010887r;
RA   Zaia J., Boynton R., Heinegard D., Barry F.;
RT   "Posttranslational modifications to human bone sialoprotein determined by
RT   mass spectrometry.";
RL   Biochemistry 40:12983-12991(2001).
RN   [10]
RP   FUNCTION, DOMAIN, AND MUTAGENESIS OF 286-ARG--ASP-288 AND ASP-288.
RX   PubMed=24103036; DOI=10.1111/eos.12081;
RA   Rapuano B.E., MacDonald D.E.;
RT   "Structure-activity relationship of human bone sialoprotein peptides.";
RL   Eur. J. Oral Sci. 121:600-609(2013).
RN   [11]
RP   TISSUE SPECIFICITY.
RX   PubMed=36261010; DOI=10.1016/j.celrep.2022.111511;
RA   Ghochani Y., Muthukrishnan S.D., Sohrabi A., Kawaguchi R., Condro M.C.,
RA   Bastola S., Gao F., Qin Y., Mottahedeh J., Iruela-Arispe M.L., Rao N.,
RA   Laks D.R., Liau L.M., Mathern G.W., Goldman S.A., Carmichael S.T.,
RA   Nakano I., Coppola G., Seidlits S.K., Kornblum H.I.;
RT   "A molecular interactome of the glioblastoma perivascular niche reveals
RT   integrin binding sialoprotein as a mediator of tumor cell migration.";
RL   Cell Rep. 41:111511-111511(2022).
CC   -!- FUNCTION: Binds tightly to hydroxyapatite (PubMed:11459848). Appears to
CC       form an integral part of the mineralized matrix (PubMed:1818768).
CC       Probably important to cell-matrix interaction (PubMed:1818768).
CC       Promotes adhesion and migration of various cells via the alpha-V/beta-3
CC       integrin receptor (ITGAV:ITGB3) (PubMed:10640428, PubMed:11459848,
CC       PubMed:24103036). {ECO:0000269|PubMed:10640428,
CC       ECO:0000269|PubMed:11459848, ECO:0000269|PubMed:1818768,
CC       ECO:0000269|PubMed:24103036}.
CC   -!- SUBUNIT: Monomer (PubMed:11459848). Interacts with integrins; the
CC       interaction promotes cell adhesion (By similarity).
CC       {ECO:0000250|UniProtKB:Q28862, ECO:0000269|PubMed:11459848}.
CC   -!- INTERACTION:
CC       P21815; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-18400392, EBI-10175124;
CC       P21815; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-18400392, EBI-12175685;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11459848}.
CC   -!- TISSUE SPECIFICITY: Expressed in bone (at protein level)
CC       (PubMed:11459848). Expressed in trophoblast cells of placenta (at
CC       protein level) (PubMed:1818768). Expressed in brain (PubMed:36261010).
CC       {ECO:0000269|PubMed:11459848, ECO:0000269|PubMed:1818768,
CC       ECO:0000269|PubMed:36261010}.
CC   -!- DEVELOPMENTAL STAGE: In fetal developing bone of gestational age of 14-
CC       17 weeks, expressed in mature osteoblasts, young osteocytes and
CC       osteoclasts (at protein level) (PubMed:1818768). Expressed in bone
CC       matrix (at protein level) (PubMed:1818768). Expressed in osteoid at the
CC       borderline with mature mineralized matrix (at protein level)
CC       (PubMed:1818768). Expressed in chondrocytes in the growth plate (at
CC       protein level) (PubMed:1818768). Not detected in preosteogenic cells in
CC       the inner layer of the periosteum and in the fibroblastic cells in the
CC       outer layer (at protein level) (PubMed:1818768). Not detected in
CC       cartilage matrix (at protein level) (PubMed:1818768). Not detected in
CC       ocular tissues, skin, tendon, muscle and kidney of gestational age of
CC       14-17 weeks (at protein level) (PubMed:1818768).
CC       {ECO:0000269|PubMed:1818768}.
CC   -!- DOMAIN: The Arg-Gly-Asp (RGD) sequence serves as an integrin-binding
CC       motif and is required for integrin-mediated cell attachment.
CC       {ECO:0000269|PubMed:10640428, ECO:0000269|PubMed:24103036}.
CC   -!- PTM: N-glycosylated; glycans consist of sialylated and core-fucosylated
CC       bi-, tri- and tetraantennary chains. {ECO:0000269|PubMed:11459848}.
CC   -!- PTM: O-glycosylated at eight sites; mucin-type glycans contain Gal,
CC       GlcNAc, GalNAc and terminal NeuAc. {ECO:0000269|PubMed:11459848}.
CC   -!- MISCELLANEOUS: It is possible that the segments of clustered carboxyl
CC       groups mediate the strong binding to hydroxyapatite. Highly expressed
CC       in glioblastoma samples, especially in microvascular-enriched regions
CC       (PubMed:36261010). Elevated expression correlates with poor survival in
CC       patients with proneural glioblastomas (PubMed:36261010). Promotes up-
CC       regulation of genes associated with mesenchymal phenotype in proneural
CC       glioblastoma cultures (PubMed:36261010). Promotes migration and
CC       proliferation of glioblastoma, breast carcinoma and melanoma cells
CC       (PubMed:36261010, PubMed:10640428). ITGAV, ITGAV:ITGB3 or ITGAV:ITGB5
CC       act as integrin receptors for IBSP in glioblastoma, breast carcinoma
CC       and melanoma cells (PubMed:36261010, PubMed:10640428).
CC       {ECO:0000269|PubMed:10640428, ECO:0000269|PubMed:36261010}.
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DR   EMBL; J05213; AAC95490.1; -; mRNA.
DR   EMBL; L09558; AAA60549.1; -; Genomic_DNA.
DR   EMBL; L09554; AAA60549.1; JOINED; Genomic_DNA.
DR   EMBL; L09555; AAA60549.1; JOINED; Genomic_DNA.
DR   EMBL; L09556; AAA60549.1; JOINED; Genomic_DNA.
DR   EMBL; L09557; AAA60549.1; JOINED; Genomic_DNA.
DR   EMBL; L24759; AAC37560.1; -; Genomic_DNA.
DR   EMBL; L24757; AAC37560.1; JOINED; Genomic_DNA.
DR   EMBL; AC093768; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS3624.1; -.
DR   PIR; A35043; GEHUS.
DR   RefSeq; NP_004958.2; NM_004967.3.
DR   AlphaFoldDB; P21815; -.
DR   BioGRID; 109608; 14.
DR   IntAct; P21815; 2.
DR   STRING; 9606.ENSP00000226284; -.
DR   GlyCosmos; P21815; 11 sites, No reported glycans.
DR   GlyGen; P21815; 11 sites.
DR   iPTMnet; P21815; -.
DR   PhosphoSitePlus; P21815; -.
DR   BioMuta; IBSP; -.
DR   DMDM; 317373545; -.
DR   MassIVE; P21815; -.
DR   PaxDb; 9606-ENSP00000226284; -.
DR   PeptideAtlas; P21815; -.
DR   ProteomicsDB; 53929; -.
DR   Antibodypedia; 14494; 421 antibodies from 32 providers.
DR   DNASU; 3381; -.
DR   Ensembl; ENST00000226284.7; ENSP00000226284.5; ENSG00000029559.7.
DR   GeneID; 3381; -.
DR   KEGG; hsa:3381; -.
DR   MANE-Select; ENST00000226284.7; ENSP00000226284.5; NM_004967.4; NP_004958.2.
DR   UCSC; uc003hqx.5; human.
DR   AGR; HGNC:5341; -.
DR   CTD; 3381; -.
DR   DisGeNET; 3381; -.
DR   GeneCards; IBSP; -.
DR   HGNC; HGNC:5341; IBSP.
DR   HPA; ENSG00000029559; Tissue enhanced (pituitary).
DR   MIM; 147563; gene.
DR   neXtProt; NX_P21815; -.
DR   OpenTargets; ENSG00000029559; -.
DR   PharmGKB; PA29590; -.
DR   VEuPathDB; HostDB:ENSG00000029559; -.
DR   eggNOG; KOG1181; Eukaryota.
DR   GeneTree; ENSGT00390000002485; -.
DR   HOGENOM; CLU_076119_0_0_1; -.
DR   InParanoid; P21815; -.
DR   OMA; HAYFYPH; -.
DR   OrthoDB; 4616590at2759; -.
DR   PhylomeDB; P21815; -.
DR   TreeFam; TF338678; -.
DR   PathwayCommons; P21815; -.
DR   Reactome; R-HSA-216083; Integrin cell surface interactions.
DR   Reactome; R-HSA-3000178; ECM proteoglycans.
DR   SignaLink; P21815; -.
DR   SIGNOR; P21815; -.
DR   BioGRID-ORCS; 3381; 9 hits in 1142 CRISPR screens.
DR   ChiTaRS; IBSP; human.
DR   GeneWiki; Bone_sialoprotein; -.
DR   GenomeRNAi; 3381; -.
DR   Pharos; P21815; Tbio.
DR   PRO; PR:P21815; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; P21815; Protein.
DR   Bgee; ENSG00000029559; Expressed in tibia and 105 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0031982; C:vesicle; ISS:UniProtKB.
DR   GO; GO:0005178; F:integrin binding; IMP:CAFA.
DR   GO; GO:0036094; F:small molecule binding; IPI:DisProt.
DR   GO; GO:0030282; P:bone mineralization; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; ISS:UniProtKB.
DR   GO; GO:0030198; P:extracellular matrix organization; ISS:UniProtKB.
DR   GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; IMP:CAFA.
DR   DisProt; DP00332; -.
DR   InterPro; IPR008412; BSP_II.
DR   PANTHER; PTHR10345; BONE SIALOPROTEIN 2; 1.
DR   PANTHER; PTHR10345:SF0; BONE SIALOPROTEIN 2; 1.
DR   Pfam; PF05432; BSP_II; 1.
DR   Genevisible; P21815; HS.
PE   1: Evidence at protein level;
KW   Biomineralization; Cell adhesion; Direct protein sequencing; Glycoprotein;
KW   Phosphoprotein; Reference proteome; Secreted; Sialic acid; Signal;
KW   Sulfation.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..317
FT                   /note="Integrin-binding sialoprotein"
FT                   /id="PRO_0000020330"
FT   REGION          58..254
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           286..288
FT                   /note="Integrin-binding motif"
FT                   /evidence="ECO:0000305|PubMed:10640428,
FT                   ECO:0000305|PubMed:24103036"
FT   COMPBIAS        69..103
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..171
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        172..195
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         31
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:11669636"
FT   MOD_RES         67
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28862"
FT   MOD_RES         74
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28862"
FT   MOD_RES         75
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28862"
FT   MOD_RES         94
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28862"
FT   MOD_RES         100
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28862"
FT   MOD_RES         149
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28862"
FT   MOD_RES         280
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q28862"
FT   MOD_RES         313
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000269|PubMed:11669636"
FT   MOD_RES         314
FT                   /note="Sulfotyrosine"
FT                   /evidence="ECO:0000269|PubMed:11669636"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        119
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000305|PubMed:11459848"
FT   CARBOHYD        122
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000305|PubMed:11459848"
FT   CARBOHYD        177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        227
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000305|PubMed:11459848"
FT   CARBOHYD        228
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000305|PubMed:11459848"
FT   CARBOHYD        229
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000305|PubMed:11459848"
FT   CARBOHYD        238
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000305|PubMed:11459848"
FT   CARBOHYD        239
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000305|PubMed:11459848"
FT   VARIANT         195
FT                   /note="G -> E (in dbSNP:rs1054627)"
FT                   /evidence="ECO:0000269|PubMed:8061918,
FT                   ECO:0000269|PubMed:8406493"
FT                   /id="VAR_058014"
FT   VARIANT         213
FT                   /note="D -> G (in dbSNP:rs13144371)"
FT                   /evidence="ECO:0000269|PubMed:11459848,
FT                   ECO:0000269|PubMed:2404984, ECO:0000269|PubMed:8061918,
FT                   ECO:0000269|PubMed:8406493"
FT                   /id="VAR_058015"
FT   VARIANT         219
FT                   /note="R -> G (in dbSNP:rs17013181)"
FT                   /evidence="ECO:0000269|PubMed:2404984,
FT                   ECO:0000269|PubMed:8406493"
FT                   /id="VAR_058016"
FT   VARIANT         256
FT                   /note="T -> A (in dbSNP:rs17013182)"
FT                   /id="VAR_056579"
FT   VARIANT         268
FT                   /note="A -> V (in dbSNP:rs1054628)"
FT                   /evidence="ECO:0000269|PubMed:2404984"
FT                   /id="VAR_056580"
FT   VARIANT         270
FT                   /note="E -> D (in dbSNP:rs1054629)"
FT                   /evidence="ECO:0000269|PubMed:8061918,
FT                   ECO:0000269|PubMed:8406493"
FT                   /id="VAR_058017"
FT   MUTAGEN         286..288
FT                   /note="RGD->KAE: Significantly reduces cell attachment
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:24103036"
FT   MUTAGEN         288
FT                   /note="D->E: Modestly reduces cell attachment activity."
FT                   /evidence="ECO:0000269|PubMed:24103036"
FT   CONFLICT        94
FT                   /note="S -> L (in Ref. 3; AAC37560)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   317 AA;  35148 MW;  736CB6B8C3716FE7 CRC64;
     MKTALILLSI LGMACAFSMK NLHRRVKIED SEENGVFKYR PRYYLYKHAY FYPHLKRFPV
     QGSSDSSEEN GDDSSEEEEE EEETSNEGEN NEESNEDEDS EAENTTLSAT TLGYGEDATP
     GTGYTGLAAI QLPKKAGDIT NKATKEKESD EEEEEEEEGN ENEESEAEVD ENEQGINGTS
     TNSTEAENGN GSSGGDNGEE GEEESVTGAN AEDTTETGRQ GKGTSKTTTS PNGGFEPTTP
     PQVYRTTSPP FGKTTTVEYE GEYEYTGANE YDNGYEIYES ENGEPRGDNY RAYEDEYSYF
     KGQGYDGYDG QNYYHHQ
//