SRPK3_HUMAN
ID SRPK3_HUMAN Reviewed; 567 AA.
AC Q9UPE1; Q13583; Q4F970; Q562F5; Q9UM62;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=SRSF protein kinase 3;
DE EC=2.7.11.1;
DE AltName: Full=Muscle-specific serine kinase 1;
DE Short=MSSK-1;
DE AltName: Full=Serine/arginine-rich protein-specific kinase 3;
DE Short=SR-protein-specific kinase 3;
DE AltName: Full=Serine/threonine-protein kinase 23;
GN Name=SRPK3; Synonyms=MSSK1, STK23;
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] (ISOFORMS 2 AND 3).
RC TISSUE=Skeletal muscle;
RA Brenner V., Rosenthal A., Platzer M.;
RT "Cloning and sequencing of a new human serine kinase gene located in human
RT Xq28.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RA Zhou G., Nong W., Li H., Ke R., Shen C., Zhong G., Zheng Z., Liang M.,
RA Wen S., Lin L., Yang S.;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Brain;
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 [6]
RP TISSUE SPECIFICITY.
RX PubMed=11063724; DOI=10.1093/hmg/9.18.2651;
RA Grunau C., Hindermann W., Rosenthal A.;
RT "Large-scale methylation analysis of human genomic DNA reveals tissue-
RT specific differences between the methylation profiles of genes and
RT pseudogenes.";
RL Hum. Mol. Genet. 9:2651-2663(2000).
RN [7]
RP REVIEW ON FUNCTION.
RX PubMed=21205200; DOI=10.1111/j.1742-4658.2010.07987.x;
RA Giannakouros T., Nikolakaki E., Mylonis I., Georgatsou E.;
RT "Serine-arginine protein kinases: a small protein kinase family with a
RT large cellular presence.";
RL FEBS J. 278:570-586(2011).
RN [8]
RP VARIANTS [LARGE SCALE ANALYSIS] CYS-101; GLU-114 AND LYS-233.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Serine/arginine-rich protein-specific kinase which
CC specifically phosphorylates its substrates at serine residues located
CC in regions rich in arginine/serine dipeptides, known as RS domains.
CC Phosphorylates the SR splicing factor SRSF1 and the lamin-B receptor
CC (LBR) in vitro. Required for normal muscle development (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- INTERACTION:
CC Q9UPE1; Q96SB4: SRPK1; NbExp=3; IntAct=EBI-6381269, EBI-539478;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9UPE1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UPE1-2; Sequence=VSP_040939, VSP_040940, VSP_040941;
CC Name=3;
CC IsoId=Q9UPE1-3; Sequence=VSP_040940, VSP_040941;
CC Name=4;
CC IsoId=Q9UPE1-4; Sequence=VSP_040940;
CC -!- TISSUE SPECIFICITY: Exclusively expressed in skeletal and heart muscle.
CC {ECO:0000269|PubMed:11063724}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; AF027406; AAD01848.1; -; mRNA.
DR EMBL; U82808; AAD00539.1; -; mRNA.
DR EMBL; DQ099381; AAZ13757.1; -; mRNA.
DR EMBL; AK301749; BAG63211.1; -; mRNA.
DR EMBL; U52111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC092416; AAH92416.1; -; mRNA.
DR EMBL; BC117124; AAI17125.1; -; mRNA.
DR CCDS; CCDS35441.1; -. [Q9UPE1-1]
DR CCDS; CCDS55537.1; -. [Q9UPE1-3]
DR CCDS; CCDS55538.1; -. [Q9UPE1-4]
DR RefSeq; NP_001164231.1; NM_001170760.1. [Q9UPE1-4]
DR RefSeq; NP_001164232.1; NM_001170761.1. [Q9UPE1-3]
DR RefSeq; NP_055185.2; NM_014370.3. [Q9UPE1-1]
DR AlphaFoldDB; Q9UPE1; -.
DR SMR; Q9UPE1; -.
DR BioGRID; 117745; 144.
DR IntAct; Q9UPE1; 138.
DR STRING; 9606.ENSP00000359119; -.
DR BindingDB; Q9UPE1; -.
DR ChEMBL; CHEMBL5415; -.
DR DrugCentral; Q9UPE1; -.
DR GuidetoPHARMACOLOGY; 2210; -.
DR iPTMnet; Q9UPE1; -.
DR PhosphoSitePlus; Q9UPE1; -.
DR BioMuta; SRPK3; -.
DR DMDM; 332278151; -.
DR EPD; Q9UPE1; -.
DR jPOST; Q9UPE1; -.
DR MassIVE; Q9UPE1; -.
DR MaxQB; Q9UPE1; -.
DR PaxDb; Q9UPE1; -.
DR PeptideAtlas; Q9UPE1; -.
DR PRIDE; Q9UPE1; -.
DR ProteomicsDB; 85367; -. [Q9UPE1-1]
DR ProteomicsDB; 85368; -. [Q9UPE1-2]
DR ProteomicsDB; 85369; -. [Q9UPE1-3]
DR ProteomicsDB; 85370; -. [Q9UPE1-4]
DR Antibodypedia; 30953; 172 antibodies from 26 providers.
DR DNASU; 26576; -.
DR Ensembl; ENST00000370101.8; ENSP00000359119.3; ENSG00000184343.11. [Q9UPE1-1]
DR Ensembl; ENST00000370104.5; ENSP00000359122.1; ENSG00000184343.11. [Q9UPE1-4]
DR Ensembl; ENST00000393786.7; ENSP00000377376.3; ENSG00000184343.11. [Q9UPE1-3]
DR GeneID; 26576; -.
DR KEGG; hsa:26576; -.
DR MANE-Select; ENST00000370101.8; ENSP00000359119.3; NM_014370.4; NP_055185.2.
DR UCSC; uc004fil.4; human. [Q9UPE1-1]
DR CTD; 26576; -.
DR DisGeNET; 26576; -.
DR GeneCards; SRPK3; -.
DR HGNC; HGNC:11402; SRPK3.
DR HPA; ENSG00000184343; Tissue enhanced (skeletal muscle, tongue).
DR MIM; 301002; gene.
DR neXtProt; NX_Q9UPE1; -.
DR OpenTargets; ENSG00000184343; -.
DR PharmGKB; PA162404805; -.
DR VEuPathDB; HostDB:ENSG00000184343; -.
DR eggNOG; KOG1290; Eukaryota.
DR GeneTree; ENSGT00940000157877; -.
DR InParanoid; Q9UPE1; -.
DR OMA; IEKYEWP; -.
DR OrthoDB; 866496at2759; -.
DR TreeFam; TF105334; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; Q9UPE1; -.
DR SignaLink; Q9UPE1; -.
DR BioGRID-ORCS; 26576; 8 hits in 725 CRISPR screens.
DR ChiTaRS; SRPK3; human.
DR GenomeRNAi; 26576; -.
DR Pharos; Q9UPE1; Tchem.
DR PRO; PR:Q9UPE1; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9UPE1; protein.
DR Bgee; ENSG00000184343; Expressed in hindlimb stylopod muscle and 136 other tissues.
DR ExpressionAtlas; Q9UPE1; baseline and differential.
DR Genevisible; Q9UPE1; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0060537; P:muscle tissue development; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0050684; P:regulation of mRNA processing; IBA:GO_Central.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR GO; GO:0000245; P:spliceosomal complex assembly; IBA:GO_Central.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Developmental protein; Differentiation;
KW Kinase; Myogenesis; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..567
FT /note="SRSF protein kinase 3"
FT /id="PRO_0000086709"
FT DOMAIN 79..565
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..280
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 212
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 85..93
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0G2"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0G2"
FT VAR_SEQ 1..42
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_040939"
FT VAR_SEQ 259
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.2"
FT /id="VSP_040940"
FT VAR_SEQ 318..350
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_040941"
FT VARIANT 101
FT /note="R -> C (in dbSNP:rs55910507)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041119"
FT VARIANT 114
FT /note="G -> E (in dbSNP:rs35865042)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041120"
FT VARIANT 233
FT /note="E -> K (in dbSNP:rs34497419)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041121"
SQ SEQUENCE 567 AA; 62014 MW; 754A9F3759ADEE82 CRC64;
MSASTGGGGD SGGSGGSSSS SQASCGPESS GSELALATPV PQMLQGLLGS DDEEQEDPKD
YCKGGYHPVK IGDVFNGRYH VVRKLGWGHF STVWLCWDIQ RKRFVALKVV KSAGHYTETA
VDEIKLLKCV RDSDPSDPKR ETIVQLIDDF RISGVNGVHV CMVLEVLGHQ LLKWIIKSNY
QGLPVPCVKS IVRQVLHGLD YLHTKCKIIH TDIKPENILL CVGDAYIRRL AAEATEWQQA
GAPPPSRSIV STAPQEVLQT GKLSKNKRKK MRRKRKQQKR LLEERLRDLQ RLEAMEAATQ
AEDSGLRLDG GSGSTSSSGC HPGGARAGPS PASSSPAPGG GRSLSAGSQT SGFSGSLFSP
ASCSILSGSS NQRETGGLLS PSTPFGASNL LVNPLEPQNA DKIKIKIADL GNACWVHKHF
TEDIQTRQYR AVEVLIGAEY GPPADIWSTA CMAFELATGD YLFEPHSGED YSRDEDHIAH
IVELLGDIPP AFALSGRYSR EFFNRRGELR HIHNLKHWGL YEVLMEKYEW PLEQATQFSA
FLLPMMEYIP EKRASAADCL QHPWLNP
