ID   SF3A1_MOUSE             Reviewed;         791 AA.
AC   Q8K4Z5; Q8C0M7; Q8C128; Q8C175; Q921T3;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 176.
DE   RecName: Full=Splicing factor 3A subunit 1;
DE   AltName: Full=SF3a120;
GN   Name=Sf3a1;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skin, and Testis;
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   [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 [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary gland, and Mammary tumor;
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   [4]
RP   PROTEIN SEQUENCE OF 238-246; 471-484 AND 755-763, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
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).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [7]
RP   STRUCTURE BY NMR OF 685-786.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of ubiquitin-like domain in Sf3a120.";
RL   Submitted (NOV-2004) to the PDB data bank.
CC   -!- FUNCTION: Component of the 17S U2 SnRNP complex of the spliceosome, a
CC       large ribonucleoprotein complex that removes introns from transcribed
CC       pre-mRNAs. The 17S U2 SnRNP complex (1) directly participates in early
CC       spliceosome assembly and (2) mediates recognition of the intron branch
CC       site during pre-mRNA splicing by promoting the selection of the pre-
CC       mRNA branch-site adenosine, the nucleophile for the first step of
CC       splicing. Within the 17S U2 SnRNP complex, SF3A1 is part of the SF3A
CC       subcomplex that contributes to the assembly of the 17S U2 snRNP, and
CC       the subsequent assembly of the pre-spliceosome 'E' complex and the pre-
CC       catalytic spliceosome 'A' complex. Involved in pre-mRNA splicing as a
CC       component of pre-catalytic spliceosome 'B' complexes.
CC       {ECO:0000250|UniProtKB:Q15459}.
CC   -!- SUBUNIT: Component of the 17S U2 SnRNP complex, a ribonucleoprotein
CC       complex that contains small nuclear RNA (snRNA) U2 and a number of
CC       specific proteins. Part of the SF3A subcomplex of the 17S U2 SnRNP
CC       complex which is composed of three subunits; SF3A3/SAP61, SF3A2/SAP62
CC       and SF3A1/SAP114. SF3A associates with the splicing factor SF3B and a
CC       12S RNA unit to form the mature 17S U2 small nuclear ribonucleoprotein
CC       complex (17S U2 snRNP). SF3A1 functions as a scaffold that interacts
CC       directly with both SF3A2 and SF3A3. Identified in the spliceosome 'E'
CC       complex, a precursor of the spliceosome 'A' complex. Identified in the
CC       spliceosome 'A' and 'B' complexes. Identified in the spliceosome 'C'
CC       complex. {ECO:0000250|UniProtKB:Q15459}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15459}. Nucleus
CC       speckle {ECO:0000250|UniProtKB:Q15459}.
CC   -!- DOMAIN: SURP motif 2 mediates direct binding to SF3A3. {ECO:0000250}.
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DR   EMBL; AK028829; BAC26142.1; -; mRNA.
DR   EMBL; AK029095; BAC26294.1; -; mRNA.
DR   EMBL; AK030223; BAC26853.1; -; mRNA.
DR   EMBL; AL807825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC010727; AAH10727.1; -; mRNA.
DR   EMBL; BC029753; AAH29753.1; -; mRNA.
DR   CCDS; CCDS24380.1; -.
DR   RefSeq; NP_080451.4; NM_026175.5.
DR   PDB; 1WE7; NMR; -; A=685-786.
DR   PDBsum; 1WE7; -.
DR   AlphaFoldDB; Q8K4Z5; -.
DR   BMRB; Q8K4Z5; -.
DR   SMR; Q8K4Z5; -.
DR   BioGRID; 212207; 66.
DR   IntAct; Q8K4Z5; 38.
DR   MINT; Q8K4Z5; -.
DR   STRING; 10090.ENSMUSP00000002198; -.
DR   iPTMnet; Q8K4Z5; -.
DR   PhosphoSitePlus; Q8K4Z5; -.
DR   SwissPalm; Q8K4Z5; -.
DR   EPD; Q8K4Z5; -.
DR   jPOST; Q8K4Z5; -.
DR   MaxQB; Q8K4Z5; -.
DR   PaxDb; 10090-ENSMUSP00000002198; -.
DR   PeptideAtlas; Q8K4Z5; -.
DR   ProteomicsDB; 261504; -.
DR   Pumba; Q8K4Z5; -.
DR   Antibodypedia; 254; 354 antibodies from 27 providers.
DR   DNASU; 67465; -.
DR   Ensembl; ENSMUST00000002198.4; ENSMUSP00000002198.4; ENSMUSG00000002129.12.
DR   GeneID; 67465; -.
DR   KEGG; mmu:67465; -.
DR   UCSC; uc007hup.2; mouse.
DR   AGR; MGI:1914715; -.
DR   CTD; 10291; -.
DR   MGI; MGI:1914715; Sf3a1.
DR   VEuPathDB; HostDB:ENSMUSG00000002129; -.
DR   eggNOG; KOG0007; Eukaryota.
DR   GeneTree; ENSGT00730000111077; -.
DR   HOGENOM; CLU_013259_1_0_1; -.
DR   InParanoid; Q8K4Z5; -.
DR   OMA; HAYYRHR; -.
DR   OrthoDB; 168687at2759; -.
DR   PhylomeDB; Q8K4Z5; -.
DR   TreeFam; TF105705; -.
DR   Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR   BioGRID-ORCS; 67465; 28 hits in 80 CRISPR screens.
DR   ChiTaRS; Sf3a1; mouse.
DR   EvolutionaryTrace; Q8K4Z5; -.
DR   PRO; PR:Q8K4Z5; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q8K4Z5; Protein.
DR   Bgee; ENSMUSG00000002129; Expressed in epiblast (generic) and 272 other cell types or tissues.
DR   GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR   GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005681; C:spliceosomal complex; ISO:MGI.
DR   GO; GO:0005686; C:U2 snRNP; ISS:UniProtKB.
DR   GO; GO:0071005; C:U2-type precatalytic spliceosome; ISS:UniProtKB.
DR   GO; GO:0071004; C:U2-type prespliceosome; ISS:UniProtKB.
DR   GO; GO:0005684; C:U2-type spliceosomal complex; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR   GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
DR   GO; GO:0006397; P:mRNA processing; ISO:MGI.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR   GO; GO:1903241; P:U2-type prespliceosome assembly; ISS:UniProtKB.
DR   CDD; cd01800; Ubl_SF3a120; 1.
DR   Gene3D; 1.10.10.790; Surp module; 2.
DR   InterPro; IPR045146; SF3A1.
DR   InterPro; IPR022030; SF3A1_dom.
DR   InterPro; IPR035563; SF3As1_ubi.
DR   InterPro; IPR000061; Surp.
DR   InterPro; IPR035967; SWAP/Surp_sf.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR15316; SPLICEOSOME ASSOCIATED PROTEIN 114/SWAP SPLICING FACTOR-RELATED; 1.
DR   PANTHER; PTHR15316:SF1; SPLICING FACTOR 3A SUBUNIT 1; 1.
DR   Pfam; PF12230; PRP21_like_P; 1.
DR   Pfam; PF01805; Surp; 2.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SMART; SM00648; SWAP; 2.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF109905; Surp module (SWAP domain); 2.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50128; SURP; 2.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
DR   Genevisible; Q8K4Z5; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; Isopeptide bond;
KW   mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Spliceosome; Ubl conjugation.
FT   CHAIN           1..791
FT                   /note="Splicing factor 3A subunit 1"
FT                   /id="PRO_0000114918"
FT   REPEAT          52..94
FT                   /note="SURP motif 1"
FT   REPEAT          166..208
FT                   /note="SURP motif 2"
FT   DOMAIN          705..788
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          318..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          528..582
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          664..684
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          678..700
FT                   /note="Required and sufficient for nuclear import"
FT                   /evidence="ECO:0000250|UniProtKB:Q15459"
FT   COMPBIAS        1..18
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        321..338
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..383
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..502
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        529..545
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..582
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            169
FT                   /note="Critical for binding to SF3A3"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         55
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         320
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15459"
FT   MOD_RES         329
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15459"
FT   MOD_RES         357
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15459"
FT   MOD_RES         411
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15459"
FT   MOD_RES         449
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15459"
FT   MOD_RES         454
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15459"
FT   MOD_RES         506
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15459"
FT   MOD_RES         757
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q15459"
FT   CROSSLNK        20
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15459"
FT   CROSSLNK        131
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15459"
FT   CROSSLNK        422
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15459"
FT   CROSSLNK        497
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15459"
FT   CROSSLNK        540
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15459"
FT   CROSSLNK        684
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q15459"
FT   CONFLICT        257
FT                   /note="R -> G (in Ref. 1; BAC26142)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        368
FT                   /note="P -> L (in Ref. 1; BAC26294)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        708
FT                   /note="Q -> L (in Ref. 1; BAC26853)"
FT                   /evidence="ECO:0000305"
FT   HELIX           685..687
FT                   /evidence="ECO:0007829|PDB:1WE7"
FT   HELIX           692..698
FT                   /evidence="ECO:0007829|PDB:1WE7"
FT   STRAND          703..709
FT                   /evidence="ECO:0007829|PDB:1WE7"
FT   STRAND          713..715
FT                   /evidence="ECO:0007829|PDB:1WE7"
FT   STRAND          721..729
FT                   /evidence="ECO:0007829|PDB:1WE7"
FT   HELIX           736..745
FT                   /evidence="ECO:0007829|PDB:1WE7"
FT   TURN            750..752
FT                   /evidence="ECO:0007829|PDB:1WE7"
FT   STRAND          753..757
FT                   /evidence="ECO:0007829|PDB:1WE7"
FT   STRAND          760..762
FT                   /evidence="ECO:0007829|PDB:1WE7"
FT   HELIX           768..771
FT                   /evidence="ECO:0007829|PDB:1WE7"
FT   STRAND          778..783
FT                   /evidence="ECO:0007829|PDB:1WE7"
SQ   SEQUENCE   791 AA;  88545 MW;  D83D0432469C3708 CRC64;
     MQAGPVQAVP PPPPVATESK QPIEEEASSK EDPTPSKPVV GIIYPPPEVR NIVDKTASFV
     ARNGPEFEAR IRQNEINNPK FNFLNPNDPY HAYYRHKVSE FKEGKAQEPS AAIPKVMQQQ
     QQATQQQLPQ KVQAQVIQET IVPKEPPPEF EFIADPPSIS AFDLDVVKLT AQFVARNGRQ
     FLTQLMQKEQ RNYQFDFLRP QHSLFNYFTK LVEQYTKILI PPKGLFSKLK KEAENPREVL
     DQVCYRVEWA KFQERERKKE EEEKEKERVA YAQIDWHDFV VVETVDFQPN EQGNFPPPTT
     PEELGARILI QERYEKFGES EEVEMEVESD EEDQEKAEET PSQLDQDTQV QDMDEGSDDE
     EEGQKVPPPP ETPMPPPLPP TPDQVIVRKD YDPKASKPLP PAPAPDEYLV SPITGEKIPA
     SKMQEHMRIG LLDPRWLEQR DRSIREKQSD DEVYAPGLDI ESSLKQLAER RTDIFGVEET
     AIGKKIGEEE IQKPEEKVTW DGHSGSMART QQAAQANITL QEQIEAIHKA KGLVPEDDTK
     EKIGPSKPNE IPQQPPPPSS ATNIPSSAPP ITSVPRPPAM PPPVRTTVVS AVPVMPRPPM
     ASVVRLPPGS VIAPMPPIIH APRINVVPMP PAAPPIMAPR PPPMIVPTAF VPAPPVAPVP
     APAPMPPVHP PPPMEDEPPS KKLKTEDSLM PEEEFLRRNK GPVSIKVQVP NMQDKTEWKL
     NGQGLVFTLP LTDQVSVIKV KIHEATGMPA GKQKLQYEGI FIKDSNSLAY YNMASGAVIH
     LALKERGGRK K
//