ID KHDR2_HUMAN Reviewed; 349 AA. AC Q5VWX1; A8K7M8; Q8N4I4; Q8TCZ4; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 1. DT 24-JAN-2024, entry version 174. DE RecName: Full=KH domain-containing, RNA-binding, signal transduction-associated protein 2; DE AltName: Full=Sam68-like mammalian protein 1; DE Short=SLM-1; DE Short=hSLM-1; GN Name=KHDRBS2; Synonyms=SLM1; 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 TISSUE SPECIFICITY. RC TISSUE=Fetal brain; RX PubMed=12549823; DOI=10.1023/a:1021246109101; RA Wang L., Xu J., Zeng L., Ye X., Wu Q., Dai J., Ji C., Gu S., Zhao C., RA Xie Y., Mao Y.; RT "Cloning and characterization of a novel human STAR domain containing cDNA RT KHDRBS2."; RL Mol. Biol. Rep. 29:369-375(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Spleen; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 METHYLATION. RX PubMed=12529443; DOI=10.1091/mbc.e02-08-0484; RA Cote J., Boisvert F.-M., Boulanger M.-C., Bedford M.T., Richard S.; RT "Sam68 RNA binding protein is an in vivo substrate for protein arginine N- RT methyltransferase 1."; RL Mol. Biol. Cell 14:274-287(2003). RN [7] RP INTERACTION WITH RBMX. RX PubMed=19282290; DOI=10.1074/jbc.m901026200; RA Heinrich B., Zhang Z., Raitskin O., Hiller M., Benderska N., Hartmann A.M., RA Bracco L., Elliott D., Ben-Ari S., Soreq H., Sperling J., Sperling R., RA Stamm S.; RT "Heterogeneous nuclear ribonucleoprotein G regulates splice site selection RT by binding to CC(A/C)-rich regions in pre-mRNA."; RL J. Biol. Chem. 284:14303-14315(2009). CC -!- FUNCTION: RNA-binding protein that plays a role in the regulation of CC alternative splicing and influences mRNA splice site selection and exon CC inclusion. Binds both poly(A) and poly(U) homopolymers. Phosphorylation CC by PTK6 inhibits its RNA-binding ability (By similarity). Induces an CC increased concentration-dependent incorporation of exon in CD44 pre- CC mRNA by direct binding to purine-rich exonic enhancer. Can regulate CC alternative splicing of NRXN1 in the laminin G-like domain 6 containing CC the evolutionary conserved neurexin alternative spliced segment 4 (AS4) CC involved in neurexin selective targeting to postsynaptic partners. CC Regulates cell-type specific alternative splicing of NRXN1 at AS4 and CC acts synergystically with SAM68 in exon skipping. In contrast acts CC antagonistically with SAM68 in NRXN3 exon skipping at AS4. Its CC phosphorylation by FYN inhibits its ability to regulate splice site CC selection. May function as an adapter protein for Src kinases during CC mitosis. {ECO:0000250|UniProtKB:Q920F3, ECO:0000250|UniProtKB:Q9WU01}. CC -!- SUBUNIT: Self-associates to form homooligomers (By similarity). CC Interacts with KHDRBS1/SAM68; heterooligomer formation of KHDRBS family CC proteins may modulate RNA substrate specificity (By similarity). CC Interacts with RBMX (PubMed:19282290). Interacts with SAFB, SFRS9 and CC YTHDC1. Interacts with FYN and PLCG1 (via SH3 domain). Interacts CC (phosphorylated) with FYN, GRB2, PLCG1 and RASA1 (via SH2 domain) (By CC similarity). {ECO:0000250|UniProtKB:Q920F3, CC ECO:0000250|UniProtKB:Q9WU01, ECO:0000269|PubMed:19282290}. CC -!- INTERACTION: CC Q5VWX1; Q8WTP8: AEN; NbExp=3; IntAct=EBI-742808, EBI-8637627; CC Q5VWX1; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-742808, EBI-742750; CC Q5VWX1; P18075: BMP7; NbExp=3; IntAct=EBI-742808, EBI-1035195; CC Q5VWX1; Q8NEC5: CATSPER1; NbExp=6; IntAct=EBI-742808, EBI-744545; CC Q5VWX1; Q9Y3Y2: CHTOP; NbExp=3; IntAct=EBI-742808, EBI-347794; CC Q5VWX1; Q9Y3Y2-3: CHTOP; NbExp=3; IntAct=EBI-742808, EBI-11984237; CC Q5VWX1; Q14011: CIRBP; NbExp=4; IntAct=EBI-742808, EBI-538850; CC Q5VWX1; Q8NE01: CNNM3; NbExp=3; IntAct=EBI-742808, EBI-741032; CC Q5VWX1; Q5D0E6-2: DALRD3; NbExp=3; IntAct=EBI-742808, EBI-9090939; CC Q5VWX1; Q92608: DOCK2; NbExp=6; IntAct=EBI-742808, EBI-448771; CC Q5VWX1; Q6VB84: FOXD4L3; NbExp=3; IntAct=EBI-742808, EBI-11961494; CC Q5VWX1; P02008: HBZ; NbExp=4; IntAct=EBI-742808, EBI-719843; CC Q5VWX1; Q03014: HHEX; NbExp=3; IntAct=EBI-742808, EBI-747421; CC Q5VWX1; P61978-2: HNRNPK; NbExp=4; IntAct=EBI-742808, EBI-7060731; CC Q5VWX1; O43390: HNRNPR; NbExp=3; IntAct=EBI-742808, EBI-713419; CC Q5VWX1; O75525: KHDRBS3; NbExp=4; IntAct=EBI-742808, EBI-722504; CC Q5VWX1; Q8IXW0: LMNTD2; NbExp=3; IntAct=EBI-742808, EBI-12028858; CC Q5VWX1; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-742808, EBI-739832; CC Q5VWX1; Q13330: MTA1; NbExp=3; IntAct=EBI-742808, EBI-714236; CC Q5VWX1; Q96AH0: NABP1; NbExp=3; IntAct=EBI-742808, EBI-2889252; CC Q5VWX1; Q9NQX5: NPDC1; NbExp=6; IntAct=EBI-742808, EBI-748927; CC Q5VWX1; Q8WWY3: PRPF31; NbExp=8; IntAct=EBI-742808, EBI-1567797; CC Q5VWX1; P79522: PRR3; NbExp=6; IntAct=EBI-742808, EBI-2803328; CC Q5VWX1; Q13882: PTK6; NbExp=4; IntAct=EBI-742808, EBI-1383632; CC Q5VWX1; P98175: RBM10; NbExp=3; IntAct=EBI-742808, EBI-721525; CC Q5VWX1; Q96PK6: RBM14; NbExp=3; IntAct=EBI-742808, EBI-954272; CC Q5VWX1; P98179: RBM3; NbExp=8; IntAct=EBI-742808, EBI-2949699; CC Q5VWX1; P38159: RBMX; NbExp=10; IntAct=EBI-742808, EBI-743526; CC Q5VWX1; P40938: RFC3; NbExp=3; IntAct=EBI-742808, EBI-1055010; CC Q5VWX1; O00560: SDCBP; NbExp=6; IntAct=EBI-742808, EBI-727004; CC Q5VWX1; Q9UQ90: SPG7; NbExp=3; IntAct=EBI-742808, EBI-717201; CC Q5VWX1; P0DMM9: SULT1A3; NbExp=3; IntAct=EBI-742808, EBI-10196922; CC Q5VWX1; P29597: TYK2; NbExp=7; IntAct=EBI-742808, EBI-1383454; CC Q5VWX1; Q8TAI1: TYMSOS; NbExp=3; IntAct=EBI-742808, EBI-742060; CC Q5VWX1; Q96MU7: YTHDC1; NbExp=6; IntAct=EBI-742808, EBI-2849854; CC Q5VWX1; G3V1X1: ZFC3H1; NbExp=3; IntAct=EBI-742808, EBI-6448783; CC Q5VWX1; Q6ZNH5: ZNF497; NbExp=3; IntAct=EBI-742808, EBI-10486136; CC Q5VWX1; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-742808, EBI-745520; CC Q5VWX1; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-742808, EBI-16429014; CC Q5VWX1; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-742808, EBI-11962574; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9WU01}. CC -!- TISSUE SPECIFICITY: Highly expressed in brain, lung, kidney and small CC intestine. Weakly expressed in placenta, liver, spleen, thymus, ovary CC and colon. {ECO:0000269|PubMed:12549823}. CC -!- PTM: Methylated. {ECO:0000269|PubMed:12529443}. CC -!- PTM: Tyrosine phosphorylated by FYN, PTK6 and SRC. Tyrosine CC phosphorylated by SRC during mitosis (By similarity). CC {ECO:0000250|UniProtKB:Q9WU01}. CC -!- SIMILARITY: Belongs to the KHDRBS family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY077838; AAL77219.1; -; mRNA. DR EMBL; AK292043; BAF84732.1; -; mRNA. DR EMBL; AL360220; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL355347; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL391644; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL138882; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL049544; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z93021; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471143; EAW88490.1; -; Genomic_DNA. DR EMBL; BC034043; AAH34043.1; -; mRNA. DR CCDS; CCDS4963.1; -. DR RefSeq; NP_689901.2; NM_152688.3. DR AlphaFoldDB; Q5VWX1; -. DR SMR; Q5VWX1; -. DR BioGRID; 128436; 136. DR IntAct; Q5VWX1; 73. DR MINT; Q5VWX1; -. DR STRING; 9606.ENSP00000281156; -. DR GlyGen; Q5VWX1; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q5VWX1; -. DR PhosphoSitePlus; Q5VWX1; -. DR BioMuta; KHDRBS2; -. DR DMDM; 74762274; -. DR EPD; Q5VWX1; -. DR jPOST; Q5VWX1; -. DR MassIVE; Q5VWX1; -. DR MaxQB; Q5VWX1; -. DR PaxDb; 9606-ENSP00000281156; -. DR PeptideAtlas; Q5VWX1; -. DR ProteomicsDB; 65566; -. DR Antibodypedia; 17553; 169 antibodies from 20 providers. DR DNASU; 202559; -. DR Ensembl; ENST00000281156.5; ENSP00000281156.3; ENSG00000112232.10. DR GeneID; 202559; -. DR KEGG; hsa:202559; -. DR MANE-Select; ENST00000281156.5; ENSP00000281156.3; NM_152688.4; NP_689901.2. DR UCSC; uc003peg.3; human. DR AGR; HGNC:18114; -. DR CTD; 202559; -. DR DisGeNET; 202559; -. DR GeneCards; KHDRBS2; -. DR HGNC; HGNC:18114; KHDRBS2. DR HPA; ENSG00000112232; Tissue enhanced (brain, retina, thyroid gland). DR MIM; 610487; gene. DR neXtProt; NX_Q5VWX1; -. DR OpenTargets; ENSG00000112232; -. DR PharmGKB; PA30093; -. DR VEuPathDB; HostDB:ENSG00000112232; -. DR eggNOG; KOG1588; Eukaryota. DR GeneTree; ENSGT00940000157134; -. DR HOGENOM; CLU_034976_0_1_1; -. DR InParanoid; Q5VWX1; -. DR OMA; PEYYEYG; -. DR PhylomeDB; Q5VWX1; -. DR TreeFam; TF314878; -. DR PathwayCommons; Q5VWX1; -. DR Reactome; R-HSA-8849468; PTK6 Regulates Proteins Involved in RNA Processing. DR SignaLink; Q5VWX1; -. DR BioGRID-ORCS; 202559; 11 hits in 1150 CRISPR screens. DR ChiTaRS; KHDRBS2; human. DR GenomeRNAi; 202559; -. DR Pharos; Q5VWX1; Tbio. DR PRO; PR:Q5VWX1; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q5VWX1; Protein. DR Bgee; ENSG00000112232; Expressed in cortical plate and 83 other cell types or tissues. DR ExpressionAtlas; Q5VWX1; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0008143; F:poly(A) binding; IBA:GO_Central. DR GO; GO:0008266; F:poly(U) RNA binding; IEA:Ensembl. DR GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl. DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central. DR CDD; cd22469; KH-I_KHDRBS2; 1. DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 1. DR InterPro; IPR045071; BBP-like. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR036612; KH_dom_type_1_sf. DR InterPro; IPR032571; Qua1_dom. DR InterPro; IPR032335; Sam68-YY. DR PANTHER; PTHR11208:SF34; KH DOMAIN-CONTAINING, RNA-BINDING, SIGNAL TRANSDUCTION-ASSOCIATED PROTEIN 2; 1. DR PANTHER; PTHR11208; RNA-BINDING PROTEIN RELATED; 1. DR Pfam; PF00013; KH_1; 1. DR Pfam; PF16274; Qua1; 1. DR Pfam; PF16568; Sam68-YY; 1. DR SMART; SM00322; KH; 1. DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1. DR PROSITE; PS50084; KH_TYPE_1; 1. DR Genevisible; Q5VWX1; HS. PE 1: Evidence at protein level; KW Methylation; mRNA processing; Nucleus; Phosphoprotein; Reference proteome; KW RNA-binding; SH3-binding; Transcription; Transcription regulation. FT CHAIN 1..349 FT /note="KH domain-containing, RNA-binding, signal FT transduction-associated protein 2" FT /id="PRO_0000308953" FT DOMAIN 65..135 FT /note="KH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117" FT REGION 182..284 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 319..349 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 206..220 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 230 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q9WU01" FT MOD_RES 240 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q9WU01" FT VARIANT 308 FT /note="G -> A (in dbSNP:rs7449840)" FT /id="VAR_036885" FT CONFLICT 65 FT /note="L -> P (in Ref. 1; AAL77219)" FT /evidence="ECO:0000305" FT CONFLICT 232 FT /note="A -> V (in Ref. 1; AAL77219)" FT /evidence="ECO:0000305" FT CONFLICT 326 FT /note="R -> S (in Ref. 5; AAH34043)" FT /evidence="ECO:0000305" SQ SEQUENCE 349 AA; 38927 MW; EF16E301D8A12164 CRC64; MEEEKYLPEL MAEKDSLDPS FVHASRLLAE EIEKFQGSDG KKEDEEKKYL DVISNKNIKL SERVLIPVKQ YPKFNFVGKL LGPRGNSLKR LQEETGAKMS ILGKGSMRDK AKEEELRKSG EAKYAHLSDE LHVLIEVFAP PGEAYSRMSH ALEEIKKFLV PDYNDEIRQE QLRELSYLNG SEDSGRGRGI RGRGIRIAPT APSRGRGGAI PPPPPPGRGV LTPRGSTVTR GALPVPPVAR GVPTPRARGA PTVPGYRAPP PPAHEAYEEY GYDDGYGGEY DDQTYETYDN SYATQTQSVP EYYDYGHGVS EDAYDSYAPE EWATTRSSLK APPQRSARGG YREHPYGRY //