GEMI5_MOUSE
ID GEMI5_MOUSE Reviewed; 1502 AA.
AC Q8BX17; Q3UPH2;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Gem-associated protein 5;
DE Short=Gemin5;
GN Name=Gemin5;
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;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Liver, 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 [4]
RP FUNCTION.
RX PubMed=25911097; DOI=10.1074/jbc.m115.646257;
RA Workman E., Kalda C., Patel A., Battle D.J.;
RT "Gemin5 binds to the survival motor neuron mRNA to regulate SMN
RT expression.";
RL J. Biol. Chem. 290:15662-15669(2015).
CC -!- FUNCTION: The SMN complex catalyzes the assembly of small nuclear
CC ribonucleoproteins (snRNPs), the building blocks of the spliceosome,
CC and thereby plays an important role in the splicing of cellular pre-
CC mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins
CC SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in
CC a heptameric protein ring on the Sm site of the small nuclear RNA to
CC form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1,
CC SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm
CC complex by the chaperone CLNS1A that controls the assembly of the core
CC snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm
CC proteins from CLNS1A forming an intermediate. Binding of snRNA inside
CC 5Sm ultimately triggers eviction of the SMN complex, thereby allowing
CC binding of SNRPD3 and SNRPB to complete assembly of the core snRNP.
CC Within the SMN complex, GEMIN5 recognizes and delivers the small
CC nuclear RNAs (snRNAs) to the SMN complex. Binds to the 7-
CC methylguanosine cap of RNA molecules (By similarity). Binds to the 3'-
CC UTR of SMN1 mRNA and regulates its translation; does not affect mRNA
CC stability (PubMed:25911097). May play a role in the regulation of
CC protein synthesis via its interaction with ribosomes (By similarity).
CC {ECO:0000250|UniProtKB:Q8TEQ6, ECO:0000269|PubMed:25911097}.
CC -!- SUBUNIT: Part of the core SMN complex that contains SMN1, GEMIN2/SIP1,
CC DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP.
CC Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1,
CC DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and
CC the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG.
CC Interacts directly with SMN1, SNRPB, SNRPD1, SNRPD2, SNRPD3 and SNRPE.
CC Identified in a SMN complex that contains GEMIN2/SIP1. Interacts with
CC cytosolic DDX20/GEMIN3 and GEMIN4. Interacts with SNRNP70 and HNRNPU.
CC Identified in a complex with 80S ribosomes; binds to the 60S large
CC ribosomal subunit. Interacts with the ribosomal subunits RPL3 and RPL4.
CC {ECO:0000250|UniProtKB:Q8TEQ6}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q8TEQ6}. Nucleus, gem
CC {ECO:0000250|UniProtKB:Q8TEQ6}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8TEQ6}. Note=Found both in the nucleoplasm and
CC in nuclear bodies called gems (Gemini of Cajal bodies) that are often
CC in proximity to Cajal (coiled) bodies. Also found in the cytoplasm.
CC {ECO:0000250|UniProtKB:Q8TEQ6}.
CC -!- DOMAIN: The WD repeat domain mediates binding to U1 snRNA and to U4
CC snRNA. The WD repeat domain also mediates binding to the 7-
CC methylguanosine cap that is found both on mRNA and snRNA molecules. The
CC regions that bind snRNA molecules and the isolated 7-methylguanosine
CC cap overlap at least partially. Besides, the WD repeat domain mediates
CC interaction with the 60S large ribosomal subunit.
CC {ECO:0000250|UniProtKB:Q8TEQ6}.
CC -!- SIMILARITY: Belongs to the WD repeat gemin-5 family. {ECO:0000305}.
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DR EMBL; AK049216; BAC33614.1; -; mRNA.
DR EMBL; AK143536; BAE25423.1; -; mRNA.
DR EMBL; AL672182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS24723.1; -.
DR RefSeq; NP_001160141.1; NM_001166669.1.
DR RefSeq; NP_001160142.1; NM_001166670.1.
DR RefSeq; NP_001160143.1; NM_001166671.1.
DR RefSeq; NP_766146.2; NM_172558.3.
DR AlphaFoldDB; Q8BX17; -.
DR SMR; Q8BX17; -.
DR BioGRID; 229781; 3.
DR IntAct; Q8BX17; 6.
DR MINT; Q8BX17; -.
DR STRING; 10090.ENSMUSP00000036603; -.
DR iPTMnet; Q8BX17; -.
DR PhosphoSitePlus; Q8BX17; -.
DR EPD; Q8BX17; -.
DR jPOST; Q8BX17; -.
DR MaxQB; Q8BX17; -.
DR PaxDb; Q8BX17; -.
DR PeptideAtlas; Q8BX17; -.
DR PRIDE; Q8BX17; -.
DR ProteomicsDB; 263351; -.
DR Antibodypedia; 28334; 76 antibodies from 17 providers.
DR DNASU; 216766; -.
DR Ensembl; ENSMUST00000035604; ENSMUSP00000036603; ENSMUSG00000037275.
DR GeneID; 216766; -.
DR KEGG; mmu:216766; -.
DR UCSC; uc007jan.2; mouse.
DR CTD; 25929; -.
DR MGI; MGI:2449311; Gemin5.
DR VEuPathDB; HostDB:ENSMUSG00000037275; -.
DR eggNOG; ENOG502QPYZ; Eukaryota.
DR GeneTree; ENSGT00620000088064; -.
DR InParanoid; Q8BX17; -.
DR OMA; YWFNRND; -.
DR OrthoDB; 283127at2759; -.
DR TreeFam; TF328886; -.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR BioGRID-ORCS; 216766; 12 hits in 41 CRISPR screens.
DR ChiTaRS; Gemin5; mouse.
DR PRO; PR:Q8BX17; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BX17; protein.
DR Bgee; ENSMUSG00000037275; Expressed in spermatocyte and 198 other tissues.
DR ExpressionAtlas; Q8BX17; baseline and differential.
DR Genevisible; Q8BX17; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0097504; C:Gemini of coiled bodies; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032797; C:SMN complex; ISS:UniProtKB.
DR GO; GO:0034718; C:SMN-Gemin2 complex; ISS:UniProtKB.
DR GO; GO:0034719; C:SMN-Sm protein complex; ISS:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:UniProtKB.
DR GO; GO:0043022; F:ribosome binding; ISS:UniProtKB.
DR GO; GO:0000340; F:RNA 7-methylguanosine cap binding; ISS:UniProtKB.
DR GO; GO:0017069; F:snRNA binding; ISS:UniProtKB.
DR GO; GO:0030619; F:U1 snRNA binding; ISS:UniProtKB.
DR GO; GO:0030621; F:U4 snRNA binding; ISS:UniProtKB.
DR GO; GO:0030622; F:U4atac snRNA binding; ISO:MGI.
DR GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR024977; Apc4_WD40_dom.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12894; ANAPC4_WD40; 3.
DR Pfam; PF00400; WD40; 2.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 13.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Phosphoprotein; Protein biosynthesis; Reference proteome; Repeat;
KW RNA-binding; Translation regulation; Ubl conjugation; WD repeat.
FT CHAIN 1..1502
FT /note="Gem-associated protein 5"
FT /id="PRO_0000051005"
FT REPEAT 62..104
FT /note="WD 1"
FT REPEAT 107..148
FT /note="WD 2"
FT REPEAT 150..189
FT /note="WD 3"
FT REPEAT 193..264
FT /note="WD 4"
FT REPEAT 280..321
FT /note="WD 5"
FT REPEAT 333..374
FT /note="WD 6"
FT REPEAT 377..417
FT /note="WD 7"
FT REPEAT 424..464
FT /note="WD 8"
FT REPEAT 468..509
FT /note="WD 9"
FT REPEAT 533..573
FT /note="WD 10"
FT REPEAT 576..622
FT /note="WD 11"
FT REPEAT 637..677
FT /note="WD 12"
FT REPEAT 680..720
FT /note="WD 13"
FT REGION 1..124
FT /note="Important for interaction with U1 snRNA"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT REGION 13..15
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT REGION 740..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1309..1338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1378..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1355..1382
FT /evidence="ECO:0000255"
FT SITE 33
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT SITE 284
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT SITE 335
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT SITE 359
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT SITE 381
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT SITE 422
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT SITE 426
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT SITE 470
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT SITE 474
FT /note="Interaction with U4 snRNA and with the 7-
FT methylguanosine cap of RNA molecules"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT SITE 556
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT SITE 579
FT /note="Interaction with U4 snRNA"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT SITE 641
FT /note="Interaction with U4 snRNA and with the 7-
FT methylguanosine cap of RNA molecules"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT SITE 660
FT /note="Interaction with U4 snRNA and with the 7-
FT methylguanosine cap of RNA molecules"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT SITE 684
FT /note="Interaction with U4 snRNA and with the 7-
FT methylguanosine cap of RNA molecules"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT MOD_RES 624
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT MOD_RES 770
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT CROSSLNK 754
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8TEQ6"
FT CONFLICT 1236
FT /note="T -> A (in Ref. 1; BAC33614)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1502 AA; 166592 MW; B3F9889CA20E2271 CRC64;
MKPEPRTLPP SPNWYCSRCS DAAPGGIFGF AARTSVFLVR VGPGAGASPG APPFRVVGEL
VGHTERVSGF TFSHHPGQYN LCATSSDDGT VKVWDVETKT VVTEHTLHQH TISALHWSPT
VKDLIVSGDE KGVVFCYWLN RNDSQHLFTE PRTIFCLTCS PHHENLVAIG YKDGIVVIID
ISKKGEVIHR LRGHDDEIHS IAWCPLSGED CLSISQEENS EEPDIPNGKL IAETPITKGC
YLATGSKDQT IRIWSCSRGR GVMVLKLPFL KRRSGGVDPT VKERLWLTLH WPKNQPTQLV
SSCFGGELLL WDLTQSWRRK YTLFSTSAEG HNHSRIVFNL CSLKTEDGKQ LLLSTSMDRD
VKCWDMATLE CCWTLPSLGG FAYSLAFSPV DVGSLAIGVG DGMIRVWNTL SIKNNYDVKN
FWQGVKSKVT ALCWHPNKEG CLAFGTDDGK VGLYDTCSNK PPQISSTYHK KTVYRLAWGP
PVPPMSLGGE GDRPSLTLYS CGGEGVVLQH NPWKLSGEAF DINKLVRDTN SIRYKLPVHT
EISWKGDGKV LALGNEDGSI EIFQVPNLRL LCTIQQHHKL VNAIVWHHEH GSRPELSCLL
ASGSNNAVIY VHNLKAVLES NPESPITITE PYRTLSGHTA KITSLAWSPH HDGRLVSACY
DGTAQVWDAL REEPLFNFRG HRGRLLCVAW SPVDPECIYS GADDFCVYRW LTSMQDHSRP
PQGKKCIELE KKRLSQFKPK LKKKKKPTLR LPVKQDSSVG NEDESVKENS GPAENGLSDQ
DGEEEAQEPE LPPSPVVCVE PVSCTDICSG FEKSKVTVSS KATSLKKEPA KEKPEALLKK
RKARSMLPLS TSLDHRSKEE LHRDCLVLAT ATHAKAELNE DVSADLEERF HLGLFTDRAT
LYRMMETEGK GHLESGHPEL FHQLMLWKGD LKGVLQAAAE RGELTDSLVA VAPVAGYSVW
LWAVEAFAKQ LCFQDQYVKA ASYLLSIHKV YEAVELLKSN HLYREAIAVA KARLRPEDPV
LKELYLSWGS ILERDGHYAI AAKCYLGATS AYDAAKVLAR KGDAASLRTA AELAAIAGEH
ELAASLALRC AQELLLMKNW VGAQEALGLH ESLQGQRLVF CLLELLCRHL EEKQPLEVRG
PSSIYHQWAT GSEGTLVQRV TGVWRSAFSV DTPEQCQAAL QKLQDVKYPS ATSNTPFRQL
LLHVCHDLTL AMLSQQAAAW EEAVPALLQA VVRSYTSGNF TLMQEIYSAF LPGGCDHLRD
KLGDLSPAMA AYKSLEAFCI YGQLYEVWWS LCGPGPESSV WVLSAESTVS DKQSKPEDSA
SAEDMEQPPG PGPRLSAESE RLLSACKELF SERHASLQTS QRTVAEVQET LAEMIRQHQK
SQLCKATTNG PSRDEPSRDE PSQEAERAPS QPPSPTEERN APVSLPELTR RLTEANERIA
EFPESVKAWP FPDVLECCLV LLHIGSQCPD AVDPEMQQQA QELLHKYGHT RAYRRHCQSR
HT
