AFF4_MOUSE
ID AFF4_MOUSE Reviewed; 1160 AA.
AC Q9ESC8; B2RST9; Q8C6K4; Q8C6W3; Q8CCH3;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=AF4/FMR2 family member 4;
GN Name=Aff4; Synonyms=Alf4;
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 [MRNA].
RC STRAIN=NIH Black Swiss;
RX PubMed=10704283; DOI=10.1006/geno.1999.6100;
RA Wenderfer S.E., Slack J.P., McCluskey T.S., Monaco J.J.;
RT "Identification of 40 genes on a 1-Mb contig around the IL-4 cytokine
RT family gene cluster on mouse chromosome 11.";
RL Genomics 63:354-373(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, Ovary, 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 [3]
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 [4]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=16024815; DOI=10.1128/mcb.25.15.6834-6845.2005;
RA Urano A., Endoh M., Wada T., Morikawa Y., Itoh M., Kataoka Y., Taki T.,
RA Akazawa H., Nakajima H., Komuro I., Yoshida N., Hayashi Y., Handa H.,
RA Kitamura T., Nosaka T.;
RT "Infertility with defective spermiogenesis in mice lacking AF5q31, the
RT target of chromosomal translocation in human infant leukemia.";
RL Mol. Cell. Biol. 25:6834-6845(2005).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482; SER-485; SER-486;
RP SER-689; SER-698; SER-701; SER-809 AND SER-1040, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Pancreas, 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 SUBCELLULAR LOCATION.
RX PubMed=22195968; DOI=10.1016/j.molcel.2011.12.008;
RA Smith E.R., Lin C., Garrett A.S., Thornton J., Mohaghegh N., Hu D.,
RA Jackson J., Saraf A., Swanson S.K., Seidel C., Florens L., Washburn M.P.,
RA Eissenberg J.C., Shilatifard A.;
RT "The little elongation complex regulates small nuclear RNA transcription.";
RL Mol. Cell 44:954-965(2011).
RN [7]
RP INTERACTION WITH ELL3.
RX PubMed=23273992; DOI=10.1016/j.cell.2012.12.015;
RA Lin C., Garruss A.S., Luo Z., Guo F., Shilatifard A.;
RT "The RNA Pol II elongation factor Ell3 marks enhancers in ES cells and
RT primes future gene activation.";
RL Cell 152:144-156(2013).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-817, 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).
CC -!- FUNCTION: Key component of the super elongation complex (SEC), a
CC complex required to increase the catalytic rate of RNA polymerase II
CC transcription by suppressing transient pausing by the polymerase at
CC multiple sites along the DNA. In the SEC complex, AFF4 acts as a
CC central scaffold that recruits other factors through direct
CC interactions with ELL proteins (ELL, ELL2 or ELL3) and the P-TEFb
CC complex. In case of infection by HIV-1 virus, the SEC complex is
CC recruited by the viral Tat protein to stimulate viral gene expression
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the super elongation complex (SEC), at least
CC composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb
CC complex and ELL (ELL, ELL2 or ELL3). Interacts with ELL2; the
CC interaction is direct and leads to stabilize ELL2 and prevent ELL2
CC ubiquitination and degradation (By similarity). Interacts with ELL3;
CC the interaction is direct. {ECO:0000250, ECO:0000269|PubMed:23273992}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22195968}.
CC Note=Associates to transcriptionally active chromatin but not at snRNA
CC genes.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis by Sertoli cells, and at
CC low levels in other tissues. {ECO:0000269|PubMed:16024815}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout embryogenesis with maximum
CC expression at 10.5 and 12.5 dpc. {ECO:0000269|PubMed:16024815}.
CC -!- DISRUPTION PHENOTYPE: Mice are infertile with azoospermia.
CC Spermatogenesis is arrested at the level of spermiogenesis.
CC {ECO:0000269|PubMed:16024815}.
CC -!- SIMILARITY: Belongs to the AF4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC28178.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC35763.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF190449; AAG17126.1; -; mRNA.
DR EMBL; AK033163; BAC28178.1; ALT_FRAME; mRNA.
DR EMBL; AK053034; BAC35244.1; -; mRNA.
DR EMBL; AK054401; BAC35763.1; ALT_FRAME; mRNA.
DR EMBL; BC138999; AAI39000.1; -; mRNA.
DR CCDS; CCDS24676.1; -.
DR RefSeq; NP_291043.1; NM_033565.2.
DR RefSeq; XP_011247633.1; XM_011249331.2.
DR AlphaFoldDB; Q9ESC8; -.
DR SMR; Q9ESC8; -.
DR BioGRID; 220280; 2.
DR IntAct; Q9ESC8; 2.
DR STRING; 10090.ENSMUSP00000051479; -.
DR iPTMnet; Q9ESC8; -.
DR PhosphoSitePlus; Q9ESC8; -.
DR EPD; Q9ESC8; -.
DR jPOST; Q9ESC8; -.
DR MaxQB; Q9ESC8; -.
DR PaxDb; Q9ESC8; -.
DR PRIDE; Q9ESC8; -.
DR ProteomicsDB; 285769; -.
DR Antibodypedia; 14555; 267 antibodies from 31 providers.
DR DNASU; 93736; -.
DR Ensembl; ENSMUST00000060945; ENSMUSP00000051479; ENSMUSG00000049470.
DR GeneID; 93736; -.
DR KEGG; mmu:93736; -.
DR UCSC; uc007ivu.2; mouse.
DR CTD; 27125; -.
DR MGI; MGI:2136171; Aff4.
DR VEuPathDB; HostDB:ENSMUSG00000049470; -.
DR eggNOG; ENOG502QR32; Eukaryota.
DR GeneTree; ENSGT00950000182974; -.
DR HOGENOM; CLU_006484_0_0_1; -.
DR InParanoid; Q9ESC8; -.
DR OMA; SYSADHY; -.
DR OrthoDB; 558558at2759; -.
DR PhylomeDB; Q9ESC8; -.
DR TreeFam; TF326216; -.
DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation.
DR BioGRID-ORCS; 93736; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Aff4; mouse.
DR PRO; PR:Q9ESC8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9ESC8; protein.
DR Bgee; ENSMUSG00000049470; Expressed in undifferentiated genital tubercle and 256 other tissues.
DR ExpressionAtlas; Q9ESC8; baseline and differential.
DR Genevisible; Q9ESC8; MM.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032783; C:super elongation complex; IBA:GO_Central.
DR GO; GO:0008023; C:transcription elongation factor complex; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR InterPro; IPR007797; AF4/FMR2.
DR InterPro; IPR043640; AF4/FMR2_CHD.
DR InterPro; IPR043639; AF4_int.
DR PANTHER; PTHR10528; PTHR10528; 1.
DR Pfam; PF18876; AF-4_C; 1.
DR Pfam; PF18875; AF4_int; 1.
PE 1: Evidence at protein level;
KW Acetylation; Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..1160
FT /note="AF4/FMR2 family member 4"
FT /id="PRO_0000239394"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1031..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB7"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB7"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB7"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB7"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB7"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB7"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 485
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB7"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB7"
FT MOD_RES 669
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB7"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB7"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 698
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 707
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB7"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 817
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 831
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB7"
FT MOD_RES 1040
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1052
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB7"
FT MOD_RES 1055
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB7"
FT MOD_RES 1059
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB7"
FT CROSSLNK 578
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UHB7"
FT CONFLICT 932
FT /note="R -> S (in Ref. 2; BAC28178)"
FT /evidence="ECO:0000305"
FT CONFLICT 980
FT /note="L -> Q (in Ref. 2; BAC28178)"
FT /evidence="ECO:0000305"
FT CONFLICT 1088
FT /note="Q -> K (in Ref. 2; BAC28178)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1160 AA; 126639 MW; 0C13253EAC9192B3 CRC64;
MNREDRNVLR MKERERRNQE IQQGEDAFPP SSPLFAEPYK VTSKEDKLSS RIQSMLGNYD
EMKDYIGDRS IPKLVAIPKP AVPTTTDEKA NPNFFEQRHG GSHQSSKWTP VGPAPSTSQS
QKRSSALQSG HSSQRSGAGG SGASSSGQRH DRDSYSSSRK KGQHGSEHSK SRSSSPGKPQ
AVSSLSSSHS RSHGNDHHSK EHQRSKSPRD PDANWDSPSR GPFSSGQHSS QSFPPSLMSK
SSSMLQKPTA YVRPMDGQES VEPKLSSEHY SSQSHGNSMT ELKPSSKAHL TKLKIPSRPL
DASVSGDVSC VDEILKEMTH SWPPPLTAIH TPCKTEPSKF PFPTKESQQS NFGPGEQKRY
STAKTSNGHQ SKSMLKDDLK LSSSEDSDGE QDCDKTMPRS TPGSNSEPSH HNSEGADNSR
DDSSSHSGSE SSSGSDSESE SSSSDSEANE PSQSASPEPE PPPTNKWQLD NWLNKVNPHK
VSPASSVDSN IPSSQAYKKE GREQGTASNY TDPGGTKETS SATPGRDSKT IQKGSESGRG
RQKSPAQSDS TTQRRTVGKK QPKKPEKSAA EEPRGGLKIE SETPVDMAAS MPSSRHKAAT
KGSRKPNIKK ESKSSPRPTA EKKKYKSASK PSQKSREIIE TDTSSSDSDG SESLPPSSQT
PKYPESNRTP VKPSSVEEED SFFRQRMFSP MEEKELLSPL SEPDDRYPLI VKIDLNLLTR
IPGKPYKETE PPKGEKKNVP EKHSREVQKQ ASEKASNKGK RKHKNDDDTR ASESKKPKTE
DKNSSGHKPS SSRESSKQSS TKEKDLLPSP AGPILSKDSK TEHGSRKRTV SQSSSLKSSG
TSSKENSGSS SKSSSSSTAK QKKTEGKGPS SSKEAKEKAP NSSSNCPPST PTSESSKPRR
TKLAFDDRNY SADHYLQEAK KLKHNADALS DRFEKAVYYL DAVVSFIECG NALEKNAQES
KSPFPMYSDT VELIKYTMKL KNYLAPDATA ADKRLTVLCL RCQSLLYLRL FKLKKENALK
YSKTLTEHLK NSYSNSQAPS PGLGSKAVGM PSPVSPKLSP GNSGSYSSGG SSASASGSSV
TIPQKIHQMA ASYVQVTSNF LYATEIWDQA EQLSKEQKEF FAELDKVMGP LIFNASIMTD
LARYTRQGLH WLRQDAKLIS
