SPEF2_MOUSE
ID SPEF2_MOUSE Reviewed; 1724 AA.
AC Q8C9J3; A2RSG5; E0CYG3; G0Z098;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 3.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Sperm flagellar protein 2;
DE AltName: Full=Protein KPL2;
GN Name=Spef2; Synonyms=Kpl2;
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] (ISOFORM 4), AND FUNCTION.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AEA11026.1};
RC TISSUE=Testis {ECO:0000312|EMBL:AEA11026.1};
RX PubMed=21715716; DOI=10.1095/biolreprod.111.091132;
RA Sironen A., Kotaja N., Mulhern H., Wyatt T.A., Sisson J.H., Pavlik J.A.,
RA Miiluniemi M., Fleming M.D., Lee L.;
RT "Loss of SPEF2 function in mice results in spermatogenesis defects and
RT primary ciliary dyskinesia.";
RL Biol. Reprod. 85:690-701(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [5]
RP INTERACTION WITH IFT20, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND ALTERNATIVE SPLICING.
RX PubMed=19889948; DOI=10.1095/biolreprod.108.074971;
RA Sironen A., Hansen J., Thomsen B., Andersson M., Vilkki J., Toppari J.,
RA Kotaja N.;
RT "Expression of SPEF2 during mouse spermatogenesis and identification of
RT IFT20 as an interacting protein.";
RL Biol. Reprod. 82:580-590(2010).
RN [6]
RP FUNCTION, INTERACTION WITH DYNC1I2, AND SUBCELLULAR LOCATION.
RX PubMed=28619825; DOI=10.1242/dev.152108;
RA Lehti M.S., Zhang F.P., Kotaja N., Sironen A.;
RT "SPEF2 functions in microtubule-mediated transport in elongating spermatids
RT to ensure proper male germ cell differentiation.";
RL Development 144:2683-2693(2017).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=29339787; DOI=10.1038/s41598-018-19204-5;
RA Lehti M.S., Henriksson H., Rummukainen P., Wang F., Uusitalo-Kylmaelae L.,
RA Kiviranta R., Heino T.J., Kotaja N., Sironen A.;
RT "Cilia-related protein SPEF2 regulates osteoblast differentiation.";
RL Sci. Rep. 8:859-859(2018).
CC -!- FUNCTION: Required for correct axoneme development in spermatozoa
CC (PubMed:21715716, PubMed:28619825). Important for normal development of
CC the manchette and sperm head morphology (PubMed:28619825). Essential
CC for male fertility (PubMed:21715716, PubMed:28619825). Plays a role in
CC localization of the intraflagellar transport protein IFT20 to the
CC manchette, suggesting function as an adapter for dynein-mediated
CC protein transport during spermatogenesis. Also plays a role in bone
CC growth where it seems to be required for normal osteoblast
CC differentiation (PubMed:28619825). {ECO:0000269|PubMed:21715716,
CC ECO:0000269|PubMed:28619825}.
CC -!- SUBUNIT: Interacts (via C-terminus) with IFT20 (PubMed:19889948).
CC Interacts with DYNC1I2 (PubMed:28619825). {ECO:0000269|PubMed:19889948,
CC ECO:0000269|PubMed:28619825}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum
CC {ECO:0000250|UniProtKB:Q9C093}. Cytoplasm
CC {ECO:0000269|PubMed:19889948}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19889948, ECO:0000269|PubMed:28619825}. Golgi
CC apparatus {ECO:0000269|PubMed:19889948}. Note=Shows dynamic
CC localization in developing spermatozoa (PubMed:19889948). Localizes to
CC the manchette in step 10-12 elongating spermatids, where it is mainly
CC found on the basal side below the perinuclear ring (PubMed:19889948,
CC PubMed:28619825). Detected in the basal body and neck area of step 13-
CC 14 spermatids (PubMed:19889948). Localizes to the midpiece of the sperm
CC tail in step 15-16 spermatids (PubMed:19889948). During the epididymal
CC transport of spermatozoa, expression in the sperm tail reduces and
CC becomes concentrated at the distal part of the midpiece
CC (PubMed:19889948). Detected in the Golgi apparatus of late
CC spermatocytes and round spermatids (PubMed:19889948). Detected in the
CC cytoplasm of Sertoli cells (PubMed:19889948).
CC {ECO:0000269|PubMed:19889948, ECO:0000269|PubMed:28619825}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=A number of isoforms are produced.
CC {ECO:0000269|PubMed:19889948};
CC Name=1;
CC IsoId=Q8C9J3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C9J3-2; Sequence=VSP_027528, VSP_027529;
CC Name=3;
CC IsoId=Q8C9J3-3; Sequence=VSP_027526, VSP_027527;
CC Name=4;
CC IsoId=Q8C9J3-4; Sequence=VSP_059848, VSP_059849;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis, where it primarily
CC localizes to late spermatocytes, round spermatids and elongating
CC spermatids (at protein level) (PubMed:19889948, PubMed:29339787). Found
CC in Sertoli cells of the testis (at protein level) (PubMed:19889948).
CC Expressed at lower levels in epididymis (at protein level)
CC (PubMed:19889948, PubMed:29339787). Detected in lung, brain, liver and
CC kidney (PubMed:19889948, PubMed:29339787). Also detected in bone,
CC cartilage, trachea, pituitary gland and eye (PubMed:29339787).
CC Expressed in osteoblasts and chondrocytes (PubMed:29339787).
CC {ECO:0000269|PubMed:19889948, ECO:0000269|PubMed:29339787}.
CC -!- DEVELOPMENTAL STAGE: Shows increasing expression levels in testis
CC during postnatal stages, reaching highest levels by postnatal day 50.
CC In testis, first detected in pachytene spermatocytes (stage VII),
CC reaching peak expression in meitotically dividing spermatocytes (stage
CC XII). {ECO:0000269|PubMed:19889948}.
CC -!- DISRUPTION PHENOTYPE: Lethality occurs at approximately 3 weeks of age,
CC accompanied by severe hydrocephaly. Weight at birth is similar to wild
CC type but subsequently there is significant growth retardation. Bone
CC mineralization is reduced in the vertebral column and hindlimbs,
CC associated with decreased bone strength. Bone length and skull
CC thickness is also slightly reduced. Trabecular bone density is reduced,
CC along with reduced trabecular number and increased open porosity.
CC Expression of the osteoblast marker genes RUNX2, BGLAP/OCN and
CC COL1A1/COL1 is reduced in bone tissue. Expression of SP7/OSX and ALPL
CC is also reduced in cultured calvarial osteoblasts. Osteoclast
CC differentiation does not appear to be affected. No obvious effects on
CC cilia length or axonemal structure. {ECO:0000269|PubMed:29339787}.
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DR EMBL; HQ856050; AEA11026.1; -; mRNA.
DR EMBL; AK041992; BAC31126.1; -; mRNA.
DR EMBL; AC133586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC133959; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC132098; AAI32099.1; -; mRNA.
DR EMBL; BC132288; AAI32289.1; -; mRNA.
DR CCDS; CCDS37041.1; -. [Q8C9J3-2]
DR CCDS; CCDS84163.1; -. [Q8C9J3-3]
DR RefSeq; NP_001291971.1; NM_001305042.1. [Q8C9J3-4]
DR RefSeq; NP_001291973.1; NM_001305044.1. [Q8C9J3-3]
DR RefSeq; NP_796097.2; NM_177123.4. [Q8C9J3-2]
DR AlphaFoldDB; Q8C9J3; -.
DR BioGRID; 235900; 5.
DR IntAct; Q8C9J3; 1.
DR STRING; 10090.ENSMUSP00000035762; -.
DR iPTMnet; Q8C9J3; -.
DR PhosphoSitePlus; Q8C9J3; -.
DR jPOST; Q8C9J3; -.
DR MaxQB; Q8C9J3; -.
DR PaxDb; Q8C9J3; -.
DR PRIDE; Q8C9J3; -.
DR ProteomicsDB; 257344; -. [Q8C9J3-1]
DR ProteomicsDB; 257345; -. [Q8C9J3-2]
DR ProteomicsDB; 257346; -. [Q8C9J3-3]
DR ProteomicsDB; 310131; -.
DR Antibodypedia; 22874; 51 antibodies from 12 providers.
DR Ensembl; ENSMUST00000041840; ENSMUSP00000035762; ENSMUSG00000072663. [Q8C9J3-2]
DR Ensembl; ENSMUST00000159368; ENSMUSP00000124723; ENSMUSG00000072663. [Q8C9J3-3]
DR Ensembl; ENSMUST00000160236; ENSMUSP00000124222; ENSMUSG00000072663. [Q8C9J3-1]
DR GeneID; 320277; -.
DR KEGG; mmu:320277; -.
DR UCSC; uc007vfq.2; mouse. [Q8C9J3-2]
DR UCSC; uc007vfr.2; mouse. [Q8C9J3-3]
DR CTD; 79925; -.
DR MGI; MGI:2443727; Spef2.
DR VEuPathDB; HostDB:ENSMUSG00000072663; -.
DR eggNOG; ENOG502QR7Y; Eukaryota.
DR GeneTree; ENSGT00390000008160; -.
DR HOGENOM; CLU_002424_1_0_1; -.
DR InParanoid; Q8C9J3; -.
DR OMA; LWDICDN; -.
DR OrthoDB; 81320at2759; -.
DR PhylomeDB; Q8C9J3; -.
DR TreeFam; TF329522; -.
DR BioGRID-ORCS; 320277; 3 hits in 58 CRISPR screens.
DR ChiTaRS; Spef2; mouse.
DR PRO; PR:Q8C9J3; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8C9J3; protein.
DR Bgee; ENSMUSG00000072663; Expressed in olfactory epithelium and 36 other tissues.
DR ExpressionAtlas; Q8C9J3; baseline and differential.
DR Genevisible; Q8C9J3; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:GOC.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0002177; C:manchette; IDA:MGI.
DR GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
DR GO; GO:0097225; C:sperm midpiece; IDA:MGI.
DR GO; GO:0048854; P:brain morphogenesis; IMP:MGI.
DR GO; GO:0090660; P:cerebrospinal fluid circulation; IGI:MGI.
DR GO; GO:0003351; P:epithelial cilium movement involved in extracellular fluid movement; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IGI:MGI.
DR GO; GO:0120197; P:mucociliary clearance; IMP:MGI.
DR GO; GO:0060541; P:respiratory system development; IMP:MGI.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0007288; P:sperm axoneme assembly; IMP:MGI.
DR GO; GO:0120316; P:sperm flagellum assembly; IGI:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR010441; CH_2.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF06294; CH_2; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium; Coiled coil; Cytoplasm;
KW Cytoskeleton; Differentiation; Flagellum; Golgi apparatus;
KW Reference proteome; Spermatogenesis.
FT CHAIN 1..1724
FT /note="Sperm flagellar protein 2"
FT /id="PRO_0000299030"
FT DOMAIN 1..105
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 545..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1177..1241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1580
FT /note="Interaction with IFT20"
FT /evidence="ECO:0000250|UniProtKB:Q9C093"
FT REGION 1580..1618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1704..1724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..203
FT /evidence="ECO:0000255"
FT COILED 255..351
FT /evidence="ECO:0000255"
FT COILED 665..691
FT /evidence="ECO:0000255"
FT COILED 995..1021
FT /evidence="ECO:0000255"
FT COMPBIAS 551..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1588..1617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1707..1724
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 138
FT /note="E -> ERLKNLIPRQTDFNLMRVTCRFQEKCKQMKEDLARMNFEKFEKIQKL
FT EEEQRHFNIEK (in isoform 4)"
FT /id="VSP_059848"
FT VAR_SEQ 452..456
FT /note="NMVGE -> VHTNM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027526"
FT VAR_SEQ 457..1724
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_027527"
FT VAR_SEQ 873..875
FT /note="SVS -> SGD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027528"
FT VAR_SEQ 873
FT /note="S -> SETQHGKQESQPEGKGKK (in isoform 4)"
FT /id="VSP_059849"
FT VAR_SEQ 876..1724
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027529"
FT CONFLICT 1146
FT /note="A -> T (in Ref. 1; AEA11026)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1724 AA; 197972 MW; 9AB4F1737BD770C1 CRC64;
MSEILCQWLN QELRVSRTVS PKSFAKAFSN GYLIGEVLFK FELQSDFAEF SESRGSTAKL
NNFSRLQPTL HLLGLQFDQN VAQSIITEKP GAATKLLYQL YIALQKKKKT GLTGLEIQTM
QPQTNLRLQT LKSEAFREQR LNRRRQNEIM AKIQAAIIQI PKPESNRTLK AIEAQKLMKK
KKEAEDVANE IKKFEALIKK DLQIKESVSK TSLETTDQTT AELLNTYSDD DYIKKIQKRL
EEDAFAREQR EKRRRRLLMD QLMAHEAQEE AYREEQLIHR LMRQSQQERR IAVQLMHVRH
EKEVLWQNRI FREKQFEERR LKDFQDALDR EAALAKQAKI DFAEQTLREK EIHEKISVER
AQQRYKKHYG ICAEILDQML DLCTKVADYR LLTNNLIPHK MMHDWKELFF SGIPIYEQTS
LTHGQTEPTE DHRAEVKKRN LLDSKDYEDY KNMVGEWALP EDMVNSSPPS NNSILGHVLL
RLIEKADPSA SNAEATELPS LAVKGCILGK TLSGKTTVLK SLQNDFPVHV LSIDTLVQEA
IQAFHERQKS GKTPPTQEDD KRDPVVNQEK VSKTQDKNVL AVSPVPGDRT SQKEGVKINE
FEQFRSSDSF LSLSMRAQLG AKSELMLRRG KSIPDILLVS ILVNAIKEIP VDQSWVLDGF
PITLNQAKLL EEALTGYKRK FLQLKKKKEQ MPTLALDPST STEVSLLPSA LDFVILLDIS
DNSSLARTND IIAKEISHEI SHENVGRPGT GTSQDNKSED RNLRDHIQHR IVGFLDNWPL
LEEWFTQPKN ILTKVNAEID EALLCQKVKE IFATETVNKK IKVEKTLEEK ETEKKAGAPP
AEPPAMSPPL SSEAEKDKEL HQAKTPGKGK TQSVSPKGKA QGGKVSVKKS PVGSAEVSPT
PTAPPPPKAG TEEWVYVNEP IPEELPSFLV PYWELIEKSY INHIKTVLRH LRERQHNVLS
YLYETRTSFQ EFLRRPDHKQ DFVSQWQADF NSVPEDLWED EETKAELHQR VNDLRDRLWD
ICEARKEEAE QERLDIINES WLQDSIGITM NHFFSLMQAE VNRFQDTKRL LQDYYRAMES
KIPLEDSKKF TRVPLVQLDG KEISESQLRI PLVPRISNSP ENSAVKPKVG TFLKGRSDPP
LEVLEANFEI DEKILLDTWQ QASLAISNMV AAEVHQRLTE EEKEPPQLDS KEKSPQSGAN
KKAKKEKEAP KKKKTDKKGK GKSSPVAEVS PVTVTPEEMA EMEKRNELRL RIKEEHLAAL
QTEEQAAQFR LELIKLKALS VLEDLVTKVI DVYRLMEKWL GKRYLNEMAS IQKLTELARY
HIETATKIQN EIYLSQEDFY INGDIKVFPD PSPPTRPPPV EREENGTLTI EQLDNLRDQF
LDMAPKGIIG NKAFSDILLD LITLNLGTNN FPSSWMHLSQ LDLQEITSLL TVNTEFVDWR
KFLMVTAMPW PMALEDELLD TLQRFKALDE AQTGTITYEQ YKQAGLWFSG DEDIKIPENP
LEPLPFNRQE HLIEFFFRLF ADCEKEPPQL DYTQMLLYFA CHPDTLEGVY RALSVAVGTH
IFRQVETPML MAEKTSISTV SPIEEFPETE ESSAKEDREL KEEKDDQKEE EIPENANTEK
ISMETLLKVF GGGNEVLDAN RFASYLKSEN IYAENFIKTF QDLGARNLEP IAVNILLKHP
YIQDLIANYV DYKFPDIKMI LQRSEHAQGS DGERSPSRLT DEKK
