FREM1_MOUSE
ID FREM1_MOUSE Reviewed; 2191 AA.
AC Q684R7; Q5H8C2; Q5M7B3; Q8C732;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=FRAS1-related extracellular matrix protein 1;
DE AltName: Full=Protein QBRICK;
DE Flags: Precursor;
GN Name=Frem1;
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 1), FUNCTION, DISEASE, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=15345741; DOI=10.1073/pnas.0402760101;
RA Smyth I., Du X., Taylor M.S., Justice M.J., Beutler B., Jackson I.J.;
RT "The extracellular matrix gene Frem1 is essential for the normal adhesion
RT of the embryonic epidermis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13560-13565(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF ASP-207.
RX PubMed=15878328; DOI=10.1016/j.yexcr.2005.01.020;
RA Kiyozumi D., Osada A., Sugimoto N., Weber C.N., Ono Y., Imai T., Okada A.,
RA Sekiguchi K.;
RT "Identification of a novel cell-adhesive protein spatiotemporally expressed
RT in the basement membrane of mouse developing hair follicle.";
RL Exp. Cell Res. 306:9-23(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1096-2191 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1737-2191.
RC TISSUE=Limb;
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).
CC -!- FUNCTION: Extracellular matrix protein that plays a role in epidermal
CC differentiation and is required for epidermal adhesion during embryonic
CC development. {ECO:0000269|PubMed:15345741}.
CC -!- SUBUNIT: Interacts with FREM2. {ECO:0000250|UniProtKB:Q5SZK8}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000269|PubMed:15878328}. Note=Localizes
CC at the basement membrane zone of embryonic epidermis and hair
CC follicles. {ECO:0000269|PubMed:15878328}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q684R7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q684R7-2; Sequence=VSP_015032;
CC Name=3;
CC IsoId=Q684R7-3; Sequence=VSP_015033, VSP_015034;
CC -!- TISSUE SPECIFICITY: Expressed in epidermis and hair follicles.
CC Expressed in many developing epidermal appendages, including the
CC whisker and sensory vibrissae, cranial and trunk hair follicles,
CC meibomian glands, teeth, footpads, eyelash primordia and invaginating
CC mammary glands. Limb expression localizes to sheets of dermal cells on
CC the apical and basal surfaces of the digits but, unlike FRAS1, is
CC excluded from the apical ectodermal ridge. Usually expressed at higher
CC level in dermal cells underlying the differentiating epithelial
CC components, especially underlying the epidermis of the head, limbs, and
CC eyelids. Expression in the eyelid dermis is apparent as early as 13
CC dpc. Postnatal expression in the skin is limited to the dermal
CC papillae. In the kidney, it is expressed from 12.5 dpc in the
CC mesenchyme surrounding the branching ureteric tree, with a strong
CC expression in the more proximal regions of these tubules rather than at
CC the proliferating and branching ends of the ureteric buds. In hair
CC follicle, it is selectively expressed in the vibrissal hair primordia
CC during development. Preferentially expressed in the whisker pad
CC epithelia of 12.5 dpc embryos, in both the epithelial and mesenchymal
CC cells of developing hair follicles. In the early stages of hair
CC follicle development (i.e. stages 0-1), it is expressed in both hair
CC placodes and dermal condensations. In stage 2, it is detected in dermal
CC condensations and adjacent epithelia, but not in the upper region of
CC the hair follicles. Expressed at the tip of developing hair follicles
CC in the later stages (i.e. stages 3-5). {ECO:0000269|PubMed:15345741,
CC ECO:0000269|PubMed:15878328}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryos of all stages examined
CC and in some adult tissues including eye, kidney, ovary, urinary bladder
CC and testes; however, the overall expression levels in adult tissues are
CC relatively low compared with those in embryonic tissues.
CC -!- DOMAIN: The Calx-beta domain binds calcium with high affinity and
CC undergo a major conformational shift upon binding. {ECO:0000250}.
CC -!- DISEASE: Note=Defects in Frem1 are the cause of head blebs (heb) which
CC is a spontaneous mutation that is characterized by absent or malformed
CC eyes, which are often open at birth. Cryptophthalmos is noted in all
CC heb homozygous animals, as is occasional hindlimb polydactyly.
CC {ECO:0000269|PubMed:15345741}.
CC -!- MISCELLANEOUS: Was termed QBRICK because it contains 12 repeats: 'Q'
CC stands for queen and is taken from the queen being the 12th in a suit
CC of playing card, and 'BRICK' stands for the repeating unit.
CC -!- MISCELLANEOUS: Frem1 also corresponds to a N-ethyl-N-nitrosourea-
CC induced allele called 'bat'. Homozygous bat mice display similar
CC phenotype than heb mice.
CC -!- SIMILARITY: Belongs to the FRAS1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH88732.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC35069.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ616838; CAE83577.1; -; mRNA.
DR EMBL; AB160986; BAD89014.1; -; mRNA.
DR EMBL; AK052629; BAC35069.1; ALT_INIT; mRNA.
DR EMBL; BC088732; AAH88732.1; ALT_FRAME; mRNA.
DR CCDS; CCDS38791.1; -. [Q684R7-1]
DR CCDS; CCDS57281.1; -. [Q684R7-2]
DR RefSeq; NP_001185740.1; NM_001198811.1. [Q684R7-2]
DR RefSeq; NP_808531.2; NM_177863.4. [Q684R7-1]
DR RefSeq; XP_006538076.1; XM_006538013.3. [Q684R7-2]
DR RefSeq; XP_006538077.1; XM_006538014.2. [Q684R7-2]
DR RefSeq; XP_006538078.1; XM_006538015.1. [Q684R7-2]
DR RefSeq; XP_011248357.1; XM_011250055.2. [Q684R7-2]
DR AlphaFoldDB; Q684R7; -.
DR DIP; DIP-61243N; -.
DR IntAct; Q684R7; 2.
DR STRING; 10090.ENSMUSP00000071627; -.
DR GlyGen; Q684R7; 6 sites.
DR iPTMnet; Q684R7; -.
DR PhosphoSitePlus; Q684R7; -.
DR MaxQB; Q684R7; -.
DR PaxDb; Q684R7; -.
DR PRIDE; Q684R7; -.
DR ProteomicsDB; 266856; -. [Q684R7-1]
DR ProteomicsDB; 266857; -. [Q684R7-2]
DR ProteomicsDB; 266858; -. [Q684R7-3]
DR Antibodypedia; 42751; 97 antibodies from 23 providers.
DR DNASU; 329872; -.
DR Ensembl; ENSMUST00000071708; ENSMUSP00000071627; ENSMUSG00000059049. [Q684R7-1]
DR Ensembl; ENSMUST00000107230; ENSMUSP00000102849; ENSMUSG00000059049. [Q684R7-2]
DR GeneID; 329872; -.
DR KEGG; mmu:329872; -.
DR UCSC; uc008tkm.2; mouse. [Q684R7-1]
DR CTD; 158326; -.
DR MGI; MGI:2670972; Frem1.
DR VEuPathDB; HostDB:ENSMUSG00000059049; -.
DR eggNOG; KOG3597; Eukaryota.
DR GeneTree; ENSGT00940000156990; -.
DR InParanoid; Q684R7; -.
DR OMA; MVYVTDG; -.
DR OrthoDB; 13258at2759; -.
DR PhylomeDB; Q684R7; -.
DR TreeFam; TF316876; -.
DR BioGRID-ORCS; 329872; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Frem1; mouse.
DR PRO; PR:Q684R7; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q684R7; protein.
DR Bgee; ENSMUSG00000059049; Expressed in renal medulla interstitium and 158 other tissues.
DR ExpressionAtlas; Q684R7; baseline and differential.
DR Genevisible; Q684R7; MM.
DR GO; GO:0005604; C:basement membrane; IDA:BHF-UCL.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
DR GO; GO:0097094; P:craniofacial suture morphogenesis; ISS:UniProtKB.
DR Gene3D; 2.60.40.2030; -; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR039005; CSPG_rpt.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR045658; FRAS1-rel_N.
DR InterPro; IPR032825; FREM1.
DR PANTHER; PTHR45739:SF7; PTHR45739:SF7; 1.
DR Pfam; PF03160; Calx-beta; 1.
DR Pfam; PF19309; Frem_N; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF141072; SSF141072; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS51854; CSPG; 12.
PE 1: Evidence at protein level;
KW Alternative splicing; Basement membrane; Calcium; Cell adhesion;
KW Developmental protein; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Lectin; Metal-binding; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..2191
FT /note="FRAS1-related extracellular matrix protein 1"
FT /id="PRO_0000010123"
FT REPEAT 300..394
FT /note="CSPG 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 419..506
FT /note="CSPG 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 527..621
FT /note="CSPG 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 648..779
FT /note="CSPG 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 801..892
FT /note="CSPG 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 912..1007
FT /note="CSPG 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1049..1151
FT /note="CSPG 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1172..1273
FT /note="CSPG 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1294..1391
FT /note="CSPG 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1412..1504
FT /note="CSPG 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1525..1614
FT /note="CSPG 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1650..1742
FT /note="CSPG 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT DOMAIN 1749..1848
FT /note="Calx-beta"
FT DOMAIN 2072..2186
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 1874..1921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 205..207
FT /note="Cell attachment site"
FT COMPBIAS 1896..1912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1039
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 2163..2177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 729..747
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15878328"
FT /id="VSP_015032"
FT VAR_SEQ 1500..1544
FT /note="RFTISNGLQTQRGVFEITLQTVDSALPVLTKNKRLRLAEGAMGLL -> SRW
FT GHKSPCRLPCLSLPDLPSAMDCRPSVGCLKSHCRLWTAPCLC (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015033"
FT VAR_SEQ 1545..2191
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015034"
FT MUTAGEN 207
FT /note="D->E: Impairs cell adhesion ability in vitro."
FT /evidence="ECO:0000269|PubMed:15878328"
SQ SEQUENCE 2191 AA; 244544 MW; A7D18FD3E32FD3C3 CRC64;
MHSPGCTGPK AQWFLLLQLL LLHLDRVSAT FISINRGLRV MKGSSAFLSG DHLRVAVPKE
KDACRLEVVM NEPVTQRVGK LSPQVFDCHF LPNEVKYVHN GCPILDEDSV KLRLYRFTET
DTFMETFLLR VYLVEPDCNI IRMSSNVLEV TEFYGLSQAI DKNLLQFDYD RTASLDCTIR
LDPLRTQLPA HGKLVVVNRK SEGPRGDQPH SFFSETELGA GLKCPDGSCA LELKQVASLK
VSCEEFLLTG FHYQHMQPPS PNIDYIPIQL DLTDRRSKTV YKSESAWLPV YIRVGIPNQV
PRAAFMAMFV LEVDQFILTP LTTSVLDCEE DETPKPLLVF NITKAPLQGY VTHLLDHTRP
ISSFTWKDLS DMQVAYQPPN SSHPERRHYT MELEVYDFFF ERSAPITVHI SIRTADTNAP
RVSWNTGLNL LEGQSRAITW EQFQIVDNDD IGAVQLVTIG GLQHGRLTVR EGKGFLFTVT
DLQAGVVRYH HDDSDTTKDF VAFRIFDGHH SSHHKFPINI LPKDDSPPFL ITNVVIELEE
GKTILIQGSM LRASDMDSSD DYIFFNITKF PQAGEIMKKP GPRLIGYPVP GFLQRDLFSG
IIYYRHFGGE IFEDSFEFVL WDSHEPPNLS VPQVVTIHIT PVDDQLPKEA PGISRHLVVK
ETEVAYITKK HLHFLDMESR DGELIYTVTR PPCFSFSHRH LDAGKLFMVD SIPKLTKNPT
APGLSSFTQG LILISANQHT CSSQFASQHA VNHMKVAYMP PMQDIGPSPR HVQFTVSVSN
QHGGALHGIC FNITVLPVDN QVPEVFTNTL RVVEGGQCTI STEHILVSDV DTPLDSISLS
LKERPLHGGV ELDGFPLNPR GTFSWRDLNT LKVWYQHDGS EVLQDEIFLE VTDGTNSAAF
VLHIEVFPVN DEPPILKADL IPMMHCSEGG EVTITPEYIS ATDADSDDLE LLFLIAREPQ
HGVVRKAGLH VDRFSQGDVI SGAVTYKHTG GEIGLEPCSD TVVLVVSDGE ADPLMNGCCY
DGPDSSVPLH KSFPTYQLNI TVHPVDNQPP SIIIGRMLTV DEGFSAALTT HHLTVVDWDT
APDDLKFMLA SQPQFGYLEN ALPSAGFEKS NIGIRIASFQ WTDMKASHIN YVQSRHLRVE
PTADQFTVYA TDGKHRSLET TFHVIINPTN DEAPDLAVQN ITVYEGHMVE LDSSIISATD
RDIPKDPLLF SIALKPQHGL LVDAAISKDS HQIKQLQHEI HSFSVDLLKN GMKLVYAHDD
SESSADNFVI QLSDGKHKIL KTISVNITPV NDETPTLSKK AEISMAVGDT RVLSSAVLSA
TDKDSPREKI HYVFERLPQN GQLQLKIGRD WVPLSTGMQC TQEDVDLNLL RYTHAGKTDS
QDGDSFTFYL WDEDNRSPAF DCHIIIEDMG KGDIVIHAKP LVVVKGDRGL LTTATLLAVD
GADKPEELLY LITSPPRHGQ VEYVHSPGVP IASFSQMDIA GQTVCYIHKS RTAVPTDSFR
FTISNGLQTQ RGVFEITLQT VDSALPVLTK NKRLRLAEGA MGLLSADHLQ LTDPDTPPEN
LTFFLAQLPR HGYLFLRGKA LQHNFTQRDV DSGGVAYQHS GGGAREDYFT FLATDRKNQG
FVVDGKVQKE PVRFTIQVDQ LDKAAPRITH LHSPTQVGLL KNGCYGIYIT SRVLKASDPD
TEDDQIIFKI LRGPLYGRLE NTTTGEFIHE RFSQKDLSHK TILYIINPSL QVTSDILEFQ
AMDPTGNTAT PQSLDLRWSY IEWAQTAYEV CENVGLLPLE VTRRGYPMDS AFVGVEVNQV
SATVGKDFTV TPSKLLQFDP GMSTKMWNIA ITYDGLEEDD EVFEVILNSP VNAVLGTQTK
AAVKILDSKG GRCHPSNSFN QSKHSTWGKG PWHPLPSGSS SLTTSGSPLL ERPPPSFTSG
DALQGFGLTD LTQRKTMTQG NGKSVLPSSV CRNGTDTIYN YHGIVSLKLE GDRFSAHKRK
AKISIVSQPQ RTIKVAELPL ADKVESTTDL HFLRQGLRPL FPKNCSVDLK GLFHFEESTH
RLYQCDGISW KAWSPQTKGL EDRSCPGGWL LHSGYCHILV TRQKGTWTTA TRACREQHQG
DLVTVLSRRH MQWLWAMSGR KPFWIGLKNQ PRTGHWEWIG GEPVAFTNWR RGAPLHPKPG
KNCALVQKRG QWQTKNCSKG KAHNFVCSRK L
