FR1L5_HUMAN
ID FR1L5_HUMAN Reviewed; 2057 AA.
AC A0AVI2; A0A096LNV2; Q17RH2; Q6ZU24;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2017, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Fer-1-like protein 5;
GN Name=FER1L5;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 77-211 (ISOFORM 1).
RC TISSUE=Testis;
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).
CC -!- FUNCTION: Plays a role in myoblast fusion; probable mediator of
CC endocytic recycling for membrane trafficking events during myotube
CC formation. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000255|PROSITE-
CC ProRule:PRU00041};
CC -!- SUBUNIT: Interacts (via second C2 domain) with EHD1 and EHD2.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Membrane
CC {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
CC Note=Colocalizes with EHD1 and EHD2 at plasma membrane in myoblasts and
CC myotubes. Localizes into foci at the plasma membrane (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A0AVI2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0AVI2-2; Sequence=VSP_031852;
CC Name=3;
CC IsoId=A0AVI2-4; Sequence=VSP_031852, VSP_059071;
CC -!- MISCELLANEOUS: [Isoform 1]: Gene prediction based on partial mRNA data.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ferlin family. {ECO:0000305}.
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DR EMBL; AC068539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117324; AAI17325.1; -; mRNA.
DR EMBL; BC126368; AAI26369.1; -; mRNA.
DR EMBL; AK126032; BAC86403.1; -; mRNA.
DR CCDS; CCDS77438.1; -. [A0AVI2-1]
DR RefSeq; NP_001280012.1; NM_001293083.1. [A0AVI2-1]
DR AlphaFoldDB; A0AVI2; -.
DR SMR; A0AVI2; -.
DR BioGRID; 124699; 3.
DR IntAct; A0AVI2; 1.
DR STRING; 9606.ENSP00000485487; -.
DR iPTMnet; A0AVI2; -.
DR PhosphoSitePlus; A0AVI2; -.
DR BioMuta; FER1L5; -.
DR jPOST; A0AVI2; -.
DR MassIVE; A0AVI2; -.
DR PeptideAtlas; A0AVI2; -.
DR PRIDE; A0AVI2; -.
DR ProteomicsDB; 19; -. [A0AVI2-1]
DR ProteomicsDB; 20; -. [A0AVI2-2]
DR Antibodypedia; 73876; 15 antibodies from 6 providers.
DR DNASU; 90342; -.
DR Ensembl; ENST00000624922.6; ENSP00000485238.1; ENSG00000249715.13. [A0AVI2-1]
DR GeneID; 90342; -.
DR KEGG; hsa:90342; -.
DR MANE-Select; ENST00000624922.6; ENSP00000485238.1; NM_001293083.2; NP_001280012.1.
DR UCSC; uc010fia.3; human. [A0AVI2-1]
DR CTD; 90342; -.
DR DisGeNET; 90342; -.
DR GeneCards; FER1L5; -.
DR HGNC; HGNC:19044; FER1L5.
DR HPA; ENSG00000249715; Tissue enhanced (choroid plexus, testis).
DR neXtProt; NX_A0AVI2; -.
DR OpenTargets; ENSG00000249715; -.
DR PharmGKB; PA142671764; -.
DR VEuPathDB; HostDB:ENSG00000249715; -.
DR eggNOG; KOG1326; Eukaryota.
DR GeneTree; ENSGT00940000161318; -.
DR InParanoid; A0AVI2; -.
DR OMA; SEGWEYG; -.
DR OrthoDB; 20162at2759; -.
DR PhylomeDB; A0AVI2; -.
DR PathwayCommons; A0AVI2; -.
DR SignaLink; A0AVI2; -.
DR BioGRID-ORCS; 90342; 13 hits in 133 CRISPR screens.
DR ChiTaRS; FER1L5; human.
DR GenomeRNAi; 90342; -.
DR Pharos; A0AVI2; Tdark.
DR PRO; PR:A0AVI2; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; A0AVI2; protein.
DR Bgee; ENSG00000249715; Expressed in sperm and 80 other tissues.
DR ExpressionAtlas; A0AVI2; baseline and differential.
DR Genevisible; A0AVI2; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030315; C:T-tubule; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IBA:GO_Central.
DR GO; GO:0002281; P:macrophage activation involved in immune response; IBA:GO_Central.
DR GO; GO:0061025; P:membrane fusion; IBA:GO_Central.
DR GO; GO:0002280; P:monocyte activation involved in immune response; IBA:GO_Central.
DR GO; GO:0007520; P:myoblast fusion; IEA:InterPro.
DR GO; GO:0050765; P:negative regulation of phagocytosis; IBA:GO_Central.
DR GO; GO:0007009; P:plasma membrane organization; IBA:GO_Central.
DR GO; GO:0001778; P:plasma membrane repair; IBA:GO_Central.
DR GO; GO:0033292; P:T-tubule organization; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR CDD; cd08373; C2A_Ferlin; 1.
DR CDD; cd04011; C2B_Ferlin; 1.
DR CDD; cd04017; C2D_Ferlin; 1.
DR CDD; cd04037; C2E_Ferlin; 1.
DR CDD; cd08374; C2F_Ferlin; 1.
DR Gene3D; 2.60.40.150; -; 6.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037726; C2A_Ferlin.
DR InterPro; IPR037720; C2B_Ferlin.
DR InterPro; IPR037723; C2D_Ferlin.
DR InterPro; IPR037724; C2E_Ferlin.
DR InterPro; IPR037725; C2F_Ferlin.
DR InterPro; IPR029997; Fer1L5.
DR InterPro; IPR012968; FerIin_dom.
DR InterPro; IPR037721; Ferlin.
DR InterPro; IPR012560; Ferlin_A-domain.
DR InterPro; IPR012561; Ferlin_B-domain.
DR InterPro; IPR032362; Ferlin_C.
DR InterPro; IPR006614; Peroxin/Ferlin.
DR PANTHER; PTHR12546; PTHR12546; 1.
DR PANTHER; PTHR12546:SF34; PTHR12546:SF34; 1.
DR Pfam; PF00168; C2; 7.
DR Pfam; PF08165; FerA; 1.
DR Pfam; PF08150; FerB; 1.
DR Pfam; PF16165; Ferlin_C; 1.
DR SMART; SM00239; C2; 6.
DR SMART; SM00694; DysFC; 2.
DR SMART; SM00693; DysFN; 2.
DR SMART; SM01200; FerA; 1.
DR SMART; SM01201; FerB; 1.
DR SMART; SM01202; FerI; 1.
DR SUPFAM; SSF49562; SSF49562; 7.
DR PROSITE; PS50004; C2; 7.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cell membrane; Membrane; Metal-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..2057
FT /note="Fer-1-like protein 5"
FT /id="PRO_0000300498"
FT TRANSMEM 1962..1982
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1..99
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 152..265
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 308..425
FT /note="C2 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1057..1188
FT /note="C2 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1213..1346
FT /note="C2 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1467..1587
FT /note="C2 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 1705..1853
FT /note="C2 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1502
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1502
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1508
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1557
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1557
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1558
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1559
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1559
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1559
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1562
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1565
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1565
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1824
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1827
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 1830
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT VAR_SEQ 1..1255
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031852"
FT VAR_SEQ 1298
FT /note="Missing (in isoform 3)"
FT /id="VSP_059071"
FT VARIANT 354
FT /note="I -> T (in dbSNP:rs4907201)"
FT /id="VAR_059285"
FT VARIANT 687
FT /note="T -> A (in dbSNP:rs7599598)"
FT /id="VAR_059286"
SQ SEQUENCE 2057 AA; 237935 MW; E48E0652AD6CE253 CRC64;
MLRLVVQSAK IDPPLAPLPR PCMSIDFRDI KKRTRVVEGN DPVWNETLIW HLWNRPLEND
SFLQVTLQDM GSQKKERFIG LATVLLKPLL KQPSEVLFVK DLTLLNHSMK PTDCTVTLQV
AHMSNQDIEK TGAEDHLGIT AREAASQKLM VPGSTAHRAL SSKPQHFQVR VKVFEARQLM
GNNIKPVVKV SIAGQQHQTR IKMGNNPFFN EIFFQNFHEV PAKFFDETIL IQVVNSSAMR
YKAEIGRFQT DIGFIYHSPG HTLLRKWLGL CQPNNPGSGV TGYLKVTIYA LGVGDQALID
QKLLYGTDDT DIQIFKSAVV PINMAYLQLF IYCAEDLHLK KHQSVNPQLE VELIGEKLRT
HMQTQTDNPI WNQILTFRIQ LPCLSSYIKF RVLDCRKKDC PDEIGTASLS LNQISSTGEE
IEGVYSGFLP CFGPSFLTLH GGKKAPFRIQ EEGACIPDSV RDGLAYRGRV FLELITQIKS
YQDSTIKDLS HEVTRIEKHQ NRQKYGLCVI FLSCTMMPNF KELIHFEVSI GHYGNKMDLN
YKPLVSSTPY SPVIYDGNIY HYVPWYNTKP VVAVTSNWED VSFRMNCLNL LHFTRDRLKA
NLDTLKSTRN PKDPALLYQW EKLLRELAED CKRPLPCMTY QPKATSLDRK RWQLRSLLLQ
ELAQKAKQAK PKDMVATAED WLYRLNTVLP EPQMGLPDVM IWLVAKEQRV AYAQVPAHSV
LFSPAGALHS GRLCGKIQTL FLQYPEGEGQ KDVLPAHLRV CMWLGNVTDS KDLQLLRQGD
TAVYAEMYEN QAKYKDQWGQ QGLYHCPNFS DVMGNKTLPM TDFQPPLGWH WQDSWTVEPQ
RRLLLDIDIN KSQVLEEVYE NQGRDTRGAW GPAAIPNTDV NGQPMEAREN VKCPQGWHFK
KDWVVELNHA VDSKGWEYGV GIPPSGLPQV WSPVEKTYHS CRRRRWARVR FRNHGELSHE
QETLSFLQLG LAKGEEEGWE YDTFGSKFHL NPQPQSRFRR RCWRRRLAPN KDKGIAPIFL
LEGSLAMDLK YHAGKEEDSK TWPWGLDRQF RDPQRQDTRP PNLPFIYCTF NKPHYYQLFC
YIYQARNLVS NQILTFQGPF IRVVFLNHSQ CTQTLRSSAG PTWAQTLIFQ HLLLYENPQD
TKESPPLVVL ELWQRDFWGK ESLWGRSVWP PMVWLDLQDR ILPPMRWHPL VKELGKEEGE
ILASCELILQ TEKLGEKQLP ILSVPWKNGA YTLPKSIQPT IKRMAIEILA WGLRNMKKAS
SPQLLVEFGE ESLRTEPIRD FQTNPNFPES ESVLVLTVLM PTEEAYALPL VVKVVDNWAF
GQQTVTGQAN IDFLQPYFCD PWAQDYMHPK LPTLSEKKHQ DFLGYLYRKF WFKSSKAEDE
YEHEVDWWSK LFWATDEHKS LKYKYKDYHT LKVYECELEA VPAFQGLQDF CQTFKLYQEQ
PKLDSPVVGE FKGLFRIYPF PENPEAPKPP LQFLVWPERE DFPQPCLVRV YMVRAINLQP
QDYNGLCDPY VILKLGKTEL GNRDMYQPNT LDPIFGMMFE LTCNIPLEKD LEIQLYDFDL
FSPDDKIGTT VIDLENRLLS GFGAHCGLSK SYCQSGPFRW RDQMPPSYLL ERYAKRKGLP
PPLFSPEEDA VFYNGKKFKL QSFEPKTPTV HGLGPKKERL ALYLLHTQGL VPEHVETRTL
YSHSQPGIDQ GKVQMWVDIF PKKLGPPGPQ VNINPRKPKR YELRCIIWKT ANVDLVDDNL
SREKTSDIYI KGWLYGLEKD MQKTDIHYHS LTGEADFNWR FIFTMDYLAA ERTCVQSQKD
YIWSLDATSM KFPARLIIQV WDNDIFSPDD FLGVLELDLS DMPLPARHAK QCSIRMMDAD
PKWPYFIQYK HFSLFKKKTV TGWWPCQVLD GGKWRLSGKV KMSLEILSEK EALIKPAGRG
QSEPNQYPTL HPPLRTNTSF TWLRSPVQNF CYIFWKRYRF KLIAFMVISI IALMLFNFIY
SAPHYLAMSW IKPQLQLYPP IKIFNIINSL NTSNASSSIL PTQDPNLKPT IDHEWKLHPG
PTNHLSDIFP ELPAPGD
