FZD3_HUMAN
ID FZD3_HUMAN Reviewed; 666 AA.
AC Q9NPG1; A8K615;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Frizzled-3;
DE Short=Fz-3;
DE Short=hFz3;
DE Flags: Precursor;
GN Name=FZD3;
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 [MRNA].
RC TISSUE=Fetal brain;
RX PubMed=10777673; DOI=10.1006/bbrc.2000.2578;
RA Kirikoshi H., Koike J., Sagara N., Saitoh T., Tokuhara M., Tanaka K.,
RA Sekihara H., Hirai M., Katoh M.;
RT "Molecular cloning and genomic structure of human frizzled-3 at chromosome
RT 8p21.";
RL Biochem. Biophys. Res. Commun. 271:8-14(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal brain;
RX PubMed=10873558; DOI=10.1006/bbrc.2000.2882;
RA Sala C.F., Formenti E., Terstappen G.C., Caricasole A.;
RT "Identification, gene structure and expression of human frizzled-3
RT (FZD3).";
RL Biochem. Biophys. Res. Commun. 273:27-34(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Keratinocyte;
RX PubMed=11407985; DOI=10.1046/j.1523-1747.2001.01336.x;
RA Hung B.S., Wang X.-Q., Cam G.R., Rothnagel J.A.;
RT "Characterization of mouse frizzled-3 expression in hair follicle
RT development and identification of the human homolog in keratinocytes.";
RL J. Invest. Dermatol. 116:940-946(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
RN [5]
RP PROTEIN SEQUENCE OF 23-37.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [6]
RP VARIANTS SER-4; MET-199 AND VAL-545.
RX PubMed=22045688; DOI=10.1002/humu.21643;
RA De Marco P., Merello E., Rossi A., Piatelli G., Cama A., Kibar Z.,
RA Capra V.;
RT "FZD6 is a novel gene for human neural tube defects.";
RL Hum. Mutat. 33:384-390(2012).
CC -!- FUNCTION: Receptor for Wnt proteins. Most of frizzled receptors are
CC coupled to the beta-catenin canonical signaling pathway, which leads to
CC the activation of disheveled proteins, inhibition of GSK-3 kinase,
CC nuclear accumulation of beta-catenin and activation of Wnt target
CC genes. A second signaling pathway involving PKC and calcium fluxes has
CC been seen for some family members, but it is not yet clear if it
CC represents a distinct pathway or if it can be integrated in the
CC canonical pathway, as PKC seems to be required for Wnt-mediated
CC inactivation of GSK-3 kinase. Both pathways seem to involve
CC interactions with G-proteins. Activation by Wnt5A stimulates PKC
CC activity via a G-protein-dependent mechanism. Involved in transduction
CC and intercellular transmission of polarity information during tissue
CC morphogenesis and/or in differentiated tissues. Plays a role in
CC controlling early axon growth and guidance processes necessary for the
CC formation of a subset of central and peripheral major fiber tracts.
CC Required for the development of major fiber tracts in the central
CC nervous system, including: the anterior commissure, the corpus
CC callosum, the thalamocortical, corticothalamic and nigrostriatal
CC tracts, the corticospinal tract, the fasciculus retroflexus, the
CC mammillothalamic tract, the medial lemniscus, and ascending fiber
CC tracts from the spinal cord to the brain. In the peripheral nervous
CC system, controls axon growth in distinct populations of cranial and
CC spinal motor neurons, including the facial branchimotor nerve, the
CC hypoglossal nerve, the phrenic nerve, and motor nerves innervating
CC dorsal limbs. Involved in the migration of cranial neural crest cells.
CC May also be implicated in the transmission of sensory information from
CC the trunk and limbs to the brain. Controls commissural sensory axons
CC guidance after midline crossing along the anterior-posterior axis in
CC the developing spinal cord in a Wnt-dependent signaling pathway.
CC Together with FZD6, is involved in the neural tube closure and plays a
CC role in the regulation of the establishment of planar cell polarity
CC (PCP), particularly in the orientation of asymmetric bundles of
CC stereocilia on the apical faces of a subset of auditory and vestibular
CC sensory cells located in the inner ear. Promotes neurogenesis by
CC maintaining sympathetic neuroblasts within the cell cycle in a beta-
CC catenin-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:Q61086}.
CC -!- SUBUNIT: Interacts with VANGL2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell
CC membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell
CC surface {ECO:0000250|UniProtKB:Q61086}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q61086}; Multi-pass membrane protein.
CC Note=Colocalizes with FZD6 at the apical face of the cell (By
CC similarity). {ECO:0000250|UniProtKB:Q61086}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=Q9NPG1-1; Sequence=Displayed;
CC Name=Short; Synonyms=FZD3deltaC;
CC IsoId=Q9NPG1-2; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Widely expressed. Relatively high expression in the
CC CNS, including regions of the limbic system, in kidney, pancreas,
CC skeletal muscle, uterus and testis.
CC -!- DOMAIN: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl
CC (Disheveled) family members and is involved in the activation of the
CC Wnt/beta-catenin signaling pathway. {ECO:0000250}.
CC -!- DOMAIN: The FZ domain is involved in binding with Wnt ligands.
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated by ZNRF3, leading to its degradation by the
CC proteasome. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC {ECO:0000305}.
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DR EMBL; AB039723; BAA94968.1; -; mRNA.
DR EMBL; AJ272427; CAB89114.1; -; mRNA.
DR EMBL; AY005130; AAF89088.1; -; mRNA.
DR EMBL; AK291480; BAF84169.1; -; mRNA.
DR CCDS; CCDS6069.1; -. [Q9NPG1-1]
DR PIR; JC7312; JC7312.
DR RefSeq; NP_059108.1; NM_017412.3. [Q9NPG1-1]
DR RefSeq; NP_665873.1; NM_145866.1. [Q9NPG1-1]
DR AlphaFoldDB; Q9NPG1; -.
DR SMR; Q9NPG1; -.
DR BioGRID; 113689; 25.
DR IntAct; Q9NPG1; 8.
DR STRING; 9606.ENSP00000437489; -.
DR GlyGen; Q9NPG1; 4 sites.
DR iPTMnet; Q9NPG1; -.
DR PhosphoSitePlus; Q9NPG1; -.
DR BioMuta; FZD3; -.
DR DMDM; 17433071; -.
DR EPD; Q9NPG1; -.
DR jPOST; Q9NPG1; -.
DR MassIVE; Q9NPG1; -.
DR MaxQB; Q9NPG1; -.
DR PaxDb; Q9NPG1; -.
DR PeptideAtlas; Q9NPG1; -.
DR PRIDE; Q9NPG1; -.
DR ProteomicsDB; 81989; -. [Q9NPG1-1]
DR Antibodypedia; 10432; 461 antibodies from 35 providers.
DR DNASU; 7976; -.
DR Ensembl; ENST00000240093.8; ENSP00000240093.3; ENSG00000104290.11. [Q9NPG1-1]
DR Ensembl; ENST00000537916.2; ENSP00000437489.1; ENSG00000104290.11. [Q9NPG1-1]
DR GeneID; 7976; -.
DR KEGG; hsa:7976; -.
DR MANE-Select; ENST00000240093.8; ENSP00000240093.3; NM_017412.4; NP_059108.1.
DR UCSC; uc003xgx.4; human. [Q9NPG1-1]
DR CTD; 7976; -.
DR DisGeNET; 7976; -.
DR GeneCards; FZD3; -.
DR HGNC; HGNC:4041; FZD3.
DR HPA; ENSG00000104290; Tissue enhanced (retina).
DR MalaCards; FZD3; -.
DR MIM; 606143; gene.
DR neXtProt; NX_Q9NPG1; -.
DR OpenTargets; ENSG00000104290; -.
DR PharmGKB; PA28458; -.
DR VEuPathDB; HostDB:ENSG00000104290; -.
DR eggNOG; KOG3577; Eukaryota.
DR GeneTree; ENSGT00940000156491; -.
DR HOGENOM; CLU_007873_4_1_1; -.
DR InParanoid; Q9NPG1; -.
DR OMA; WIVFYLW; -.
DR OrthoDB; 330751at2759; -.
DR PhylomeDB; Q9NPG1; -.
DR TreeFam; TF317907; -.
DR PathwayCommons; Q9NPG1; -.
DR Reactome; R-HSA-373080; Class B/2 (Secretin family receptors).
DR Reactome; R-HSA-4086398; Ca2+ pathway.
DR Reactome; R-HSA-4086400; PCP/CE pathway.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR SignaLink; Q9NPG1; -.
DR SIGNOR; Q9NPG1; -.
DR BioGRID-ORCS; 7976; 14 hits in 1072 CRISPR screens.
DR ChiTaRS; FZD3; human.
DR GeneWiki; FZD3; -.
DR GenomeRNAi; 7976; -.
DR Pharos; Q9NPG1; Tbio.
DR PRO; PR:Q9NPG1; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9NPG1; protein.
DR Bgee; ENSG00000104290; Expressed in Brodmann (1909) area 23 and 185 other tissues.
DR ExpressionAtlas; Q9NPG1; baseline and differential.
DR Genevisible; Q9NPG1; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0032433; C:filopodium tip; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0048786; C:presynaptic active zone; IEA:Ensembl.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR GO; GO:0042813; F:Wnt receptor activity; IBA:GO_Central.
DR GO; GO:0017147; F:Wnt-protein binding; IPI:UniProtKB.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0033278; P:cell proliferation in midbrain; IEA:Ensembl.
DR GO; GO:0071679; P:commissural neuron axon guidance; IEA:Ensembl.
DR GO; GO:0036514; P:dopaminergic neuron axon guidance; IEA:Ensembl.
DR GO; GO:0001736; P:establishment of planar polarity; IEA:Ensembl.
DR GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
DR GO; GO:1904693; P:midbrain morphogenesis; TAS:ParkinsonsUK-UCL.
DR GO; GO:0097475; P:motor neuron migration; IEA:Ensembl.
DR GO; GO:1900118; P:negative regulation of execution phase of apoptosis; ISS:UniProtKB.
DR GO; GO:0045976; P:negative regulation of mitotic cell cycle, embryonic; ISS:UniProtKB.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:1904938; P:planar cell polarity pathway involved in axon guidance; IEA:Ensembl.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; ISS:UniProtKB.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IEA:Ensembl.
DR GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0036515; P:serotonergic neuron axon guidance; IEA:Ensembl.
DR GO; GO:0061549; P:sympathetic ganglion development; ISS:UniProtKB.
DR GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; NAS:ParkinsonsUK-UCL.
DR CDD; cd07449; CRD_FZ3; 1.
DR Gene3D; 1.10.2000.10; -; 1.
DR InterPro; IPR015526; Frizzled/SFRP.
DR InterPro; IPR000539; Frizzled/Smoothened_TM.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR041769; FZ3_CRD.
DR InterPro; IPR026553; FZD3_vertebrates.
DR InterPro; IPR017981; GPCR_2-like.
DR PANTHER; PTHR11309; PTHR11309; 1.
DR PANTHER; PTHR11309:SF22; PTHR11309:SF22; 1.
DR Pfam; PF01534; Frizzled; 1.
DR Pfam; PF01392; Fz; 1.
DR PRINTS; PR00489; FRIZZLED.
DR SMART; SM00063; FRI; 1.
DR SMART; SM01330; Frizzled; 1.
DR SUPFAM; SSF63501; SSF63501; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Developmental protein;
KW Direct protein sequencing; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Neurogenesis; Receptor; Reference proteome; Signal;
KW Transducer; Transmembrane; Transmembrane helix; Ubl conjugation;
KW Wnt signaling pathway.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 23..666
FT /note="Frizzled-3"
FT /id="PRO_0000012982"
FT TOPO_DOM 23..205
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 227..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..288
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..374
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..420
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..441
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 442..477
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..666
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 23..136
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 538..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 502..507
FT /note="Lys-Thr-X-X-X-Trp motif, mediates interaction with
FT the PDZ domain of Dvl family members"
FT /evidence="ECO:0000250"
FT COMPBIAS 545..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..601
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..635
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 36..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 73..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 99..133
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 103..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT VARIANT 4
FT /note="T -> S (in dbSNP:rs140115204)"
FT /evidence="ECO:0000269|PubMed:22045688"
FT /id="VAR_066960"
FT VARIANT 199
FT /note="L -> M (in dbSNP:rs757589666)"
FT /evidence="ECO:0000269|PubMed:22045688"
FT /id="VAR_066961"
FT VARIANT 545
FT /note="I -> V (in dbSNP:rs199839949)"
FT /evidence="ECO:0000269|PubMed:22045688"
FT /id="VAR_066962"
FT CONFLICT 127
FT /note="C -> R (in Ref. 4; BAF84169)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="I -> V (in Ref. 4; BAF84169)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="T -> A (in Ref. 4; BAF84169)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 666 AA; 76263 MW; 46D7C46E21160215 CRC64;
MAMTWIVFSL WPLTVFMGHI GGHSLFSCEP ITLRMCQDLP YNTTFMPNLL NHYDQQTAAL
AMEPFHPMVN LDCSRDFRPF LCALYAPICM EYGRVTLPCR RLCQRAYSEC SKLMEMFGVP
WPEDMECSRF PDCDEPYPRL VDLNLAGEPT EGAPVAVQRD YGFWCPRELK IDPDLGYSFL
HVRDCSPPCP NMYFRREELS FARYFIGLIS IICLSATLFT FLTFLIDVTR FRYPERPIIF
YAVCYMMVSL IFFIGFLLED RVACNASIPA QYKASTVTQG SHNKACTMLF MILYFFTMAG
SVWWVILTIT WFLAAVPKWG SEAIEKKALL FHASAWGIPG TLTIILLAMN KIEGDNISGV
CFVGLYDVDA LRYFVLAPLC LYVVVGVSLL LAGIISLNRV RIEIPLEKEN QDKLVKFMIR
IGVFSILYLV PLLVVIGCYF YEQAYRGIWE TTWIQERCRE YHIPCPYQVT QMSRPDLILF
LMKYLMALIV GIPSVFWVGS KKTCFEWASF FHGRRKKEIV NESRQVLQEP DFAQSLLRDP
NTPIIRKSRG TSTQGTSTHA SSTQLAMVDD QRSKAGSIHS KVSSYHGSLH RSRDGRYTPC
SYRGMEERLP HGSMSRLTDH SRHSSSHRLN EQSRHSSIRD LSNNPMTHIT HGTSMNRVIE
EDGTSA
