FLVC2_HUMAN
ID FLVC2_HUMAN Reviewed; 526 AA.
AC Q9UPI3; B7Z485; Q53ZT9; Q96JY3; Q9NX90;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Feline leukemia virus subgroup C receptor-related protein 2;
DE AltName: Full=Calcium-chelate transporter;
DE Short=CCT;
GN Name=FLVCR2; Synonyms=C14orf58;
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] (ISOFORM 1), AND CHARACTERIZATION.
RC TISSUE=Pituitary;
RX PubMed=14729055; DOI=10.1016/j.yexcr.2003.10.002;
RA Brasier G., Tikellis C., Xuereb L., Craigie J., Casley D., Kovacs C.S.,
RA Fudge N.J., Kalnins R., Cooper M.E., Wookey P.J.;
RT "Novel hexad repeats conserved in a putative transporter with restricted
RT expression in cell types associated with growth, calcium exchange and
RT homeostasis.";
RL Exp. Cell Res. 293:31-42(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Brown J., Pirani H., Tailor C.S.;
RT "An aspartic acid in the presumptive extracellular loop six of subgroup C
RT feline leukemia virus receptor FLVCR1 is involved in virus infection.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ALA-16.
RC TISSUE=Placenta, and Umbilical cord blood;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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 [7]
RP FUNCTION.
RX PubMed=20823265; DOI=10.1128/mcb.00690-10;
RA Duffy S.P., Shing J., Saraon P., Berger L.C., Eiden M.V., Wilde A.,
RA Tailor C.S.;
RT "The Fowler syndrome-associated protein FLVCR2 is an importer of heme.";
RL Mol. Cell. Biol. 30:5318-5324(2010).
RN [8]
RP VARIANTS PVHH ARG-280; VAL-398 AND ARG-430.
RX PubMed=20206334; DOI=10.1016/j.ajhg.2010.02.004;
RA Meyer E., Ricketts C., Morgan N.V., Morris M.R., Pasha S., Tee L.J.,
RA Rahman F., Bazin A., Bessieres B., Dechelotte P., Yacoubi M.T.,
RA Al-Adnani M., Marton T., Tannahill D., Trembath R.C., Fallet-Bianco C.,
RA Cox P., Williams D., Maher E.R.;
RT "Mutations in FLVCR2 are associated with proliferative vasculopathy and
RT hydranencephaly-hydrocephaly syndrome (Fowler syndrome).";
RL Am. J. Hum. Genet. 86:471-478(2010).
RN [9]
RP VARIANTS PVHH 110-ASN--PHE-112 DELINS ILE; VAL-326 AND VAL-398.
RX PubMed=20518025; DOI=10.1002/humu.21293;
RA Lalonde E., Albrecht S., Ha K.C., Jacob K., Bolduc N., Polychronakos C.,
RA Dechelotte P., Majewski J., Jabado N.;
RT "Unexpected allelic heterogeneity and spectrum of mutations in Fowler
RT syndrome revealed by next-generation exome sequencing.";
RL Hum. Mutat. 31:918-923(2010).
RN [10]
RP VARIANTS PVHH HIS-84; ARG-352; VAL-398; ARG-412 AND MET-430.
RX PubMed=20690116; DOI=10.1002/humu.21329;
RA Thomas S., Encha-Razavi F., Devisme L., Etchevers H.,
RA Bessieres-Grattagliano B., Goudefroye G., Elkhartoufi N., Pateau E.,
RA Ichkou A., Bonniere M., Marcorelle P., Parent P., Manouvrier S., Holder M.,
RA Laquerriere A., Loeuillet L., Roume J., Martinovic J., Mougou-Zerelli S.,
RA Gonzales M., Meyer V., Wessner M., Feysot C.B., Nitschke P., Leticee N.,
RA Munnich A., Lyonnet S., Wookey P., Gyapay G., Foliguet B., Vekemans M.,
RA Attie-Bitach T.;
RT "High-throughput sequencing of a 4.1 Mb linkage interval reveals FLVCR2
RT deletions and mutations in lethal cerebral vasculopathy.";
RL Hum. Mutat. 31:1134-1141(2010).
CC -!- FUNCTION: Acts as an importer of heme. Also acts as a transporter for a
CC calcium-chelator complex, important for growth and calcium metabolism.
CC {ECO:0000269|PubMed:20823265}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UPI3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UPI3-2; Sequence=VSP_043048, VSP_043049;
CC -!- TISSUE SPECIFICITY: Expressed in non-hematopoietic tissues, with
CC relative abundant expression in brain, placenta, lung, liver and
CC kidney. Also expressed in hematopoietic tissues (fetal liver, spleen,
CC lymph node, thymus, leukocytes and bone marrow). Found in acidophil
CC cells of the pituitary that secrete growth hormone and prolactin.
CC -!- DISEASE: Proliferative vasculopathy and hydranencephaly-hydrocephaly
CC syndrome (PVHH) [MIM:225790]: A rare prenatally lethal disorder
CC characterized by hydranencephaly, a distinctive glomerular vasculopathy
CC in the central nervous system and retina, and diffuse ischemic lesions
CC of the brain stem, basal ganglia, and spinal cord with calcifications.
CC Hydranencephaly is a condition where the greater portions of the
CC cerebral hemispheres and corpus striatum are replaced by cerebrospinal
CC fluid and glial tissue. {ECO:0000269|PubMed:20206334,
CC ECO:0000269|PubMed:20518025, ECO:0000269|PubMed:20690116}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Feline
CC leukemia virus subgroup C receptor (TC 2.A.1.28.1) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55381.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY260572; AAP86633.1; -; mRNA.
DR EMBL; AY260577; AAP86638.1; -; mRNA.
DR EMBL; AF456126; AAO15528.1; -; mRNA.
DR EMBL; AK000378; BAA91126.1; -; mRNA.
DR EMBL; AK027804; BAB55381.1; ALT_INIT; mRNA.
DR EMBL; AK297002; BAH12471.1; -; mRNA.
DR EMBL; AC007182; AAD51374.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW81235.1; -; Genomic_DNA.
DR EMBL; BC019087; AAH19087.1; -; mRNA.
DR CCDS; CCDS55933.1; -. [Q9UPI3-2]
DR CCDS; CCDS9844.1; -. [Q9UPI3-1]
DR RefSeq; NP_001182212.1; NM_001195283.1. [Q9UPI3-2]
DR RefSeq; NP_060261.2; NM_017791.2. [Q9UPI3-1]
DR AlphaFoldDB; Q9UPI3; -.
DR SMR; Q9UPI3; -.
DR BioGRID; 120777; 30.
DR IntAct; Q9UPI3; 3.
DR STRING; 9606.ENSP00000238667; -.
DR TCDB; 2.A.1.28.4; the major facilitator superfamily (mfs).
DR iPTMnet; Q9UPI3; -.
DR PhosphoSitePlus; Q9UPI3; -.
DR BioMuta; FLVCR2; -.
DR DMDM; 46396034; -.
DR jPOST; Q9UPI3; -.
DR MassIVE; Q9UPI3; -.
DR MaxQB; Q9UPI3; -.
DR PaxDb; Q9UPI3; -.
DR PeptideAtlas; Q9UPI3; -.
DR PRIDE; Q9UPI3; -.
DR ProteomicsDB; 85372; -. [Q9UPI3-1]
DR ProteomicsDB; 85373; -. [Q9UPI3-2]
DR Antibodypedia; 51434; 130 antibodies from 22 providers.
DR DNASU; 55640; -.
DR Ensembl; ENST00000238667.9; ENSP00000238667.4; ENSG00000119686.10. [Q9UPI3-1]
DR Ensembl; ENST00000539311.5; ENSP00000443439.1; ENSG00000119686.10. [Q9UPI3-2]
DR GeneID; 55640; -.
DR KEGG; hsa:55640; -.
DR MANE-Select; ENST00000238667.9; ENSP00000238667.4; NM_017791.3; NP_060261.2.
DR UCSC; uc001xrs.3; human. [Q9UPI3-1]
DR CTD; 55640; -.
DR DisGeNET; 55640; -.
DR GeneCards; FLVCR2; -.
DR HGNC; HGNC:20105; FLVCR2.
DR HPA; ENSG00000119686; Low tissue specificity.
DR MalaCards; FLVCR2; -.
DR MIM; 225790; phenotype.
DR MIM; 610865; gene.
DR neXtProt; NX_Q9UPI3; -.
DR OpenTargets; ENSG00000119686; -.
DR Orphanet; 221126; Fowler vasculopaty.
DR PharmGKB; PA162388720; -.
DR VEuPathDB; HostDB:ENSG00000119686; -.
DR eggNOG; KOG2563; Eukaryota.
DR GeneTree; ENSGT01030000234625; -.
DR HOGENOM; CLU_023132_0_1_1; -.
DR InParanoid; Q9UPI3; -.
DR OMA; AINWMST; -.
DR OrthoDB; 702737at2759; -.
DR PhylomeDB; Q9UPI3; -.
DR TreeFam; TF314292; -.
DR PathwayCommons; Q9UPI3; -.
DR SignaLink; Q9UPI3; -.
DR BioGRID-ORCS; 55640; 29 hits in 1071 CRISPR screens.
DR ChiTaRS; FLVCR2; human.
DR GenomeRNAi; 55640; -.
DR Pharos; Q9UPI3; Tbio.
DR PRO; PR:Q9UPI3; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9UPI3; protein.
DR Bgee; ENSG00000119686; Expressed in secondary oocyte and 134 other tissues.
DR ExpressionAtlas; Q9UPI3; baseline and differential.
DR Genevisible; Q9UPI3; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR GO; GO:0015232; F:heme transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0097037; P:heme export; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disease variant; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..526
FT /note="Feline leukemia virus subgroup C receptor-related
FT protein 2"
FT /id="PRO_0000084846"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..491
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 25..30
FT /note="1"
FT REPEAT 31..36
FT /note="2"
FT REPEAT 37..42
FT /note="3"
FT REPEAT 43..48
FT /note="4"
FT REPEAT 49..54
FT /note="5"
FT REPEAT 55..60
FT /note="6; approximate"
FT REPEAT 61..66
FT /note="7; approximate"
FT REPEAT 67..72
FT /note="8"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 25..72
FT /note="8 X 6 AA tandem repeats of P-S-[VS]-S-[VIAG]-[HNP]"
FT REGION 500..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91X85"
FT VAR_SEQ 1..18
FT /note="MVNEGPNQEESDDTPVPE -> MSADNSSTICVCRSVRQE (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043048"
FT VAR_SEQ 19..223
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043049"
FT VARIANT 16
FT /note="V -> A (in dbSNP:rs2287015)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_018271"
FT VARIANT 84
FT /note="R -> H (in PVHH)"
FT /evidence="ECO:0000269|PubMed:20690116"
FT /id="VAR_064410"
FT VARIANT 110..112
FT /note="NIF -> I (in PVHH)"
FT /evidence="ECO:0000269|PubMed:20518025"
FT /id="VAR_064411"
FT VARIANT 280
FT /note="P -> R (in PVHH; dbSNP:rs267606823)"
FT /evidence="ECO:0000269|PubMed:20206334"
FT /id="VAR_064043"
FT VARIANT 326
FT /note="A -> V (in PVHH; dbSNP:rs267606824)"
FT /evidence="ECO:0000269|PubMed:20518025"
FT /id="VAR_064412"
FT VARIANT 352
FT /note="T -> R (in PVHH)"
FT /evidence="ECO:0000269|PubMed:20690116"
FT /id="VAR_064413"
FT VARIANT 398
FT /note="L -> V (in PVHH; dbSNP:rs267606822)"
FT /evidence="ECO:0000269|PubMed:20206334,
FT ECO:0000269|PubMed:20518025, ECO:0000269|PubMed:20690116"
FT /id="VAR_064044"
FT VARIANT 412
FT /note="G -> R (in PVHH)"
FT /evidence="ECO:0000269|PubMed:20690116"
FT /id="VAR_064414"
FT VARIANT 430
FT /note="T -> M (in PVHH; dbSNP:rs267606825)"
FT /evidence="ECO:0000269|PubMed:20690116"
FT /id="VAR_064415"
FT VARIANT 430
FT /note="T -> R (in PVHH; dbSNP:rs267606825)"
FT /evidence="ECO:0000269|PubMed:20206334"
FT /id="VAR_064045"
FT VARIANT 481
FT /note="A -> T (in dbSNP:rs35126362)"
FT /id="VAR_050299"
FT CONFLICT 419
FT /note="L -> H (in Ref. 3; BAB55381)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="S -> F (in Ref. 3; BAA91126)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 526 AA; 57241 MW; D233C07350B17870 CRC64;
MVNEGPNQEE SDDTPVPESA LQADPSVSVH PSVSVHPSVS INPSVSVHPS SSAHPSALAQ
PSGLAHPSSS GPEDLSVIKV SRRRWAVVLV FSCYSMCNSF QWIQYGSINN IFMHFYGVSA
FAIDWLSMCY MLTYIPLLLP VAWLLEKFGL RTIALTGSAL NCLGAWVKLG SLKPHLFPVT
VVGQLICSVA QVFILGMPSR IASVWFGANE VSTACSVAVF GNQLGIAIGF LVPPVLVPNI
EDRDELAYHI SIMFYIIGGV ATLLLILVII VFKEKPKYPP SRAQSLSYAL TSPDASYLGS
IARLFKNLNF VLLVITYGLN AGAFYALSTL LNRMVIWHYP GEEVNAGRIG LTIVIAGMLG
AVISGIWLDR SKTYKETTLV VYIMTLVGMV VYTFTLNLGH LWVVFITAGT MGFFMTGYLP
LGFEFAVELT YPESEGISSG LLNISAQVFG IIFTISQGQI IDNYGTKPGN IFLCVFLTLG
AALTAFIKAD LRRQKANKET LENKLQEEEE ESNTSKVPTA VSEDHL