S7A14_HUMAN
ID S7A14_HUMAN Reviewed; 771 AA.
AC Q8TBB6; B3KV33; Q9HCF9;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Probable cationic amino acid transporter;
DE AltName: Full=Solute carrier family 7 member 14;
GN Name=SLC7A14; Synonyms=KIAA1613;
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 MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-771.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-771.
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=22787143; DOI=10.1074/jbc.m112.350322;
RA Jaenecke I., Boissel J.P., Lemke M., Rupp J., Gasnier B., Closs E.I.;
RT "A chimera carrying the functional domain of the orphan protein SLC7A14 in
RT the backbone of SLC7A2 mediates trans-stimulated arginine transport.";
RL J. Biol. Chem. 287:30853-30860(2012).
RN [6]
RP VARIANTS RP68 VAL-132; SER-209; ILE-323; ARG-330; LEU-391; PHE-464; CYS-695
RP AND VAL-708, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24670872; DOI=10.1038/ncomms4517;
RA Jin Z.B., Huang X.F., Lv J.N., Xiang L., Li D.Q., Chen J., Huang C., Wu J.,
RA Lu F., Qu J.;
RT "SLC7A14 linked to autosomal recessive retinitis pigmentosa.";
RL Nat. Commun. 5:3517-3517(2014).
CC -!- FUNCTION: May be involved in arginine transport.
CC {ECO:0000269|PubMed:22787143, ECO:0000269|PubMed:24670872}.
CC -!- INTERACTION:
CC Q8TBB6; Q9ULC5: ACSL5; NbExp=3; IntAct=EBI-5235586, EBI-2876927;
CC Q8TBB6; Q9UHX3: ADGRE2; NbExp=3; IntAct=EBI-5235586, EBI-11277970;
CC Q8TBB6; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-5235586, EBI-11522760;
CC Q8TBB6; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-5235586, EBI-11957045;
CC Q8TBB6; O95236-2: APOL3; NbExp=3; IntAct=EBI-5235586, EBI-11976321;
CC Q8TBB6; O15155: BET1; NbExp=3; IntAct=EBI-5235586, EBI-749204;
CC Q8TBB6; Q12981: BNIP1; NbExp=3; IntAct=EBI-5235586, EBI-4402847;
CC Q8TBB6; Q12982: BNIP2; NbExp=3; IntAct=EBI-5235586, EBI-752094;
CC Q8TBB6; P27352: CBLIF; NbExp=3; IntAct=EBI-5235586, EBI-3953638;
CC Q8TBB6; Q9P0B6: CCDC167; NbExp=3; IntAct=EBI-5235586, EBI-9083477;
CC Q8TBB6; Q8NHW4: CCL4L2; NbExp=3; IntAct=EBI-5235586, EBI-10271156;
CC Q8TBB6; P19397: CD53; NbExp=3; IntAct=EBI-5235586, EBI-6657396;
CC Q8TBB6; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-5235586, EBI-11522780;
CC Q8TBB6; Q96PD2-2: DCBLD2; NbExp=3; IntAct=EBI-5235586, EBI-12135455;
CC Q8TBB6; Q9BUN8: DERL1; NbExp=3; IntAct=EBI-5235586, EBI-398977;
CC Q8TBB6; Q5NDL2-3: EOGT; NbExp=3; IntAct=EBI-5235586, EBI-13052900;
CC Q8TBB6; Q7Z2K6: ERMP1; NbExp=3; IntAct=EBI-5235586, EBI-10976398;
CC Q8TBB6; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-5235586, EBI-18304435;
CC Q8TBB6; O75063: FAM20B; NbExp=3; IntAct=EBI-5235586, EBI-11090967;
CC Q8TBB6; Q969F0: FATE1; NbExp=3; IntAct=EBI-5235586, EBI-743099;
CC Q8TBB6; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-5235586, EBI-3918971;
CC Q8TBB6; Q13651: IL10RA; NbExp=3; IntAct=EBI-5235586, EBI-1031656;
CC Q8TBB6; Q16873: LTC4S; NbExp=3; IntAct=EBI-5235586, EBI-12241118;
CC Q8TBB6; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-5235586, EBI-11956541;
CC Q8TBB6; A0A0C4DFN3: MGLL; NbExp=3; IntAct=EBI-5235586, EBI-12866138;
CC Q8TBB6; Q8N4V1: MMGT1; NbExp=3; IntAct=EBI-5235586, EBI-6163737;
CC Q8TBB6; Q9NZG7: NINJ2; NbExp=3; IntAct=EBI-5235586, EBI-10317425;
CC Q8TBB6; P42857: NSG1; NbExp=3; IntAct=EBI-5235586, EBI-6380741;
CC Q8TBB6; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-5235586, EBI-11721828;
CC Q8TBB6; A5D903: PRB1; NbExp=3; IntAct=EBI-5235586, EBI-10173935;
CC Q8TBB6; Q14162: SCARF1; NbExp=3; IntAct=EBI-5235586, EBI-12056025;
CC Q8TBB6; O00767: SCD; NbExp=3; IntAct=EBI-5235586, EBI-2684237;
CC Q8TBB6; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-5235586, EBI-8640191;
CC Q8TBB6; Q9NZ01: TECR; NbExp=3; IntAct=EBI-5235586, EBI-2877718;
CC Q8TBB6; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-5235586, EBI-10694905;
CC Q8TBB6; Q9NSU2-1: TREX1; NbExp=3; IntAct=EBI-5235586, EBI-16746122;
CC Q8TBB6; A5PKU2: TUSC5; NbExp=3; IntAct=EBI-5235586, EBI-11988865;
CC Q8TBB6; Q9Y5Z9: UBIAD1; NbExp=3; IntAct=EBI-5235586, EBI-2819725;
CC Q8TBB6; P63027: VAMP2; NbExp=3; IntAct=EBI-5235586, EBI-520113;
CC Q8TBB6; Q9BQB6: VKORC1; NbExp=3; IntAct=EBI-5235586, EBI-6256462;
CC Q8TBB6; Q9BSR8: YIPF4; NbExp=3; IntAct=EBI-5235586, EBI-751253;
CC Q8TBB6; Q96EC8: YIPF6; NbExp=3; IntAct=EBI-5235586, EBI-751210;
CC Q8TBB6; O95159: ZFPL1; NbExp=3; IntAct=EBI-5235586, EBI-718439;
CC -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:22787143,
CC ECO:0000269|PubMed:24670872}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22787143, ECO:0000269|PubMed:24670872}.
CC Note=Exhibits a punctated pattern in the cytoplasm, which partially
CC ovelaps with lysosomes.
CC -!- TISSUE SPECIFICITY: Expressed in skin fibroblasts.
CC {ECO:0000269|PubMed:22787143}.
CC -!- DISEASE: Retinitis pigmentosa 68 (RP68) [MIM:615725]: A retinal
CC dystrophy belonging to the group of pigmentary retinopathies. Retinitis
CC pigmentosa is characterized by retinal pigment deposits visible on
CC fundus examination and primary loss of rod photoreceptor cells followed
CC by secondary loss of cone photoreceptors. Patients typically have night
CC vision blindness and loss of midperipheral visual field. As their
CC condition progresses, they lose their far peripheral visual field and
CC eventually central vision as well. {ECO:0000269|PubMed:24670872}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. Cationic amino acid transporter (CAT) (TC 2.A.3.3) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13439.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122655; BAG53645.1; -; mRNA.
DR EMBL; AC008041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022968; AAH22968.2; -; mRNA.
DR EMBL; AB046833; BAB13439.1; ALT_SEQ; mRNA.
DR CCDS; CCDS33892.1; -.
DR RefSeq; NP_066000.2; NM_020949.2.
DR AlphaFoldDB; Q8TBB6; -.
DR SMR; Q8TBB6; -.
DR BioGRID; 121733; 76.
DR IntAct; Q8TBB6; 44.
DR STRING; 9606.ENSP00000231706; -.
DR TCDB; 2.A.3.3.7; the amino acid-polyamine-organocation (apc) family.
DR GlyGen; Q8TBB6; 2 sites.
DR iPTMnet; Q8TBB6; -.
DR PhosphoSitePlus; Q8TBB6; -.
DR BioMuta; SLC7A14; -.
DR DMDM; 296452968; -.
DR jPOST; Q8TBB6; -.
DR MassIVE; Q8TBB6; -.
DR PaxDb; Q8TBB6; -.
DR PeptideAtlas; Q8TBB6; -.
DR PRIDE; Q8TBB6; -.
DR ProteomicsDB; 73987; -.
DR Antibodypedia; 18672; 58 antibodies from 18 providers.
DR DNASU; 57709; -.
DR Ensembl; ENST00000231706.6; ENSP00000231706.4; ENSG00000013293.6.
DR GeneID; 57709; -.
DR KEGG; hsa:57709; -.
DR MANE-Select; ENST00000231706.6; ENSP00000231706.4; NM_020949.3; NP_066000.2.
DR UCSC; uc003fgz.3; human.
DR CTD; 57709; -.
DR DisGeNET; 57709; -.
DR GeneCards; SLC7A14; -.
DR HGNC; HGNC:29326; SLC7A14.
DR HPA; ENSG00000013293; Group enriched (brain, pituitary gland, retina).
DR MalaCards; SLC7A14; -.
DR MIM; 615720; gene.
DR MIM; 615725; phenotype.
DR neXtProt; NX_Q8TBB6; -.
DR OpenTargets; ENSG00000013293; -.
DR Orphanet; 791; Retinitis pigmentosa.
DR PharmGKB; PA142670913; -.
DR VEuPathDB; HostDB:ENSG00000013293; -.
DR eggNOG; KOG1286; Eukaryota.
DR GeneTree; ENSGT00940000155893; -.
DR HOGENOM; CLU_007946_15_7_1; -.
DR InParanoid; Q8TBB6; -.
DR OMA; KEACSPG; -.
DR OrthoDB; 439017at2759; -.
DR PhylomeDB; Q8TBB6; -.
DR TreeFam; TF315212; -.
DR PathwayCommons; Q8TBB6; -.
DR SignaLink; Q8TBB6; -.
DR BioGRID-ORCS; 57709; 7 hits in 1067 CRISPR screens.
DR ChiTaRS; SLC7A14; human.
DR GenomeRNAi; 57709; -.
DR Pharos; Q8TBB6; Tbio.
DR PRO; PR:Q8TBB6; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q8TBB6; protein.
DR Bgee; ENSG00000013293; Expressed in cerebellar vermis and 106 other tissues.
DR Genevisible; Q8TBB6; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006865; P:amino acid transport; IBA:GO_Central.
DR InterPro; IPR002293; AA/rel_permease1.
DR InterPro; IPR029485; CAT_C.
DR Pfam; PF13520; AA_permease_2; 1.
DR Pfam; PF13906; AA_permease_C; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Glycoprotein; Lysosome; Membrane; Phosphoprotein;
KW Reference proteome; Retinitis pigmentosa; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..771
FT /note="Probable cationic amino acid transporter"
FT /id="PRO_0000307360"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 216..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 360..380
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..585
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 596..616
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 628..648
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..675
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 736..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BXR1"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BXR1"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BXR1"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BXR1"
FT MOD_RES 769
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BXR1"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 132
FT /note="A -> V (in RP68; dbSNP:rs587777273)"
FT /evidence="ECO:0000269|PubMed:24670872"
FT /id="VAR_071050"
FT VARIANT 209
FT /note="N -> S (in RP68; uncertain pathological
FT significance; dbSNP:rs765054383)"
FT /evidence="ECO:0000269|PubMed:24670872"
FT /id="VAR_071051"
FT VARIANT 323
FT /note="M -> I (in RP68; uncertain pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:24670872"
FT /id="VAR_071052"
FT VARIANT 330
FT /note="G -> R (in RP68; affects subcellular location;
FT dbSNP:rs2276717)"
FT /evidence="ECO:0000269|PubMed:24670872"
FT /id="VAR_035417"
FT VARIANT 391
FT /note="S -> L (in RP68; uncertain pathological
FT significance; dbSNP:rs375705180)"
FT /evidence="ECO:0000269|PubMed:24670872"
FT /id="VAR_071053"
FT VARIANT 464
FT /note="C -> F (in RP68; dbSNP:rs79668755)"
FT /evidence="ECO:0000269|PubMed:24670872"
FT /id="VAR_071054"
FT VARIANT 695
FT /note="R -> C (in RP68; uncertain pathological
FT significance; dbSNP:rs181011740)"
FT /evidence="ECO:0000269|PubMed:24670872"
FT /id="VAR_071055"
FT VARIANT 708
FT /note="F -> V (in RP68; dbSNP:rs587777272)"
FT /evidence="ECO:0000269|PubMed:24670872"
FT /id="VAR_071056"
FT CONFLICT 498
FT /note="K -> R (in Ref. 1; BAG53645)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 771 AA; 84052 MW; 55F490AE219B3342 CRC64;
MSGFFTSLDP RRVQWGAAWY AMHSRILRTK PVESMLEGTG TTTAHGTKLA QVLTTVDLIS
LGVGSCVGTG MYVVSGLVAK EMAGPGVIVS FIIAAVASIL SGVCYAEFGV RVPKTTGSAY
TYSYVTVGEF VAFFIGWNLI LEYLIGTAAG ASALSSMFDS LANHTISRWM ADSVGTLNGL
GKGEESYPDL LALLIAVIVT IIVALGVKNS IGFNNVLNVL NLAVWVFIMI AGLFFINGKY
WAEGQFLPHG WSGVLQGAAT CFYAFIGFDI IATTGEEAKN PNTSIPYAIT ASLVICLTAY
VSVSVILTLM VPYYTIDTES PLMEMFVAHG FYAAKFVVAI GSVAGLTVSL LGSLFPMPRV
IYAMAGDGLL FRFLAHVSSY TETPVVACIV SGFLAALLAL LVSLRDLIEM MSIGTLLAYT
LVSVCVLLLR YQPESDIDGF VKFLSEEHTK KKEGILADCE KEACSPVSEG DEFSGPATNT
CGAKNLPSLG DNEMLIGKSD KSTYNVNHPN YGTVDMTTGI EADESENIYL IKLKKLIGPH
YYTMRIRLGL PGKMDRPTAA TGHTVTICVL LLFILMFIFC SFIIFGSDYI SEQSWWAILL
VVLMVLLIST LVFVILQQPE NPKKLPYMAP CLPFVPAFAM LVNIYLMLKL STITWIRFAV
WCFVGLLIYF GYGIWNSTLE ISAREEALHQ STYQRYDVDD PFSVEEGFSY ATEGESQEDW
GGPTEDKGFY YQQMSDAKAN GRTSSKAKSK SKHKQNSEAL IANDELDYSP E
