ID   S22AE_HUMAN             Reviewed;         594 AA.
AC   Q9Y267; A0AVS9; A1L4H6; B2RCX3; Q6DJT3;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 4.
DT   24-JAN-2024, entry version 154.
DE   RecName: Full=Solute carrier family 22 member 14 {ECO:0000303|PubMed:33882315};
DE   AltName: Full=Organic cation transporter-like 4 {ECO:0000303|PubMed:10072596};
DE            Short=ORCTL-4 {ECO:0000303|PubMed:10072596};
GN   Name=SLC22A14 {ECO:0000303|PubMed:33882315,
GN   ECO:0000312|HGNC:HGNC:8495};
GN   Synonyms=OCTL2 {ECO:0000303|PubMed:10231028}, ORCTL4
GN   {ECO:0000303|PubMed:10072596};
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], TISSUE SPECIFICITY, AND VARIANTS THR-144;
RP   MET-284 AND GLY-292.
RX   PubMed=10072596; DOI=10.1159/000015197;
RA   Nishiwaki T., Daigo Y., Tamari M., Fujii Y., Nakamura Y.;
RT   "Molecular cloning, mapping, and characterization of two novel human genes,
RT   ORCTL3 and ORCTL4, bearing homology to organic-cation transporters.";
RL   Cytogenet. Cell Genet. 83:251-255(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-144; MET-284 AND
RP   GLY-292.
RX   PubMed=10231028; DOI=10.1093/dnares/6.1.37;
RA   Daigo Y., Isomura M., Nishiwaki T., Tamari M., Ishikawa S., Kai M.,
RA   Takeuchi K., Yamane Y., Hayashi R., Minami M., Fujino M.A., Hojo Y.,
RA   Uchiyama I., Takagi T., Nakamura Y.;
RT   "Characterization of a 1200-kb genomic segment of chromosome 3p22-p21.3.";
RL   DNA Res. 6:37-44(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS MET-284; GLY-292 AND
RP   ARG-560.
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).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS MET-284 AND
RP   GLY-292.
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], AND VARIANTS MET-284; GLY-292 AND
RP   ARG-560.
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   [7]
RP   TRANSPORTER ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-388;
RP   TYR-395 AND ARG-487.
RX   PubMed=33882315; DOI=10.1016/j.celrep.2021.109025;
RA   Kuang W., Zhang J., Lan Z., Deepak R.N.V.K., Liu C., Ma Z., Cheng L.,
RA   Zhao X., Meng X., Wang W., Wang X., Xu L., Jiao Y., Luo Q., Meng Z.,
RA   Kee K., Liu X., Deng H., Li W., Fan H., Chen L.;
RT   "SLC22A14 is a mitochondrial riboflavin transporter required for sperm
RT   oxidative phosphorylation and male fertility.";
RL   Cell Rep. 35:109025-109025(2021).
CC   -!- FUNCTION: Riboflavin transporter localized at the inner mitochondrial
CC       membrane of the spermatozoa midpiece, which is required for male
CC       fertility (By similarity). SLC22A14-mediated riboflavin transport is
CC       essential for spermatozoa energy generation and motility: riboflavin is
CC       the precursor of FMN and FAD, which are coenzymes of many enzymes in
CC       the TCA cycle (the citric acid cycle) in mitochondria (By similarity).
CC       Required for sperm motility and normal sperm flagellar structure (By
CC       similarity). {ECO:0000250|UniProtKB:Q497L9}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=riboflavin(in) = riboflavin(out); Xref=Rhea:RHEA:35015,
CC         ChEBI:CHEBI:57986; Evidence={ECO:0000269|PubMed:33882315};
CC   -!- INTERACTION:
CC       Q9Y267; Q96HJ5: MS4A3; NbExp=4; IntAct=EBI-12824155, EBI-12806656;
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:33882315}; Multi-pass membrane protein
CC       {ECO:0000255}. Cell projection, cilium, flagellum membrane
CC       {ECO:0000250|UniProtKB:Q497L9}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Localizes to the principle piece of the sperm tail.
CC       {ECO:0000250|UniProtKB:Q497L9}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10072596}.
CC   -!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily.
CC       Organic cation transporter (TC 2.A.1.19) family. {ECO:0000305}.
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DR   EMBL; AB011082; BAA76351.1; -; mRNA.
DR   EMBL; AB026898; BAA77626.1; -; Genomic_DNA.
DR   EMBL; AK315317; BAG37720.1; -; mRNA.
DR   EMBL; AP006193; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471055; EAW64529.1; -; Genomic_DNA.
DR   EMBL; BC075070; AAH75070.1; -; mRNA.
DR   EMBL; BC075071; AAH75071.1; -; mRNA.
DR   EMBL; BC126482; AAI26483.1; -; mRNA.
DR   EMBL; BC130543; AAI30544.1; -; mRNA.
DR   CCDS; CCDS2677.1; -.
DR   RefSeq; NP_001306962.1; NM_001320033.1.
DR   RefSeq; NP_004794.2; NM_004803.4.
DR   RefSeq; XP_005265642.1; XM_005265585.4.
DR   RefSeq; XP_011532547.1; XM_011534245.2.
DR   AlphaFoldDB; Q9Y267; -.
DR   SMR; Q9Y267; -.
DR   BioGRID; 114789; 7.
DR   IntAct; Q9Y267; 2.
DR   STRING; 9606.ENSP00000273173; -.
DR   TCDB; 2.A.1.19.22; the major facilitator superfamily (mfs).
DR   GlyCosmos; Q9Y267; 4 sites, No reported glycans.
DR   GlyGen; Q9Y267; 4 sites.
DR   iPTMnet; Q9Y267; -.
DR   PhosphoSitePlus; Q9Y267; -.
DR   BioMuta; SLC22A14; -.
DR   DMDM; 313104317; -.
DR   MassIVE; Q9Y267; -.
DR   PaxDb; 9606-ENSP00000273173; -.
DR   PeptideAtlas; Q9Y267; -.
DR   ProteomicsDB; 85672; -.
DR   Antibodypedia; 28576; 73 antibodies from 13 providers.
DR   DNASU; 9389; -.
DR   Ensembl; ENST00000273173.4; ENSP00000273173.4; ENSG00000144671.11.
DR   Ensembl; ENST00000448498.6; ENSP00000396283.1; ENSG00000144671.11.
DR   GeneID; 9389; -.
DR   KEGG; hsa:9389; -.
DR   MANE-Select; ENST00000448498.6; ENSP00000396283.1; NM_001320033.2; NP_001306962.1.
DR   UCSC; uc003cib.3; human.
DR   AGR; HGNC:8495; -.
DR   CTD; 9389; -.
DR   GeneCards; SLC22A14; -.
DR   HGNC; HGNC:8495; SLC22A14.
DR   HPA; ENSG00000144671; Tissue enriched (testis).
DR   MIM; 604048; gene.
DR   neXtProt; NX_Q9Y267; -.
DR   OpenTargets; ENSG00000144671; -.
DR   PharmGKB; PA32815; -.
DR   VEuPathDB; HostDB:ENSG00000144671; -.
DR   eggNOG; KOG0255; Eukaryota.
DR   GeneTree; ENSGT00940000162395; -.
DR   HOGENOM; CLU_001265_33_3_1; -.
DR   InParanoid; Q9Y267; -.
DR   OMA; PGIMEVP; -.
DR   OrthoDB; 2088942at2759; -.
DR   PhylomeDB; Q9Y267; -.
DR   TreeFam; TF315847; -.
DR   PathwayCommons; Q9Y267; -.
DR   SignaLink; Q9Y267; -.
DR   BioGRID-ORCS; 9389; 10 hits in 1136 CRISPR screens.
DR   GenomeRNAi; 9389; -.
DR   Pharos; Q9Y267; Tdark.
DR   PRO; PR:Q9Y267; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9Y267; Protein.
DR   Bgee; ENSG00000144671; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 114 other cell types or tissues.
DR   ExpressionAtlas; Q9Y267; baseline and differential.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0097228; C:sperm principal piece; IEA:Ensembl.
DR   GO; GO:0032217; F:riboflavin transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
DR   GO; GO:0048240; P:sperm capacitation; IEA:Ensembl.
DR   CDD; cd17374; MFS_OAT; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR005828; MFS_sugar_transport-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   PANTHER; PTHR24064; SOLUTE CARRIER FAMILY 22 MEMBER; 1.
DR   PANTHER; PTHR24064:SF48; SOLUTE CARRIER FAMILY 22 MEMBER 14; 1.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   Genevisible; Q9Y267; HS.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Cilium; Flagellum; Glycoprotein; Membrane;
KW   Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..594
FT                   /note="Solute carrier family 22 member 14"
FT                   /id="PRO_0000230784"
FT   TOPO_DOM        1..70
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        92..184
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        206..210
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        211..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        232..235
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        257..270
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        292..297
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        298..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        319..379
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        401..408
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        409..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        432..437
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        438..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        459..488
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        489..509
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        510..512
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        513..533
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        534..538
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        539..559
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        560..594
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          566..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..594
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        125
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        150
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         108
FT                   /note="P -> H (in dbSNP:rs9847584)"
FT                   /id="VAR_055108"
FT   VARIANT         112
FT                   /note="K -> E (in dbSNP:rs2073714)"
FT                   /id="VAR_055109"
FT   VARIANT         144
FT                   /note="I -> T (in dbSNP:rs194685)"
FT                   /evidence="ECO:0000269|PubMed:10072596,
FT                   ECO:0000269|PubMed:10231028"
FT                   /id="VAR_055110"
FT   VARIANT         245
FT                   /note="S -> L (in dbSNP:rs1078846)"
FT                   /id="VAR_055111"
FT   VARIANT         284
FT                   /note="V -> M (in dbSNP:rs818818)"
FT                   /evidence="ECO:0000269|PubMed:10072596,
FT                   ECO:0000269|PubMed:10231028, ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|Ref.5"
FT                   /id="VAR_055112"
FT   VARIANT         292
FT                   /note="S -> G (in dbSNP:rs818817)"
FT                   /evidence="ECO:0000269|PubMed:10072596,
FT                   ECO:0000269|PubMed:10231028, ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334, ECO:0000269|Ref.5"
FT                   /id="VAR_055113"
FT   VARIANT         466
FT                   /note="L -> P (in dbSNP:rs34256819)"
FT                   /id="VAR_055114"
FT   VARIANT         512
FT                   /note="A -> V (in dbSNP:rs2070492)"
FT                   /id="VAR_055115"
FT   VARIANT         560
FT                   /note="P -> R (in dbSNP:rs240033)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_055116"
FT   MUTAGEN         388
FT                   /note="W->A: Strongly reduced riboflavin transport; when
FT                   associated with A-395 and A-487."
FT                   /evidence="ECO:0000269|PubMed:33882315"
FT   MUTAGEN         395
FT                   /note="Y->A: Strongly reduced riboflavin transport; when
FT                   associated with A-388 and A-487."
FT                   /evidence="ECO:0000269|PubMed:33882315"
FT   MUTAGEN         487
FT                   /note="R->A: Strongly reduced riboflavin transport; when
FT                   associated with A-388 and A-395."
FT                   /evidence="ECO:0000269|PubMed:33882315"
FT   CONFLICT        282
FT                   /note="G -> W (in Ref. 1; BAA76351 and 2; BAA77626)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        470
FT                   /note="R -> H (in Ref. 3; BAG37720)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   594 AA;  66684 MW;  7EA290B06222B681 CRC64;
     MAGEENFKEE LRSQDASRNL NQHEVAGHPH SWSLEMLLRR LRAVHTKQDD KFANLLDAVG
     EFGTFQQRLV ALTFIPSIMS AFFMFADHFV FTAQKPYCNT SWILAVGPHL SKAEQLNLTI
     PQAPNGSFLT CFMYLPVPWN LDSIIQFGLN DTDTCQDGWI YPDAKKRSLI NEFDLVCGME
     TKKDTAQIMF MAGLPIGSLI FRLITDKMGR YPAILLSLLG LIIFGFGTAF MNSFHLYLFF
     RFGISQSVVG YAISSISLAT EWLVGEHRAH AIILGHCFFA VGAVLLTGIA YSLPHWQLLF
     LVGGILVIPF ISYIWILPES PRWLMMKGKV KEAKQVLCYA ASVNKKTIPS NLLDELQLPR
     KKVTRASVLD FCKNRQLCKV TLVMSCVWFT VSYTYFTLSL RMRELGVSVH FRHVVPSIME
     VPARLCCIFL LQQIGRKWSL AVTLLQAIIW CLLLLFLPEG EDGLRLKWPR CPATELKSMT
     ILVLMLREFS LAATVTVFFL YTAELLPTVL RATGLGLVSL ASVAGAILSL TIISQTPSLL
     PIFLCCVLAI VAFSLSSLLP ETRDQPLSES LNHSSQIRNK VKDMKTKETS SDDV
//