CTR3_HUMAN
ID CTR3_HUMAN Reviewed; 619 AA.
AC Q8WY07; D3DVU7; Q5JQR2; Q8N185; Q8NCA7; Q96SZ7;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Cationic amino acid transporter 3;
DE Short=CAT-3;
DE Short=CAT3;
DE AltName: Full=Cationic amino acid transporter y+;
DE AltName: Full=Solute carrier family 7 member 3;
GN Name=SLC7A3; Synonyms=ATRC3, CAT3;
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], FUNCTION, GLYCOSYLATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Teratocarcinoma;
RX PubMed=11591158; DOI=10.1021/bi011345c;
RA Vekony N., Wolf S., Boissel J.-P., Gnauert K., Closs E.I.;
RT "Human cationic amino acid transporter hCAT-3 is preferentially expressed
RT in peripheral tissues.";
RL Biochemistry 40:12387-12394(2001).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-508.
RC TISSUE=Lung;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-606 AND SER-618, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [7]
RP VARIANT LYS-356.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: Mediates the uptake of the cationic amino acids arginine,
CC lysine and ornithine in a sodium-independent manner.
CC {ECO:0000269|PubMed:11591158}.
CC -!- INTERACTION:
CC Q8WY07; Q14973: SLC10A1; NbExp=3; IntAct=EBI-13066314, EBI-3923031;
CC Q8WY07; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-13066314, EBI-10982110;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Highly expressed in thymus, uterus and testis.
CC Detected at lower levels in brain, mammary gland, prostate, salivary
CC gland and fetal spleen. In brain, highest expression in thalamus,
CC hippocampus and amygdala. {ECO:0000269|PubMed:11591158}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:11591158}.
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=BAB55118.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF320612; AAL37184.1; -; mRNA.
DR EMBL; AK027447; BAB55118.1; ALT_INIT; mRNA.
DR EMBL; AK074865; BAC11253.1; -; mRNA.
DR EMBL; AK075014; BAC11353.1; -; mRNA.
DR EMBL; AL627071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471132; EAX05329.1; -; Genomic_DNA.
DR EMBL; CH471132; EAX05330.1; -; Genomic_DNA.
DR EMBL; BC033816; AAH33816.1; -; mRNA.
DR CCDS; CCDS14404.1; -.
DR RefSeq; NP_001041629.1; NM_001048164.2.
DR RefSeq; NP_116192.4; NM_032803.5.
DR RefSeq; XP_016885401.1; XM_017029912.1.
DR AlphaFoldDB; Q8WY07; -.
DR SMR; Q8WY07; -.
DR BioGRID; 124329; 49.
DR IntAct; Q8WY07; 15.
DR STRING; 9606.ENSP00000363417; -.
DR DrugBank; DB00125; Arginine.
DR DrugBank; DB13146; Fluciclovine (18F).
DR DrugBank; DB00123; Lysine.
DR TCDB; 2.A.3.3.10; the amino acid-polyamine-organocation (apc) family.
DR GlyGen; Q8WY07; 1 site.
DR iPTMnet; Q8WY07; -.
DR PhosphoSitePlus; Q8WY07; -.
DR BioMuta; SLC7A3; -.
DR DMDM; 41016908; -.
DR EPD; Q8WY07; -.
DR jPOST; Q8WY07; -.
DR MassIVE; Q8WY07; -.
DR PaxDb; Q8WY07; -.
DR PeptideAtlas; Q8WY07; -.
DR PRIDE; Q8WY07; -.
DR ProteomicsDB; 75116; -.
DR Antibodypedia; 586; 75 antibodies from 19 providers.
DR DNASU; 84889; -.
DR Ensembl; ENST00000298085.4; ENSP00000298085.4; ENSG00000165349.12.
DR Ensembl; ENST00000374299.8; ENSP00000363417.3; ENSG00000165349.12.
DR GeneID; 84889; -.
DR KEGG; hsa:84889; -.
DR MANE-Select; ENST00000374299.8; ENSP00000363417.3; NM_032803.6; NP_116192.4.
DR UCSC; uc004dyn.4; human.
DR CTD; 84889; -.
DR DisGeNET; 84889; -.
DR GeneCards; SLC7A3; -.
DR HGNC; HGNC:11061; SLC7A3.
DR HPA; ENSG00000165349; Tissue enhanced (lymphoid).
DR MIM; 300443; gene.
DR neXtProt; NX_Q8WY07; -.
DR OpenTargets; ENSG00000165349; -.
DR PharmGKB; PA35921; -.
DR VEuPathDB; HostDB:ENSG00000165349; -.
DR eggNOG; KOG1286; Eukaryota.
DR GeneTree; ENSGT00940000154651; -.
DR HOGENOM; CLU_007946_15_7_1; -.
DR InParanoid; Q8WY07; -.
DR OMA; VIAKYWG; -.
DR OrthoDB; 439017at2759; -.
DR PhylomeDB; Q8WY07; -.
DR TreeFam; TF315212; -.
DR PathwayCommons; Q8WY07; -.
DR Reactome; R-HSA-352230; Amino acid transport across the plasma membrane.
DR SignaLink; Q8WY07; -.
DR BioGRID-ORCS; 84889; 17 hits in 698 CRISPR screens.
DR GeneWiki; SLC7A3; -.
DR GenomeRNAi; 84889; -.
DR Pharos; Q8WY07; Tbio.
DR PRO; PR:Q8WY07; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8WY07; protein.
DR Bgee; ENSG00000165349; Expressed in cauda epididymis and 85 other tissues.
DR Genevisible; Q8WY07; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0061459; F:L-arginine transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0015189; F:L-lysine transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0000064; F:L-ornithine transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0006865; P:amino acid transport; IBA:GO_Central.
DR GO; GO:0097638; P:L-arginine import across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0097639; P:L-lysine import across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0097640; P:L-ornithine import across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:1903352; P:L-ornithine transmembrane transport; IBA:GO_Central.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR InterPro; IPR002293; AA/rel_permease1.
DR InterPro; IPR015606; CAT3.
DR InterPro; IPR004755; Cat_AA_permease.
DR InterPro; IPR029485; CAT_C.
DR PANTHER; PTHR43243:SF20; PTHR43243:SF20; 1.
DR Pfam; PF13520; AA_permease_2; 1.
DR Pfam; PF13906; AA_permease_C; 1.
DR TIGRFAMs; TIGR00906; 2A0303; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..619
FT /note="Cationic amino acid transporter 3"
FT /id="PRO_0000054266"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..61
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..162
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..233
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 234..254
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..335
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 404..406
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 476..496
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 497..506
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 507..527
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 528..540
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 541..561
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255"
FT TOPO_DOM 562..569
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 570..590
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255"
FT TOPO_DOM 591..619
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 606
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 356
FT /note="M -> K (found in a renal cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064754"
FT VARIANT 508
FT /note="L -> V (in dbSNP:rs6525447)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_048154"
FT CONFLICT 191
FT /note="K -> R (in Ref. 5; AAH33816)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="E -> G (in Ref. 2; BAC11253)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 619 AA; 67169 MW; 211254FA87D43978 CRC64;
MPWQAFRRFG QKLVRRRTLE SGMAETRLAR CLSTLDLVAL GVGSTLGAGV YVLAGEVAKD
KAGPSIVICF LVAALSSVLA GLCYAEFGAR VPRSGSAYLY SYVTVGELWA FTTGWNLILS
YVIGTASVAR AWSSAFDNLI GNHISKTLQG SIALHVPHVL AEYPDFFALG LVLLLTGLLA
LGASESALVT KVFTGVNLLV LGFVMISGFV KGDVHNWKLT EEDYELAMAE LNDTYSLGPL
GSGGFVPFGF EGILRGAATC FYAFVGFDCI ATTGEEAQNP QRSIPMGIVI SLSVCFLAYF
AVSSALTLMM PYYQLQPESP LPEAFLYIGW APARYVVAVG SLCALSTSLL GSMFPMPRVI
YAMAEDGLLF RVLARIHTGT RTPIIATVVS GIIAAFMAFL FKLTDLVDLM SIGTLLAYSL
VSICVLILRY QPDQETKTGE EVELQEEAIT TESEKLTLWG LFFPLNSIPT PLSGQIVYVC
SSLLAVLLTA LCLVLAQWSV PLLSGDLLWT AVVVLLLLLI IGIIVVIWRQ PQSSTPLHFK
VPALPLLPLM SIFVNIYLMM QMTAGTWARF GVWMLIGFAI YFGYGIQHSL EEIKSNQPSR
KSRAKTVDLD PGTLYVHSV