ATRN1_HUMAN
ID ATRN1_HUMAN Reviewed; 1379 AA.
AC Q5VV63; O60283; Q5JSE8; Q5T5Y9; Q6T256; Q6ZSN4; Q86WX2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Attractin-like protein 1;
DE Flags: Precursor;
GN Name=ATRNL1; Synonyms=KIAA0534;
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).
RA Milton N.G.N.;
RT "Attractin-like peptides.";
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 47-1379 (ISOFORM 1), AND VARIANT
RP ASN-989.
RC TISSUE=Hippocampus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 352-1379 (ISOFORM 1), AND VARIANT
RP ASN-989.
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [6]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
CC -!- FUNCTION: May play a role in melanocortin signaling pathways that
CC regulate energy homeostasis. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MC4R. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5VV63-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VV63-2; Sequence=VSP_033718, VSP_033719;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC86914.1; 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; AY442317; AAR14297.1; -; mRNA.
DR EMBL; AC022542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356100; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL357059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL392087; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512304; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047716; AAH47716.1; -; mRNA.
DR EMBL; BC139916; AAI39917.1; -; mRNA.
DR EMBL; BC139923; AAI39924.1; -; mRNA.
DR EMBL; AK127277; BAC86914.1; ALT_INIT; mRNA.
DR EMBL; AB011106; BAA25460.2; -; mRNA.
DR CCDS; CCDS73204.1; -. [Q5VV63-2]
DR CCDS; CCDS7592.1; -. [Q5VV63-1]
DR PIR; T00266; T00266.
DR RefSeq; NP_001263211.1; NM_001276282.3. [Q5VV63-2]
DR RefSeq; NP_997186.1; NM_207303.4. [Q5VV63-1]
DR AlphaFoldDB; Q5VV63; -.
DR SMR; Q5VV63; -.
DR BioGRID; 117499; 7.
DR IntAct; Q5VV63; 6.
DR MINT; Q5VV63; -.
DR STRING; 9606.ENSP00000347152; -.
DR GlyGen; Q5VV63; 8 sites.
DR iPTMnet; Q5VV63; -.
DR PhosphoSitePlus; Q5VV63; -.
DR BioMuta; ATRNL1; -.
DR DMDM; 189081675; -.
DR EPD; Q5VV63; -.
DR MassIVE; Q5VV63; -.
DR PaxDb; Q5VV63; -.
DR PeptideAtlas; Q5VV63; -.
DR PRIDE; Q5VV63; -.
DR ProteomicsDB; 65449; -. [Q5VV63-1]
DR ProteomicsDB; 65450; -. [Q5VV63-2]
DR Antibodypedia; 52380; 30 antibodies from 12 providers.
DR DNASU; 26033; -.
DR Ensembl; ENST00000355044.8; ENSP00000347152.3; ENSG00000107518.18. [Q5VV63-1]
DR Ensembl; ENST00000609571.5; ENSP00000476902.2; ENSG00000107518.18. [Q5VV63-2]
DR GeneID; 26033; -.
DR KEGG; hsa:26033; -.
DR MANE-Select; ENST00000355044.8; ENSP00000347152.3; NM_207303.4; NP_997186.1.
DR UCSC; uc001lcg.4; human. [Q5VV63-1]
DR CTD; 26033; -.
DR DisGeNET; 26033; -.
DR GeneCards; ATRNL1; -.
DR HGNC; HGNC:29063; ATRNL1.
DR HPA; ENSG00000107518; Tissue enriched (brain).
DR MIM; 612869; gene.
DR neXtProt; NX_Q5VV63; -.
DR OpenTargets; ENSG00000107518; -.
DR PharmGKB; PA134961599; -.
DR VEuPathDB; HostDB:ENSG00000107518; -.
DR eggNOG; KOG1388; Eukaryota.
DR GeneTree; ENSGT00940000155790; -.
DR HOGENOM; CLU_046715_0_0_1; -.
DR InParanoid; Q5VV63; -.
DR OMA; ACDEWKT; -.
DR PhylomeDB; Q5VV63; -.
DR TreeFam; TF321873; -.
DR PathwayCommons; Q5VV63; -.
DR SignaLink; Q5VV63; -.
DR BioGRID-ORCS; 26033; 9 hits in 1065 CRISPR screens.
DR ChiTaRS; ATRNL1; human.
DR GenomeRNAi; 26033; -.
DR Pharos; Q5VV63; Tdark.
DR PRO; PR:Q5VV63; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q5VV63; protein.
DR Bgee; ENSG00000107518; Expressed in adrenal tissue and 138 other tissues.
DR ExpressionAtlas; Q5VV63; baseline and differential.
DR Genevisible; Q5VV63; HS.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd03597; CLECT_attractin_like; 1.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00055; EGF_Lam; 1.
DR Gene3D; 2.120.10.80; -; 2.
DR Gene3D; 2.60.120.290; -; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR034011; Attractin-like_CTLD.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF01437; PSI; 2.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00180; EGF_Lam; 2.
DR SMART; SM00423; PSI; 5.
DR SUPFAM; SSF117281; SSF117281; 2.
DR SUPFAM; SSF49854; SSF49854; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS00022; EGF_1; 3.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; EGF-like domain; Glycoprotein;
KW Kelch repeat; Laminin EGF-like domain; Lectin; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..52
FT /evidence="ECO:0000255"
FT CHAIN 53..1379
FT /note="Attractin-like protein 1"
FT /id="PRO_0000334650"
FT TOPO_DOM 53..1230
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1231..1251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1252..1379
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 53..91
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 93..209
FT /note="CUB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00059"
FT DOMAIN 207..245
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REPEAT 316..365
FT /note="Kelch 1"
FT REPEAT 367..415
FT /note="Kelch 2"
FT REPEAT 427..475
FT /note="Kelch 3"
FT REPEAT 480..531
FT /note="Kelch 4"
FT REPEAT 533..591
FT /note="Kelch 5"
FT REPEAT 592..638
FT /note="Kelch 6"
FT DOMAIN 614..657
FT /note="PSI 1"
FT DOMAIN 666..709
FT /note="PSI 2"
FT DOMAIN 715..760
FT /note="PSI 3"
FT DOMAIN 755..873
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 889..939
FT /note="PSI 4"
FT DOMAIN 942..1012
FT /note="PSI 5"
FT DOMAIN 1014..1059
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 1060..1108
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1354..1379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 778
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 898
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 63..79
FT /evidence="ECO:0000250"
FT DISULFID 81..90
FT /evidence="ECO:0000250"
FT DISULFID 93..119
FT /evidence="ECO:0000250"
FT DISULFID 211..221
FT /evidence="ECO:0000250"
FT DISULFID 215..233
FT /evidence="ECO:0000250"
FT DISULFID 235..244
FT /evidence="ECO:0000250"
FT DISULFID 776..872
FT /evidence="ECO:0000250"
FT DISULFID 1014..1022
FT /evidence="ECO:0000250"
FT DISULFID 1016..1028
FT /evidence="ECO:0000250"
FT DISULFID 1031..1040
FT /evidence="ECO:0000250"
FT DISULFID 1043..1057
FT /evidence="ECO:0000250"
FT DISULFID 1060..1069
FT /evidence="ECO:0000250"
FT DISULFID 1062..1076
FT /evidence="ECO:0000250"
FT DISULFID 1078..1088
FT /evidence="ECO:0000250"
FT DISULFID 1091..1106
FT /evidence="ECO:0000250"
FT VAR_SEQ 450..467
FT /note="SSNTWLVPETKGAIVQGG -> CELLKNCNFFIDWECFSL (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033718"
FT VAR_SEQ 468..1379
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033719"
FT VARIANT 989
FT /note="S -> N (in dbSNP:rs1953758)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:9628581"
FT /id="VAR_043446"
SQ SEQUENCE 1379 AA; 152639 MW; 67904F946FAF6028 CRC64;
METGGRARTG TPQPAAPGVW RARPAGGGGG GASSWLLDGN SWLLCYGFLY LALYAQVSQS
KPCERTGSCF SGRCVNSTCL CDPGWVGDQC QHCQGRFKLT EPSGYLTDGP INYKYKTKCT
WLIEGYPNAV LRLRFNHFAT ECSWDHMYVY DGDSIYAPLI AVLSGLIVPE IRGNETVPEV
VTTSGYALLH FFSDAAYNLT GFNIFYSINS CPNNCSGHGK CTTSVSVPSQ VYCECDKYWK
GEACDIPYCK ANCGSPDHGY CDLTGEKLCV CNDSWQGPDC SLNVPSTESY WILPNVKPFS
PSVGRASHKA VLHGKFMWVI GGYTFNYSSF QMVLNYNLES SIWNVGTPSR GPLQRYGHSL
ALYQENIFMY GGRIETNDGN VTDELWVFNI HSQSWSTKTP TVLGHGQQYA VEGHSAHIME
LDSRDVVMII IFGYSAIYGY TSSIQEYHIS SNTWLVPETK GAIVQGGYGH TSVYDEITKS
IYVHGGYKAL PGNKYGLVDD LYKYEVNTKT WTILKESGFA RYLHSAVLIN GAMLIFGGNT
HNDTSLSNGA KCFSADFLAY DIACDEWKIL PKPNLHRDVN RFGHSAVVIN GSMYIFGGFS
SVLLNDILVY KPPNCKAFRD EELCKNAGPG IKCVWNKNHC ESWESGNTNN ILRAKCPPKT
AASDDRCYRY ADCASCTANT NGCQWCDDKK CISANSNCSM SVKNYTKCHV RNEQICNKLT
SCKSCSLNLN CQWDQRQQEC QALPAHLCGE GWSHIGDACL RVNSSRENYD NAKLYCYNLS
GNLASLTTSK EVEFVLDEIQ KYTQQKVSPW VGLRKINISY WGWEDMSPFT NTTLQWLPGE
PNDSGFCAYL ERAAVAGLKA NPCTSMANGL VCEKPVVSPN QNARPCKKPC SLRTSCSNCT
SNGMECMWCS STKRCVDSNA YIISFPYGQC LEWQTATCSP QNCSGLRTCG QCLEQPGCGW
CNDPSNTGRG HCIEGSSRGP MKLIGMHHSE MVLDTNLCPK EKNYEWSFIQ CPACQCNGHS
TCINNNVCEQ CKNLTTGKQC QDCMPGYYGD PTNGGQCTAC TCSGHANICH LHTGKCFCTT
KGIKGDQCQL CDSENRYVGN PLRGTCYYSL LIDYQFTFSL LQEDDRHHTA INFIANPEQS
NKNLDISINA SNNFNLNITW SVGSTAGTIS GEETSIVSKN NIKEYRDSFS YEKFNFRSNP
NITFYVYVSN FSWPIKIQIA FSQHNTIMDL VQFFVTFFSC FLSLLLVAAV VWKIKQTCWA
SRRREQLLRE RQQMASRPFA SVDVALEVGA EQTEFLRGPL EGAPKPIAIE PCAGNRAAVL
TVFLCLPRGS SGAPPPGQSG LAIASALIDI SQQKASDSKD KTSGVRNRKH LSTRQGTCV
