S14L1_HUMAN
ID S14L1_HUMAN Reviewed; 715 AA.
AC Q92503; A8K4E8; B4DDI5; D5G3K1; Q99780;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=SEC14-like protein 1 {ECO:0000305};
GN Name=SEC14L1; Synonyms=SEC14L;
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), VARIANT PRO-188, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=8697811; DOI=10.1159/000134342;
RA Chinen K., Takahashi E., Nakamura Y.;
RT "Isolation and mapping of a human gene (SEC14L), partially homologous to
RT yeast SEC14, that contains a variable number of tandem repeats (VNTR) site
RT in its 3' untranslated region.";
RL Cytogenet. Cell Genet. 73:218-223(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT PRO-188.
RC TISSUE=Brain;
RA Matthes F., Hansmann I., Schlote D.;
RT "Alternative splice variants of SEC14L1.";
RL Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP PRO-188.
RC TISSUE=Adrenal gland;
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=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-188.
RA Mural R.J., Istrail S., Sutton 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), AND VARIANT PRO-188.
RC TISSUE=Testis;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 423-715 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9110174; DOI=10.1101/gr.7.4.353;
RA Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
RA Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
RT "Large-scale concatenation cDNA sequencing.";
RL Genome Res. 7:353-358(1997).
RN [8]
RP FUNCTION, INTERACTION WITH SLC18A3 AND SLC5A7, AND SUBCELLULAR LOCATION.
RX PubMed=17092608; DOI=10.1016/j.neuint.2006.09.010;
RA Ribeiro F.M., Ferreira L.T., Marion S., Fontes S., Gomez M., Ferguson S.S.,
RA Prado M.A., Prado V.F.;
RT "SEC14-like protein 1 interacts with cholinergic transporters.";
RL Neurochem. Int. 50:356-364(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-586, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP FUNCTION, INTERACTION WITH DDX58, SUBCELLULAR LOCATION, AND REGION.
RX PubMed=23843640; DOI=10.1128/jvi.01073-13;
RA Li M.T., Di W., Xu H., Yang Y.K., Chen H.W., Zhang F.X., Zhai Z.H.,
RA Chen D.Y.;
RT "Negative regulation of RIG-I-mediated innate antiviral signaling by
RT SEC14L1.";
RL J. Virol. 87:10037-10046(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-234, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May play a role in innate immunity by inhibiting the
CC antiviral RIG-I signaling pathway. In this pathway, functions as a
CC negative regulator of DDX58/RIG-I, the cytoplasmic sensor of viral
CC nucleic acids. Prevents the interaction of DDX58 with MAVS/IPS1, an
CC important step in signal propagation (PubMed:23843640). May also
CC regulate the SLC18A3 and SLC5A7 cholinergic transporters
CC (PubMed:17092608). {ECO:0000269|PubMed:17092608,
CC ECO:0000269|PubMed:23843640}.
CC -!- SUBUNIT: Interacts with DDX58 (via tandem CARD domain); the interaction
CC is direct (PubMed:23843640). Interacts (via GOLD domain) with SLC18A3;
CC the interaction is direct (PubMed:17092608). Interacts with SLC5A7 (via
CC GOLD domain); the interaction is direct (PubMed:17092608).
CC {ECO:0000269|PubMed:17092608, ECO:0000269|PubMed:23843640}.
CC -!- INTERACTION:
CC Q92503; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-2855587, EBI-739624;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17092608,
CC ECO:0000269|PubMed:23843640}. Golgi apparatus
CC {ECO:0000269|PubMed:17092608}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q92503-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92503-2; Sequence=VSP_040118;
CC Name=3;
CC IsoId=Q92503-3; Sequence=VSP_040117;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8697811}.
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DR EMBL; D67029; BAA11048.1; -; mRNA.
DR EMBL; FM995495; CAX33889.1; -; mRNA.
DR EMBL; FM995496; CAX33890.1; -; mRNA.
DR EMBL; AK290913; BAF83602.1; -; mRNA.
DR EMBL; AK293206; BAG56746.1; -; mRNA.
DR EMBL; AC068594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471099; EAW89469.1; -; Genomic_DNA.
DR EMBL; BC136523; AAI36524.1; -; mRNA.
DR EMBL; BC136525; AAI36526.1; -; mRNA.
DR EMBL; U79284; AAB50220.1; -; mRNA.
DR CCDS; CCDS11752.1; -. [Q92503-1]
DR CCDS; CCDS42385.1; -. [Q92503-2]
DR CCDS; CCDS45789.1; -. [Q92503-3]
DR RefSeq; NP_001034662.2; NM_001039573.2. [Q92503-2]
DR RefSeq; NP_001137470.1; NM_001143998.1. [Q92503-1]
DR RefSeq; NP_001137471.1; NM_001143999.1. [Q92503-1]
DR RefSeq; NP_001137473.1; NM_001144001.1. [Q92503-3]
DR RefSeq; NP_001191337.1; NM_001204408.1. [Q92503-2]
DR RefSeq; NP_001191339.1; NM_001204410.1. [Q92503-1]
DR RefSeq; NP_002994.3; NM_003003.3. [Q92503-1]
DR AlphaFoldDB; Q92503; -.
DR SMR; Q92503; -.
DR BioGRID; 112297; 15.
DR IntAct; Q92503; 11.
DR MINT; Q92503; -.
DR STRING; 9606.ENSP00000376268; -.
DR iPTMnet; Q92503; -.
DR PhosphoSitePlus; Q92503; -.
DR BioMuta; SEC14L1; -.
DR DMDM; 313104180; -.
DR EPD; Q92503; -.
DR jPOST; Q92503; -.
DR MassIVE; Q92503; -.
DR MaxQB; Q92503; -.
DR PaxDb; Q92503; -.
DR PeptideAtlas; Q92503; -.
DR PRIDE; Q92503; -.
DR ProteomicsDB; 75272; -. [Q92503-1]
DR ProteomicsDB; 75273; -. [Q92503-2]
DR ProteomicsDB; 75274; -. [Q92503-3]
DR Antibodypedia; 32469; 69 antibodies from 15 providers.
DR DNASU; 6397; -.
DR Ensembl; ENST00000392476.6; ENSP00000376268.2; ENSG00000129657.16. [Q92503-2]
DR Ensembl; ENST00000430767.8; ENSP00000408169.3; ENSG00000129657.16. [Q92503-1]
DR Ensembl; ENST00000431431.6; ENSP00000389838.1; ENSG00000129657.16. [Q92503-3]
DR Ensembl; ENST00000436233.9; ENSP00000390392.3; ENSG00000129657.16. [Q92503-1]
DR Ensembl; ENST00000443798.8; ENSP00000406030.3; ENSG00000129657.16. [Q92503-2]
DR Ensembl; ENST00000585618.5; ENSP00000466581.1; ENSG00000129657.16. [Q92503-1]
DR Ensembl; ENST00000591437.5; ENSP00000467934.1; ENSG00000129657.16. [Q92503-3]
DR GeneID; 6397; -.
DR KEGG; hsa:6397; -.
DR MANE-Select; ENST00000436233.9; ENSP00000390392.3; NM_001143998.2; NP_001137470.2.
DR UCSC; uc002jto.4; human. [Q92503-1]
DR CTD; 6397; -.
DR DisGeNET; 6397; -.
DR GeneCards; SEC14L1; -.
DR HGNC; HGNC:10698; SEC14L1.
DR HPA; ENSG00000129657; Low tissue specificity.
DR MIM; 601504; gene.
DR neXtProt; NX_Q92503; -.
DR OpenTargets; ENSG00000129657; -.
DR PharmGKB; PA35621; -.
DR VEuPathDB; HostDB:ENSG00000129657; -.
DR eggNOG; KOG1471; Eukaryota.
DR GeneTree; ENSGT00940000155386; -.
DR HOGENOM; CLU_023840_0_0_1; -.
DR InParanoid; Q92503; -.
DR OMA; RECTLHI; -.
DR OrthoDB; 1133487at2759; -.
DR PhylomeDB; Q92503; -.
DR TreeFam; TF313988; -.
DR PathwayCommons; Q92503; -.
DR SignaLink; Q92503; -.
DR BioGRID-ORCS; 6397; 32 hits in 1083 CRISPR screens.
DR ChiTaRS; SEC14L1; human.
DR GeneWiki; SEC14L1; -.
DR GenomeRNAi; 6397; -.
DR Pharos; Q92503; Tbio.
DR PRO; PR:Q92503; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q92503; protein.
DR Bgee; ENSG00000129657; Expressed in dorsal motor nucleus of vagus nerve and 206 other tissues.
DR ExpressionAtlas; Q92503; baseline and differential.
DR Genevisible; Q92503; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0039552; F:RIG-I binding; IPI:UniProtKB.
DR GO; GO:0015871; P:choline transport; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0039536; P:negative regulation of RIG-I signaling pathway; IMP:UniProtKB.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR011074; CRAL/TRIO_N_dom.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR InterPro; IPR009038; GOLD_dom.
DR InterPro; IPR036598; GOLD_dom_sf.
DR InterPro; IPR006797; PRELI/MSF1_dom.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF03765; CRAL_TRIO_N; 1.
DR Pfam; PF04707; PRELI; 1.
DR SMART; SM01100; CRAL_TRIO_N; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF101576; SSF101576; 1.
DR SUPFAM; SSF46938; SSF46938; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50866; GOLD; 1.
DR PROSITE; PS50904; PRELI_MSF1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Golgi apparatus; Immunity;
KW Innate immunity; Phosphoprotein; Reference proteome;
KW Signal transduction inhibitor.
FT CHAIN 1..715
FT /note="SEC14-like protein 1"
FT /id="PRO_0000210753"
FT DOMAIN 1..175
FT /note="PRELI/MSF1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00158"
FT DOMAIN 319..495
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT DOMAIN 521..674
FT /note="GOLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00096"
FT REGION 1..510
FT /note="Required for interaction and inhibitory function
FT toward DDX58"
FT /evidence="ECO:0000269|PubMed:23843640"
FT MOD_RES 234
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..34
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040117"
FT VAR_SEQ 715
FT /note="R -> RWRFC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9110174, ECO:0000303|Ref.2"
FT /id="VSP_040118"
FT VARIANT 37
FT /note="V -> M (in dbSNP:rs1049416)"
FT /id="VAR_057173"
FT VARIANT 97
FT /note="A -> G (in dbSNP:rs1049422)"
FT /id="VAR_060480"
FT VARIANT 98
FT /note="Y -> H (in dbSNP:rs1049423)"
FT /id="VAR_060481"
FT VARIANT 188
FT /note="T -> P (in dbSNP:rs673918)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8697811,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.5"
FT /id="VAR_060482"
FT CONFLICT 43
FT /note="N -> S (in Ref. 1; BAA11048)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="E -> G (in Ref. 3; BAG56746)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="Y -> H (in Ref. 1; BAA11048)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="I -> V (in Ref. 1; BAA11048)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="G -> R (in Ref. 1; BAA11048)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 715 AA; 81250 MW; A0B840F8FFF01D13 CRC64;
MVQKYQSPVR VYKYPFELIM AAYERRFPTC PLIPMFVGSD TVNEFKSEDG AIHVIERRCK
LDVDAPRLLK KIAGVDYVYF VQKNSLNSRE RTLHIEAYNE TFSNRVIINE HCCYTVHPEN
EDWTCFEQSA SLDIKSFFGF ESTVEKIAMK QYTSNIKKGK EIIEYYLRQL EEEGITFVPR
WSPPSITTSS ETSSSSSKKQ AASMAVVIPE AALKEGLSGD ALSSPSAPEP VVGTPDDKLD
ADYIKRYLGD LTPLQESCLI RLRQWLQETH KGKIPKDEHI LRFLRARDFN IDKAREIMCQ
SLTWRKQHQV DYILETWTPP QVLQDYYAGG WHHHDKDGRP LYVLRLGQMD TKGLVRALGE
EALLRYVLSI NEEGLRRCEE NTKVFGRPIS SWTCLVDLEG LNMRHLWRPG VKALLRIIEV
VEANYPETLG RLLILRAPRV FPVLWTLVSP FIDDNTRRKF LIYAGNDYQG PGGLLDYIDK
EIIPDFLSGE CMCEVPEGGL VPKSLYRTAE ELENEDLKLW TETIYQSASV FKGAPHEILI
QIVDASSVIT WDFDVCKGDI VFNIYHSKRS PQPPKKDSLG AHSITSPGGN NVQLIDKVWQ
LGRDYSMVES PLICKEGESV QGSHVTRWPG FYILQWKFHS MPACAASSLP RVDDVLASLQ
VSSHKCKVMY YTEVIGSEDF RGSMTSLESS HSGFSQLSAA TTSSSQSHSS SMISR
