ID   LRAD4_HUMAN             Reviewed;         306 AA.
AC   O15165; B3KNT9; E9PAY9; K7EN38; O15166; O15167; O15168; Q5U646; Q6NXP3;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   24-JAN-2024, entry version 180.
DE   RecName: Full=Low-density lipoprotein receptor class A domain-containing protein 4;
GN   Name=LDLRAD4; Synonyms=C18orf1;
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] (ISOFORMS ALPHA-1; ALPHA-2; BETA-1 AND BETA-2).
RC   TISSUE=Brain;
RX   PubMed=9479497; DOI=10.1006/geno.1997.5118;
RA   Yoshikawa T., Sanders A.R., Esterling L.E., Detera-Wadleigh S.D.;
RT   "Multiple transcriptional variants and RNA editing in C18orf1, a novel gene
RT   with LDLRA and transmembrane domains on 18p11.2.";
RL   Genomics 47:246-257(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC   TISSUE=Brain;
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=16177791; DOI=10.1038/nature03983;
RA   Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA   Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA   Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA   Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA   Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA   Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA   Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA   Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA   Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 18.";
RL   Nature 437:551-555(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] (ISOFORMS ALPHA-2; 5 AND 8).
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-251 (ISOFORM 7).
RC   TISSUE=Testis;
RA   Ebert L., Heil O., Hennig S., Neubert P., Partsch E., Peters M.,
RA   Radelof U., Schneider D., Korn B.;
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   TISSUE SPECIFICITY.
RX   PubMed=19461657; DOI=10.1038/jhg.2009.47;
RA   Meerabux J.M., Ohba H., Iwayama Y., Maekawa M., Detera-Wadleigh S.D.,
RA   DeLisi L.E., Yoshikawa T.;
RT   "Analysis of a t(18;21)(p11.1;p11.1) translocation in a family with
RT   schizophrenia.";
RL   J. Hum. Genet. 54:386-391(2009).
RN   [8]
RP   FUNCTION, INTERACTION WITH PMEPA1; SMAD2 AND SMAD3, SUBCELLULAR LOCATION,
RP   AND MOTIF.
RX   PubMed=24627487; DOI=10.1074/jbc.m114.558981;
RA   Nakano N., Maeyama K., Sakata N., Itoh F., Akatsu R., Nakata M., Katsu Y.,
RA   Ikeno S., Togawa Y., Vo Nguyen T.T., Watanabe Y., Kato M., Itoh S.;
RT   "C18 ORF1, a novel negative regulator of transforming growth factor-beta
RT   signaling.";
RL   J. Biol. Chem. 289:12680-12692(2014).
CC   -!- FUNCTION: Functions as a negative regulator of TGF-beta signaling and
CC       thereby probably plays a role in cell proliferation, differentiation,
CC       apoptosis, motility, extracellular matrix production and
CC       immunosuppression. In the canonical TGF-beta pathway, ZFYVE9/SARA
CC       recruits the intracellular signal transducer and transcriptional
CC       modulators SMAD2 and SMAD3 to the TGF-beta receptor. Phosphorylated by
CC       the receptor, SMAD2 and SMAD3 then form a heteromeric complex with
CC       SMAD4 that translocates to the nucleus to regulate transcription.
CC       Through interaction with SMAD2 and SMAD3, LDLRAD4 may compete with
CC       ZFYVE9 and SMAD4 and prevent propagation of the intracellular signal.
CC       {ECO:0000269|PubMed:24627487}.
CC   -!- SUBUNIT: Interacts with PMEPA1. Interacts (via the SMAD interaction
CC       motif) with SMAD2 and SMAD3. {ECO:0000269|PubMed:24627487}.
CC   -!- INTERACTION:
CC       O15165-2; O43681: GET3; NbExp=3; IntAct=EBI-13302279, EBI-2515857;
CC       O15165-2; O43765: SGTA; NbExp=3; IntAct=EBI-13302279, EBI-347996;
CC       O15165-2; Q8N966: ZDHHC22; NbExp=3; IntAct=EBI-13302279, EBI-10268111;
CC   -!- SUBCELLULAR LOCATION: Early endosome membrane
CC       {ECO:0000269|PubMed:24627487}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:24627487}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=8;
CC       Name=Alpha-1;
CC         IsoId=O15165-1; Sequence=Displayed;
CC       Name=Alpha-2;
CC         IsoId=O15165-2; Sequence=VSP_006440;
CC       Name=Beta-1;
CC         IsoId=O15165-3; Sequence=VSP_006439;
CC       Name=Beta-2;
CC         IsoId=O15165-4; Sequence=VSP_006439, VSP_006440;
CC       Name=5;
CC         IsoId=O15165-5; Sequence=VSP_013901;
CC       Name=6;
CC         IsoId=O15165-6; Sequence=VSP_043253;
CC       Name=7;
CC         IsoId=O15165-7; Sequence=VSP_043253, VSP_006440;
CC       Name=8;
CC         IsoId=O15165-8; Sequence=VSP_054772;
CC   -!- TISSUE SPECIFICITY: Expressed in lymphocytes.
CC       {ECO:0000269|PubMed:19461657}.
CC   -!- DOMAIN: The SMAD interaction motif is required for interaction with
CC       SMAD2 and SMAD3 and the negative regulation of TGF-beta signaling.
CC       {ECO:0000269|PubMed:24627487}.
CC   -!- SIMILARITY: Belongs to the PMEPA1 family. {ECO:0000305}.
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DR   EMBL; AF009424; AAC52023.1; -; mRNA.
DR   EMBL; AF009425; AAC52024.1; -; mRNA.
DR   EMBL; AF009426; AAC52025.1; -; mRNA.
DR   EMBL; AF009427; AAC52026.1; -; mRNA.
DR   EMBL; AK055028; BAG51451.1; -; mRNA.
DR   EMBL; AP001010; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP002439; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP002505; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP005131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471113; EAX01514.1; -; Genomic_DNA.
DR   EMBL; BC029958; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC030199; AAH30199.1; -; mRNA.
DR   EMBL; BC066971; AAH66971.1; -; mRNA.
DR   EMBL; BX114947; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS32793.1; -. [O15165-1]
DR   CCDS; CCDS32794.1; -. [O15165-2]
DR   CCDS; CCDS32795.1; -. [O15165-6]
DR   CCDS; CCDS42415.1; -. [O15165-7]
DR   CCDS; CCDS62392.1; -. [O15165-5]
DR   RefSeq; NP_001003674.1; NM_001003674.3. [O15165-6]
DR   RefSeq; NP_001003675.1; NM_001003675.3. [O15165-7]
DR   RefSeq; NP_001263178.1; NM_001276249.1. [O15165-5]
DR   RefSeq; NP_001263180.1; NM_001276251.1. [O15165-8]
DR   RefSeq; NP_852146.1; NM_181481.4. [O15165-1]
DR   RefSeq; NP_852147.1; NM_181482.4. [O15165-2]
DR   RefSeq; XP_005258197.1; XM_005258140.1.
DR   RefSeq; XP_006722416.1; XM_006722353.1. [O15165-1]
DR   RefSeq; XP_006722417.1; XM_006722354.1. [O15165-1]
DR   RefSeq; XP_011524040.1; XM_011525738.1.
DR   RefSeq; XP_016881454.1; XM_017025965.1.
DR   RefSeq; XP_016881455.1; XM_017025966.1.
DR   RefSeq; XP_016881456.1; XM_017025967.1.
DR   RefSeq; XP_016881457.1; XM_017025968.1.
DR   RefSeq; XP_016881458.1; XM_017025969.1. [O15165-5]
DR   RefSeq; XP_016881459.1; XM_017025970.1. [O15165-5]
DR   RefSeq; XP_016881460.1; XM_017025971.1.
DR   AlphaFoldDB; O15165; -.
DR   BioGRID; 107209; 58.
DR   IntAct; O15165; 41.
DR   STRING; 9606.ENSP00000352420; -.
DR   iPTMnet; O15165; -.
DR   PhosphoSitePlus; O15165; -.
DR   SwissPalm; O15165; -.
DR   BioMuta; LDLRAD4; -.
DR   MassIVE; O15165; -.
DR   PaxDb; 9606-ENSP00000352420; -.
DR   PeptideAtlas; O15165; -.
DR   ProteomicsDB; 19107; -.
DR   ProteomicsDB; 48486; -. [O15165-1]
DR   ProteomicsDB; 48487; -. [O15165-2]
DR   ProteomicsDB; 48488; -. [O15165-3]
DR   ProteomicsDB; 48489; -. [O15165-4]
DR   ProteomicsDB; 48490; -. [O15165-5]
DR   ProteomicsDB; 48491; -. [O15165-6]
DR   Antibodypedia; 21959; 87 antibodies from 10 providers.
DR   DNASU; 753; -.
DR   Ensembl; ENST00000359446.11; ENSP00000352420.5; ENSG00000168675.19. [O15165-1]
DR   Ensembl; ENST00000399848.7; ENSP00000382741.2; ENSG00000168675.19. [O15165-2]
DR   Ensembl; ENST00000585931.5; ENSP00000466772.1; ENSG00000168675.19. [O15165-5]
DR   Ensembl; ENST00000586765.1; ENSP00000474783.1; ENSG00000168675.19. [O15165-7]
DR   Ensembl; ENST00000587757.5; ENSP00000466178.1; ENSG00000168675.19. [O15165-6]
DR   Ensembl; ENST00000677744.1; ENSP00000504022.1; ENSG00000168675.19. [O15165-5]
DR   Ensembl; ENST00000677910.1; ENSP00000503996.1; ENSG00000168675.19. [O15165-5]
DR   Ensembl; ENST00000679091.1; ENSP00000503185.1; ENSG00000168675.19. [O15165-1]
DR   GeneID; 753; -.
DR   KEGG; hsa:753; -.
DR   MANE-Select; ENST00000359446.11; ENSP00000352420.5; NM_001378100.1; NP_001365029.1.
DR   UCSC; uc002ksb.4; human. [O15165-1]
DR   AGR; HGNC:1224; -.
DR   CTD; 753; -.
DR   DisGeNET; 753; -.
DR   GeneCards; LDLRAD4; -.
DR   HGNC; HGNC:1224; LDLRAD4.
DR   HPA; ENSG00000168675; Tissue enhanced (lymphoid).
DR   MIM; 606571; gene.
DR   neXtProt; NX_O15165; -.
DR   OpenTargets; ENSG00000168675; -.
DR   PharmGKB; PA25593; -.
DR   VEuPathDB; HostDB:ENSG00000168675; -.
DR   eggNOG; ENOG502QRYK; Eukaryota.
DR   GeneTree; ENSGT00390000000724; -.
DR   HOGENOM; CLU_074371_0_1_1; -.
DR   InParanoid; O15165; -.
DR   OMA; RECKFTC; -.
DR   OrthoDB; 5349462at2759; -.
DR   PhylomeDB; O15165; -.
DR   TreeFam; TF331681; -.
DR   PathwayCommons; O15165; -.
DR   SignaLink; O15165; -.
DR   BioGRID-ORCS; 753; 14 hits in 1143 CRISPR screens.
DR   ChiTaRS; LDLRAD4; human.
DR   GenomeRNAi; 753; -.
DR   Pharos; O15165; Tbio.
DR   PRO; PR:O15165; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   RNAct; O15165; Protein.
DR   Bgee; ENSG00000168675; Expressed in endothelial cell and 191 other cell types or tissues.
DR   ExpressionAtlas; O15165; baseline and differential.
DR   GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0070412; F:R-SMAD binding; IPI:UniProtKB.
DR   GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
DR   GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
DR   GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; IDA:UniProtKB.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR   CDD; cd00112; LDLa; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR043445; TMEPAI/LRAD4.
DR   PANTHER; PTHR16514; LOW DENSITY LIPOPROTEIN RECEPTOR CLASS A DOMAIN-CONTAINING 4A; 1.
DR   PANTHER; PTHR16514:SF4; LOW-DENSITY LIPOPROTEIN RECEPTOR CLASS A DOMAIN-CONTAINING PROTEIN 4; 1.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   SMART; SM00192; LDLa; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 1.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
DR   Genevisible; O15165; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; Endosome; Membrane;
KW   Reference proteome; Signal transduction inhibitor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..306
FT                   /note="Low-density lipoprotein receptor class A domain-
FT                   containing protein 4"
FT                   /id="PRO_0000185444"
FT   TOPO_DOM        1..64
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        86..306
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          16..48
FT                   /note="LDL-receptor class A"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   REGION          286..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           180..183
FT                   /note="PPxY motif 1"
FT   MOTIF           208..211
FT                   /note="SMAD interaction motif (SIM)"
FT   MOTIF           252..255
FT                   /note="PPxY motif 2"
FT   DISULFID        19..38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   DISULFID        32..47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT   VAR_SEQ         1..111
FT                   /note="MPEAGFQATNAFTECKFTCTSGKCLYLGSLVCNQQNDCGDNSDEENCLLVTE
FT                   HPPPGIFNSELEFAQIIIIVVVVTVMVVVIVCLLNHYKVSTRSFINRPNQSRRREDGLP
FT                   -> MRLDSHLECISST (in isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_054772"
FT   VAR_SEQ         1..77
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_013901"
FT   VAR_SEQ         1..61
FT                   /note="MPEAGFQATNAFTECKFTCTSGKCLYLGSLVCNQQNDCGDNSDEENCLLVTE
FT                   HPPPGIFNS -> MSSDHLNNSTLKEAQFKDLFLKKA (in isoform 6 and
FT                   isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.6"
FT                   /id="VSP_043253"
FT   VAR_SEQ         1..61
FT                   /note="MPEAGFQATNAFTECKFTCTSGKCLYLGSLVCNQQNDCGDNSDEENCLLVTE
FT                   HPPPGIFNS -> MAA (in isoform Beta-1 and isoform Beta-2)"
FT                   /evidence="ECO:0000303|PubMed:9479497"
FT                   /id="VSP_006439"
FT   VAR_SEQ         113..130
FT                   /note="Missing (in isoform Alpha-2, isoform Beta-2 and
FT                   isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:9479497, ECO:0000303|Ref.6"
FT                   /id="VSP_006440"
FT   CONFLICT        125
FT                   /note="R -> Q (in Ref. 5; AAH66971)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        135
FT                   /note="P -> T (in Ref. 5; AAH66971)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        194
FT                   /note="P -> T (in Ref. 5; AAH66971)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   306 AA;  33900 MW;  F48EF66E329201BD CRC64;
     MPEAGFQATN AFTECKFTCT SGKCLYLGSL VCNQQNDCGD NSDEENCLLV TEHPPPGIFN
     SELEFAQIII IVVVVTVMVV VIVCLLNHYK VSTRSFINRP NQSRRREDGL PQEGCLWPSD
     SAAPRLGASE IMHAPRSRDR FTAPSFIQRD RFSRFQPTYP YVQHEIDLPP TISLSDGEEP
     PPYQGPCTLQ LRDPEQQMEL NRESVRAPPN RTIFDSDLID IAMYSGGPCP PSSNSGISAS
     TCSSNGRMEG PPPTYSEVMG HHPGASFLHH QRSNAHRGSR LQFQQNNAES TIVPIKGKDR
     KPGNLV
//