ID   IFT56_HUMAN             Reviewed;         554 AA.
AC   A0AVF1; A4D1S3; B7Z5M0; C9J2N7; F8W724; Q9H9S8; Q9NTC0;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 143.
DE   RecName: Full=Intraflagellar transport protein 56 {ECO:0000305};
DE   AltName: Full=Tetratricopeptide repeat protein 26 {ECO:0000312|HGNC:HGNC:21882};
DE            Short=TPR repeat protein 26 {ECO:0000312|HGNC:HGNC:21882};
GN   Name=IFT56 {ECO:0000312|HGNC:HGNC:21882}; Synonyms=TTC26;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-335 (ISOFORM 1/2).
RC   TISSUE=Testis;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [6]
RP   INVOLVEMENT IN BRENS, AND VARIANT BRENS SER-263.
RX   PubMed=32617964; DOI=10.1111/cge.13805;
RA   David O., Eskin-Schwartz M., Ling G., Dolgin V., Kristal E., Benkowitz E.,
RA   Osyntsov L., Gradstein L., Birk O.S., Loewenthal N., Yerushalmi B.;
RT   "Pituitary stalk interruption syndrome broadens the clinical spectrum of
RT   the TTC26 ciliopathy.";
RL   Clin. Genet. 98:303-307(2020).
RN   [7]
RP   VARIANTS BRENS SER-263 AND LEU-444, CHARACTERIZATION OF VARIANT BRENS
RP   SER-263, AND FUNCTION.
RX   PubMed=31595528; DOI=10.1002/hep.30982;
RA   Shaheen R., Alsahli S., Ewida N., Alzahrani F., Shamseldin H.E., Patel N.,
RA   Al Qahtani A., Alhebbi H., Alhashem A., Al-Sheddi T., Alomar R.,
RA   Alobeid E., Abouelhoda M., Monies D., Al-Hussaini A., Alzouman M.A.,
RA   Shagrani M., Faqeih E., Alkuraya F.S.;
RT   "Biallelic Mutations in Tetratricopeptide Repeat Domain 26 (Intraflagellar
RT   Transport 56) Cause Severe Biliary Ciliopathy in Humans.";
RL   Hepatology 71:2067-2079(2020).
CC   -!- FUNCTION: Component of the intraflagellar transport (IFT) complex B
CC       required for transport of proteins in the motile cilium. Required for
CC       transport of specific ciliary cargo proteins related to motility, while
CC       it is neither required for IFT complex B assembly or motion nor for
CC       cilium assembly. Required for efficient coupling between the
CC       accumulation of GLI2 and GLI3 at the ciliary tips and their
CC       dissociation from the negative regulator SUFU. Plays a key role in
CC       maintaining the integrity of the IFT complex B and the proper ciliary
CC       localization of the IFT complex B components. Not required for IFT
CC       complex A ciliary localization or function. Essential for maintaining
CC       proper microtubule organization within the ciliary axoneme.
CC       {ECO:0000269|PubMed:31595528}.
CC   -!- SUBUNIT: Component of the IFT complex B. Interacts with IFT46; the
CC       interaction is direct. {ECO:0000250|UniProtKB:Q8BS45}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC       {ECO:0000250|UniProtKB:Q8BS45}. Note=Localizes at the base to the
CC       ciliary transition zone. {ECO:0000250|UniProtKB:Q8BS45}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=A0AVF1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A0AVF1-2; Sequence=VSP_043751;
CC       Name=3;
CC         IsoId=A0AVF1-3; Sequence=VSP_044791;
CC   -!- DISEASE: Biliary, renal, neurologic, and skeletal syndrome (BRENS)
CC       [MIM:619534]: An autosomal recessive ciliopathy with multisystemic
CC       manifestations including severe neonatal cholestasis that progresses to
CC       liver fibrosis and cirrhosis, postaxial polydactyly, hydrocephalus,
CC       retinal abnormalities, and situs inversus. Additional features may
CC       include congenital cardiac defects, echogenic kidneys with renal
CC       failure, ocular abnormalities, joint hyperextensibility, and dysmorphic
CC       facial features. Some patients have global developmental delay. Brain
CC       imaging typically shows dilated ventricles, hypomyelination, and white
CC       matter abnormalities, although some patients have been described with
CC       abnormal pituitary development. {ECO:0000269|PubMed:31595528,
CC       ECO:0000269|PubMed:32617964}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the IFT56 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAL24039.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK022633; BAB14143.1; -; mRNA.
DR   EMBL; AK299132; BAH12956.1; -; mRNA.
DR   EMBL; AC009220; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC018644; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH236950; EAL24039.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BC126331; AAI26332.1; -; mRNA.
DR   EMBL; BC130339; AAI30340.1; -; mRNA.
DR   EMBL; BC144151; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AL137393; CAB70721.2; -; mRNA.
DR   CCDS; CCDS55172.1; -. [A0AVF1-2]
DR   CCDS; CCDS55173.1; -. [A0AVF1-3]
DR   CCDS; CCDS5852.1; -. [A0AVF1-1]
DR   PIR; T46452; T46452.
DR   RefSeq; NP_001138392.1; NM_001144920.2. [A0AVF1-2]
DR   RefSeq; NP_001138395.1; NM_001144923.2. [A0AVF1-3]
DR   RefSeq; NP_079202.2; NM_024926.3. [A0AVF1-1]
DR   AlphaFoldDB; A0AVF1; -.
DR   SMR; A0AVF1; -.
DR   BioGRID; 123052; 96.
DR   ComplexPortal; CPX-5022; Intraflagellar transport complex B.
DR   CORUM; A0AVF1; -.
DR   IntAct; A0AVF1; 19.
DR   MINT; A0AVF1; -.
DR   STRING; 9606.ENSP00000419279; -.
DR   TCDB; 1.X.1.1.1; the intraflagellar transporter-a complex (ift-a) family.
DR   iPTMnet; A0AVF1; -.
DR   PhosphoSitePlus; A0AVF1; -.
DR   BioMuta; TTC26; -.
DR   EPD; A0AVF1; -.
DR   jPOST; A0AVF1; -.
DR   MassIVE; A0AVF1; -.
DR   MaxQB; A0AVF1; -.
DR   PaxDb; 9606-ENSP00000419279; -.
DR   PeptideAtlas; A0AVF1; -.
DR   ProteomicsDB; 16; -. [A0AVF1-1]
DR   ProteomicsDB; 17; -. [A0AVF1-2]
DR   ProteomicsDB; 29874; -.
DR   Pumba; A0AVF1; -.
DR   Antibodypedia; 52471; 107 antibodies from 18 providers.
DR   DNASU; 79989; -.
DR   Ensembl; ENST00000343187.8; ENSP00000339135.4; ENSG00000105948.13. [A0AVF1-3]
DR   Ensembl; ENST00000430935.5; ENSP00000410655.1; ENSG00000105948.13. [A0AVF1-2]
DR   Ensembl; ENST00000464848.5; ENSP00000419279.1; ENSG00000105948.13. [A0AVF1-1]
DR   GeneID; 79989; -.
DR   KEGG; hsa:79989; -.
DR   MANE-Select; ENST00000464848.5; ENSP00000419279.1; NM_024926.4; NP_079202.2.
DR   UCSC; uc003vus.4; human. [A0AVF1-1]
DR   AGR; HGNC:21882; -.
DR   CTD; 79989; -.
DR   DisGeNET; 79989; -.
DR   GeneCards; IFT56; -.
DR   HGNC; HGNC:21882; IFT56.
DR   HPA; ENSG00000105948; Low tissue specificity.
DR   MalaCards; IFT56; -.
DR   MIM; 617453; gene.
DR   MIM; 619534; phenotype.
DR   neXtProt; NX_A0AVF1; -.
DR   OpenTargets; ENSG00000105948; -.
DR   PharmGKB; PA144596245; -.
DR   VEuPathDB; HostDB:ENSG00000105948; -.
DR   eggNOG; KOG3785; Eukaryota.
DR   GeneTree; ENSGT00390000000159; -.
DR   HOGENOM; CLU_036306_2_0_1; -.
DR   InParanoid; A0AVF1; -.
DR   OMA; FIIRRDY; -.
DR   OrthoDB; 5473627at2759; -.
DR   PhylomeDB; A0AVF1; -.
DR   TreeFam; TF105816; -.
DR   PathwayCommons; A0AVF1; -.
DR   Reactome; R-HSA-5620924; Intraflagellar transport.
DR   SignaLink; A0AVF1; -.
DR   BioGRID-ORCS; 79989; 5 hits in 1150 CRISPR screens.
DR   ChiTaRS; TTC26; human.
DR   GenomeRNAi; 79989; -.
DR   Pharos; A0AVF1; Tbio.
DR   PRO; PR:A0AVF1; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; A0AVF1; Protein.
DR   Bgee; ENSG00000105948; Expressed in bronchial epithelial cell and 120 other cell types or tissues.
DR   ExpressionAtlas; A0AVF1; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR   GO; GO:0097546; C:ciliary base; IBA:GO_Central.
DR   GO; GO:0097542; C:ciliary tip; TAS:Reactome.
DR   GO; GO:0005929; C:cilium; IMP:UniProtKB.
DR   GO; GO:0030992; C:intraciliary transport particle B; IPI:ComplexPortal.
DR   GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR   GO; GO:0120170; F:intraciliary transport particle B binding; IBA:GO_Central.
DR   GO; GO:0035082; P:axoneme assembly; ISS:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR   GO; GO:0035720; P:intraciliary anterograde transport; IBA:GO_Central.
DR   GO; GO:0042073; P:intraciliary transport; ISS:UniProtKB.
DR   GO; GO:0035735; P:intraciliary transport involved in cilium assembly; IBA:GO_Central.
DR   GO; GO:1905198; P:manchette assembly; IEA:Ensembl.
DR   GO; GO:0061512; P:protein localization to cilium; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0007224; P:smoothened signaling pathway; ISS:UniProtKB.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR030511; TTC26.
DR   PANTHER; PTHR14781:SF0; INTRAFLAGELLAR TRANSPORT PROTEIN 56; 1.
DR   PANTHER; PTHR14781; UNCHARACTERIZED; 1.
DR   Pfam; PF12895; ANAPC3; 1.
DR   SMART; SM00028; TPR; 5.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS50293; TPR_REGION; 2.
DR   Genevisible; A0AVF1; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; Ciliopathy; Cilium; Disease variant;
KW   Protein transport; Reference proteome; Repeat; TPR repeat; Transport.
FT   CHAIN           1..554
FT                   /note="Intraflagellar transport protein 56"
FT                   /id="PRO_0000289082"
FT   REPEAT          57..90
FT                   /note="TPR 1"
FT   REPEAT          92..125
FT                   /note="TPR 2"
FT   REPEAT          151..184
FT                   /note="TPR 3"
FT   REPEAT          468..501
FT                   /note="TPR 4"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         47..77
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044791"
FT   VAR_SEQ         474..554
FT                   /note="MGQFYYSAKAFDVLERLDPNPEYWEGKRGACVGIFQMIIAGREPKETLREVL
FT                   HLLRSTGNTQVEYMIRIMKKWAKENRVSI -> RDPSRSAPFTEKHR (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_043751"
FT   VARIANT         263
FT                   /note="N -> S (in BRENS; decreased protein abundance;
FT                   associated with abnormal ciliary structure and function)"
FT                   /evidence="ECO:0000269|PubMed:31595528,
FT                   ECO:0000269|PubMed:32617964"
FT                   /id="VAR_086383"
FT   VARIANT         310
FT                   /note="D -> N (in dbSNP:rs13225917)"
FT                   /id="VAR_032568"
FT   VARIANT         444
FT                   /note="P -> L (in BRENS; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:31595528"
FT                   /id="VAR_086384"
FT   CONFLICT        85
FT                   /note="K -> E (in Ref. 1; BAB14143)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        271
FT                   /note="E -> V (in Ref. 1; BAH12956)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        470
FT                   /note="D -> V (in Ref. 1; BAB14143)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   554 AA;  64178 MW;  188062024DB89B97 CRC64;
     MMLSRAKPAV GRGVQHTDKR KKKGRKIPKL EELLSKRDFT GAITLLEFKR HVGEEEEDTN
     LWIGYCAFHL GDYKRALEEY ENATKEENCN SEVWVNLACT YFFLGMYKQA EAAGFKASKS
     RLQNRLLFHL AHKFNDEKKL MSFHQNLQDV TEDQLSLASI HYMRSHYQEA IDIYKRILLD
     NREYLALNVY VALCYYKLDY YDVSQEVLAV YLQQIPDSTI ALNLKACNHF RLYNGRAAEA
     ELKSLMDNAS SSFEFAKELI RHNLVVFRGG EGALQVLPPL VDVIPEARLN LVIYYLRQDD
     VQEAYNLIKD LEPTTPQEYI LKGVVNAALG QEMGSRDHMK IAQQFFQLVG GSASECDTIP
     GRQCMASCFF LLKQFDDVLI YLNSFKSYFY NDDIFNFNYA QAKAATGNTS EGEEAFLLIQ
     SEKMKNDYIY LSWLARCYIM NKKPRLAWEL YLKMETSGES FSLLQLIAND CYKMGQFYYS
     AKAFDVLERL DPNPEYWEGK RGACVGIFQM IIAGREPKET LREVLHLLRS TGNTQVEYMI
     RIMKKWAKEN RVSI
//