ID FRM4A_HUMAN Reviewed; 1039 AA.
AC Q9P2Q2; A7E2Y3; Q5T377;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 3.
DT 24-JAN-2024, entry version 171.
DE RecName: Full=FERM domain-containing protein 4A;
GN Name=FRMD4A {ECO:0000312|HGNC:HGNC:25491}; Synonyms=FRMD4, KIAA1294;
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].
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
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=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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604; SER-615; SER-800;
RP SER-872 AND SER-901, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Erythroleukemia;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530; SER-681 AND SER-800, AND
RP IDENTIFICATION BY 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).
RN [8]
RP INVOLVEMENT IN CCAFCA.
RX PubMed=25388005; DOI=10.1038/ejhg.2014.241;
RA Fine D., Flusser H., Markus B., Shorer Z., Gradstein L., Khateeb S.,
RA Langer Y., Narkis G., Birk R., Galil A., Shelef I., Birk O.S.;
RT "A syndrome of congenital microcephaly, intellectual disability and
RT dysmorphism with a homozygous mutation in FRMD4A.";
RL Eur. J. Hum. Genet. 23:1729-1734(2015).
RN [9]
RP FUNCTION.
RX PubMed=27044754; DOI=10.1242/jcs.180745;
RA Yan X., Nykaenen N.P., Brunello C.A., Haapasalo A., Hiltunen M.,
RA Uronen R.L., Huttunen H.J.;
RT "FRMD4A-cytohesin signaling modulates the cellular release of tau.";
RL J. Cell Sci. 129:2003-2015(2016).
CC -!- FUNCTION: Scaffolding protein that regulates epithelial cell polarity
CC by connecting ARF6 activation with the PAR3 complex (By similarity).
CC Plays a redundant role with FRMD4B in epithelial polarization (By
CC similarity). May regulate MAPT secretion by activating ARF6-signaling
CC (PubMed:27044754). {ECO:0000250|UniProtKB:Q8BIE6,
CC ECO:0000269|PubMed:27044754}.
CC -!- SUBUNIT: Interacts (via coiled-coil domain) with CYTH1 (via coiled-coil
CC domain). Interacts with PARD3 (via coiled-coil domain). Found in a
CC complex with PARD3, CYTH1 and FRMD4A. Interacts with CYTH2. Interacts
CC with CYTH3. {ECO:0000250|UniProtKB:Q8BIE6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC junction, adherens junction {ECO:0000250|UniProtKB:Q8BIE6}. Cell
CC junction, tight junction {ECO:0000250|UniProtKB:Q8BIE6}.
CC Note=Colocalized with CYTH1 at adherens junction and tight junction.
CC Colocalized with PARD3 during the process of epithelial polarization.
CC {ECO:0000250|UniProtKB:Q8BIE6}.
CC -!- DISEASE: Agenesis of the corpus callosum, with facial anomalies and
CC cerebellar ataxia (CCAFCA) [MIM:616819]: An autosomal recessive
CC intellectual disability syndrome characterized by congenital
CC microcephaly, low anterior hairline, bitemporal narrowing, low-set
CC protruding ears, strabismus and tented thick eyebrows with sparse hair
CC in their medial segment. {ECO:0000269|PubMed:25388005}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-16 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92532.1; 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; AB037715; BAA92532.1; ALT_INIT; mRNA.
DR EMBL; AK289693; BAF82382.1; -; mRNA.
DR EMBL; AC069025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL157392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL365495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC151244; AAI51245.1; -; mRNA.
DR CCDS; CCDS7101.1; -.
DR RefSeq; NP_001305265.1; NM_001318336.1.
DR RefSeq; NP_001305266.1; NM_001318337.1.
DR RefSeq; NP_001305267.1; NM_001318338.1.
DR RefSeq; NP_060497.3; NM_018027.4.
DR AlphaFoldDB; Q9P2Q2; -.
DR SMR; Q9P2Q2; -.
DR BioGRID; 120817; 15.
DR IntAct; Q9P2Q2; 8.
DR STRING; 9606.ENSP00000350032; -.
DR iPTMnet; Q9P2Q2; -.
DR PhosphoSitePlus; Q9P2Q2; -.
DR BioMuta; FRMD4A; -.
DR DMDM; 205371790; -.
DR EPD; Q9P2Q2; -.
DR jPOST; Q9P2Q2; -.
DR MassIVE; Q9P2Q2; -.
DR MaxQB; Q9P2Q2; -.
DR PaxDb; 9606-ENSP00000350032; -.
DR PeptideAtlas; Q9P2Q2; -.
DR ProteomicsDB; 83879; -.
DR Antibodypedia; 50861; 60 antibodies from 10 providers.
DR DNASU; 55691; -.
DR Ensembl; ENST00000357447.7; ENSP00000350032.2; ENSG00000151474.23.
DR GeneID; 55691; -.
DR KEGG; hsa:55691; -.
DR MANE-Select; ENST00000357447.7; ENSP00000350032.2; NM_018027.5; NP_060497.3.
DR UCSC; uc001ims.4; human.
DR AGR; HGNC:25491; -.
DR CTD; 55691; -.
DR DisGeNET; 55691; -.
DR GeneCards; FRMD4A; -.
DR HGNC; HGNC:25491; FRMD4A.
DR HPA; ENSG00000151474; Tissue enhanced (adipose).
DR MalaCards; FRMD4A; -.
DR MIM; 616305; gene.
DR MIM; 616819; phenotype.
DR neXtProt; NX_Q9P2Q2; -.
DR OpenTargets; ENSG00000151474; -.
DR Orphanet; 466688; Severe intellectual disability-corpus callosum agenesis-facial dysmorphism-cerebellar ataxia syndrome.
DR PharmGKB; PA134946784; -.
DR VEuPathDB; HostDB:ENSG00000151474; -.
DR eggNOG; KOG3529; Eukaryota.
DR GeneTree; ENSGT01020000230354; -.
DR InParanoid; Q9P2Q2; -.
DR OMA; SYNDSCY; -.
DR OrthoDB; 3400049at2759; -.
DR PhylomeDB; Q9P2Q2; -.
DR TreeFam; TF328984; -.
DR PathwayCommons; Q9P2Q2; -.
DR SignaLink; Q9P2Q2; -.
DR BioGRID-ORCS; 55691; 9 hits in 1152 CRISPR screens.
DR ChiTaRS; FRMD4A; human.
DR GenomeRNAi; 55691; -.
DR Pharos; Q9P2Q2; Tbio.
DR PRO; PR:Q9P2Q2; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9P2Q2; Protein.
DR Bgee; ENSG00000151474; Expressed in sural nerve and 183 other cell types or tissues.
DR ExpressionAtlas; Q9P2Q2; baseline and differential.
DR Genevisible; Q9P2Q2; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0005923; C:bicellular tight junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IMP:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; IEA:Ensembl.
DR GO; GO:0050709; P:negative regulation of protein secretion; IEA:Ensembl.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13191; FERM_C_FRMD4A_FRMD4B; 1.
DR CDD; cd17200; FERM_F1_FRMD4B; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR021774; CUPID.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR047176; FRMD4A/B.
DR InterPro; IPR041785; FRMD4A/B_FERM_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46079; FERM DOMAIN-CONTAINING PROTEIN 4; 1.
DR PANTHER; PTHR46079:SF3; FERM DOMAIN-CONTAINING PROTEIN 4A; 1.
DR Pfam; PF11819; CUPID; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR PRINTS; PR00935; BAND41.
DR SMART; SM00295; B41; 1.
DR SMART; SM01196; FERM_C; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 1: Evidence at protein level;
KW Cell junction; Coiled coil; Cytoplasm; Cytoskeleton;
KW Intellectual disability; Phosphoprotein; Reference proteome;
KW Tight junction.
FT CHAIN 1..1039
FT /note="FERM domain-containing protein 4A"
FT /id="PRO_0000219444"
FT DOMAIN 20..322
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 358..420
FT /note="Necessary for interaction with CYTH1"
FT /evidence="ECO:0000250|UniProtKB:Q8BIE6"
FT REGION 366..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 553..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..939
FT /note="Necessary for tight junction and adherens junction
FT localization; Requires for interaction with PARD3"
FT /evidence="ECO:0000250|UniProtKB:Q8BIE6"
FT REGION 713..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 772..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 382..416
FT /evidence="ECO:0000255"
FT COMPBIAS 569..584
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..802
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 948..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 711
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BIE6"
FT MOD_RES 800
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 872
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 901
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 242
FT /note="Q -> H (in dbSNP:rs11258565)"
FT /id="VAR_048367"
FT CONFLICT 859
FT /note="G -> C (in Ref. 1; BAA92532 and 4; AAI51245)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1039 AA; 115458 MW; D895CD6B569A683F CRC64;
MAVQLVPDSA LGLLMMTEGR RCQVHLLDDR KLELLVQPKL LAKELLDLVA SHFNLKEKEY
FGIAFTDETG HLNWLQLDRR VLEHDFPKKS GPVVLYFCVR FYIESISYLK DNATIELFFL
NAKSCIYKEL IDVDSEVVFE LASYILQEAK GDFSSNEVVR SDLKKLPALP TQALKEHPSL
AYCEDRVIEH YKKLNGQTRG QAIVNYMSIV ESLPTYGVHY YAVKDKQGIP WWLGLSYKGI
FQYDYHDKVK PRKIFQWRQL ENLYFREKKF SVEVHDPRRA SVTRRTFGHS GIAVHTWYAC
PALIKSIWAM AISQHQFYLD RKQSKSKIHA ARSLSEIAID LTETGTLKTS KLANMGSKGK
IISGSSGSLL SSGSQESDSS QSAKKDMLAA LKSRQEALEE TLRQRLEELK KLCLREAELT
GKLPVEYPLD PGEEPPIVRR RIGTAFKLDE QKILPKGEEA ELERLEREFA IQSQITEAAR
RLASDPNVSK KLKKQRKTSY LNALKKLQEI ENAINENRIK SGKKPTQRAS LIIDDGNIAS
EDSSLSDALV LEDEDSQVTS TISPLHSPHK GLPPRPPSHN RPPPPQSLEG LRQMHYHRND
YDKSPIKPKM WSESSLDEPY EKVKKRSSHS HSSSHKRFPS TGSCAEAGGG SNSLQNSPIR
GLPHWNSQSS MPSTPDLRVR SPHYVHSTRS VDISPTRLHS LALHFRHRSS SLESQGKLLG
SENDTGSPDF YTPRTRSSNG SDPMDDCSSC TSHSSSEHYY PAQMNANYST LAEDSPSKAR
QRQRQRQRAA GALGSASSGS MPNLAARGGA GGAGGAGGGV YLHSQSQPSS QYRIKEYPLY
IEGGATPVVV RSLESDQEGH YSVKAQFKTS NSYTAGGLFK ESWRGGGGDE GDTGRLTPSR
SQILRTPSLG REGAHDKGAG RAAVSDELRQ WYQRSTASHK EHSRLSHTSS TSSDSGSQYS
TSSQSTFVAH SRVTRMPQMC KATSAALPQS QRSSTPSSEI GATPPSSPHH ILTWQTGEAT
ENSPILDGSE SPPHQSTDE
//
