ID   FLIP1_HUMAN             Reviewed;        1213 AA.
AC   Q7Z7B0; B2RMU6; Q5VUL6; Q86TC3; Q8N8B9; Q96SK6; Q9NVI8; Q9ULE5;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   24-JAN-2024, entry version 143.
DE   RecName: Full=Filamin-A-interacting protein 1;
DE            Short=FILIP;
GN   Name=FILIP1; Synonyms=KIAA1275;
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   Nagano T., Sato M.;
RT   "Human orthologue of L-FILIP.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 550-1213 (ISOFORM 3).
RC   TISSUE=Small intestine;
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 MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Skeletal muscle, and Small intestine;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 74-1213 (ISOFORM 1), AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA   Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XV. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:337-345(1999).
RN   [8]
RP   INTERACTION WITH RHOD AND FLNA, AND SUBCELLULAR LOCATION.
RX   PubMed=23087206; DOI=10.1091/mbc.e12-07-0555;
RA   Gad A.K., Nehru V., Ruusala A., Aspenstrom P.;
RT   "RhoD regulates cytoskeletal dynamics via the actin nucleation-promoting
RT   factor WASp homologue associated with actin Golgi membranes and
RT   microtubules.";
RL   Mol. Biol. Cell 23:4807-4819(2012).
CC   -!- FUNCTION: By acting through a filamin-A/F-actin axis, it controls the
CC       start of neocortical cell migration from the ventricular zone. May be
CC       able to induce the degradation of filamin-A.
CC       {ECO:0000250|UniProtKB:Q8K4T4}.
CC   -!- SUBUNIT: Interacts with FLNA. Interacts with RHOD (in GTP-bound form).
CC       {ECO:0000269|PubMed:23087206}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:23087206}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=L-FILIP;
CC         IsoId=Q7Z7B0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7Z7B0-2; Sequence=VSP_018345;
CC       Name=3; Synonyms=S-FILIP;
CC         IsoId=Q7Z7B0-3; Sequence=VSP_018344;
CC   -!- TISSUE SPECIFICITY: Moderately expressed in adult heart and brain.
CC       Weakly expressed in lung, skeletal muscle, ovary, testis, kidney, and
CC       fetal brain, and hardly detectable in liver, pancreas, spleen, and
CC       fetal liver. Within brain, moderate expression is found in amygdala and
CC       caudate nucleus. {ECO:0000269|PubMed:10574462}.
CC   -!- SIMILARITY: Belongs to the FILIP1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA91763.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB086011; BAC77067.1; -; mRNA.
DR   EMBL; AK001570; BAA91763.1; ALT_INIT; mRNA.
DR   EMBL; AK027705; BAB55310.1; -; mRNA.
DR   EMBL; AK097021; BAC04928.1; -; mRNA.
DR   EMBL; AL832009; CAD89912.1; -; mRNA.
DR   EMBL; BX647178; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AL445465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL589649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471051; EAW48737.1; -; Genomic_DNA.
DR   EMBL; BC136443; AAI36444.1; -; mRNA.
DR   EMBL; BC136444; AAI36445.1; -; mRNA.
DR   EMBL; AB033101; BAA86589.1; -; mRNA.
DR   CCDS; CCDS4984.1; -. [Q7Z7B0-1]
DR   CCDS; CCDS75480.1; -. [Q7Z7B0-2]
DR   RefSeq; NP_001276916.1; NM_001289987.2.
DR   RefSeq; NP_001287795.1; NM_001300866.2. [Q7Z7B0-2]
DR   RefSeq; NP_056502.1; NM_015687.4. [Q7Z7B0-1]
DR   RefSeq; XP_005248770.1; XM_005248713.3. [Q7Z7B0-1]
DR   RefSeq; XP_011534058.1; XM_011535756.2. [Q7Z7B0-3]
DR   AlphaFoldDB; Q7Z7B0; -.
DR   SMR; Q7Z7B0; -.
DR   BioGRID; 118029; 27.
DR   CORUM; Q7Z7B0; -.
DR   IntAct; Q7Z7B0; 5.
DR   MINT; Q7Z7B0; -.
DR   STRING; 9606.ENSP00000237172; -.
DR   GlyCosmos; Q7Z7B0; 2 sites, 1 glycan.
DR   GlyGen; Q7Z7B0; 5 sites, 1 O-linked glycan (5 sites).
DR   iPTMnet; Q7Z7B0; -.
DR   PhosphoSitePlus; Q7Z7B0; -.
DR   SwissPalm; Q7Z7B0; -.
DR   BioMuta; FILIP1; -.
DR   DMDM; 74750226; -.
DR   EPD; Q7Z7B0; -.
DR   jPOST; Q7Z7B0; -.
DR   MassIVE; Q7Z7B0; -.
DR   MaxQB; Q7Z7B0; -.
DR   PaxDb; 9606-ENSP00000237172; -.
DR   PeptideAtlas; Q7Z7B0; -.
DR   ProteomicsDB; 69507; -. [Q7Z7B0-1]
DR   ProteomicsDB; 69508; -. [Q7Z7B0-2]
DR   ProteomicsDB; 69509; -. [Q7Z7B0-3]
DR   Antibodypedia; 55048; 45 antibodies from 14 providers.
DR   DNASU; 27145; -.
DR   Ensembl; ENST00000237172.12; ENSP00000237172.7; ENSG00000118407.15. [Q7Z7B0-1]
DR   Ensembl; ENST00000393004.6; ENSP00000376728.1; ENSG00000118407.15. [Q7Z7B0-2]
DR   GeneID; 27145; -.
DR   KEGG; hsa:27145; -.
DR   MANE-Select; ENST00000237172.12; ENSP00000237172.7; NM_015687.5; NP_056502.1.
DR   UCSC; uc003phy.2; human. [Q7Z7B0-1]
DR   AGR; HGNC:21015; -.
DR   CTD; 27145; -.
DR   DisGeNET; 27145; -.
DR   GeneCards; FILIP1; -.
DR   HGNC; HGNC:21015; FILIP1.
DR   HPA; ENSG00000118407; Tissue enhanced (heart muscle, skeletal muscle, tongue).
DR   MIM; 607307; gene.
DR   neXtProt; NX_Q7Z7B0; -.
DR   OpenTargets; ENSG00000118407; -.
DR   PharmGKB; PA134992638; -.
DR   VEuPathDB; HostDB:ENSG00000118407; -.
DR   eggNOG; ENOG502QRWK; Eukaryota.
DR   GeneTree; ENSGT00950000182852; -.
DR   InParanoid; Q7Z7B0; -.
DR   OMA; ITHEKGP; -.
DR   OrthoDB; 5313111at2759; -.
DR   PhylomeDB; Q7Z7B0; -.
DR   TreeFam; TF331399; -.
DR   PathwayCommons; Q7Z7B0; -.
DR   Reactome; R-HSA-9013405; RHOD GTPase cycle.
DR   SignaLink; Q7Z7B0; -.
DR   BioGRID-ORCS; 27145; 12 hits in 1142 CRISPR screens.
DR   ChiTaRS; FILIP1; human.
DR   GeneWiki; FILIP1; -.
DR   GenomeRNAi; 27145; -.
DR   Pharos; Q7Z7B0; Tdark.
DR   PRO; PR:Q7Z7B0; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q7Z7B0; Protein.
DR   Bgee; ENSG00000118407; Expressed in left ventricle myocardium and 159 other cell types or tissues.
DR   ExpressionAtlas; Q7Z7B0; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0099010; P:modification of postsynaptic structure; IEA:Ensembl.
DR   InterPro; IPR019131; Cortactin-binding_p2_N.
DR   PANTHER; PTHR23166:SF3; FILAMIN-A-INTERACTING PROTEIN 1; 1.
DR   PANTHER; PTHR23166; FILAMIN/GPBP-INTERACTING PROTEIN; 1.
DR   Pfam; PF09727; CortBP2; 1.
DR   Genevisible; Q7Z7B0; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..1213
FT                   /note="Filamin-A-interacting protein 1"
FT                   /id="PRO_0000234540"
FT   REGION          1..70
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          878..900
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          949..976
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1103..1213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          192..591
FT                   /evidence="ECO:0000255"
FT   COILED          624..781
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        31..70
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1103..1159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1196..1213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         138
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K4T4"
FT   MOD_RES         979
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CS72"
FT   VAR_SEQ         1..248
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_018344"
FT   VAR_SEQ         1165..1213
FT                   /note="GMKAGKPVVAAPGAGNLTKFEPRAETQSMKIELKKSAASSTTSLGGGKG ->
FT                   ESIIIHQLRMNSR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_018345"
FT   VARIANT         1003
FT                   /note="P -> S (in dbSNP:rs34807169)"
FT                   /id="VAR_050995"
FT   CONFLICT        40
FT                   /note="K -> R (in Ref. 3; CAD89912)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        74..90
FT                   /note="ELSKEDLIQLLSIMEGE -> AQYAIYIVSRLILLHFL (in Ref. 2;
FT                   BAA86589)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        348
FT                   /note="T -> I (in Ref. 3; CAD89912)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        373
FT                   /note="N -> D (in Ref. 3; BX647178)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        421
FT                   /note="L -> F (in Ref. 2; BAC04928)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        723
FT                   /note="E -> G (in Ref. 2; BAB55310)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        793
FT                   /note="R -> K (in Ref. 2; BAB55310)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1045
FT                   /note="T -> A (in Ref. 3; BX647178)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1102
FT                   /note="E -> G (in Ref. 3; CAD89912)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1213 AA;  138109 MW;  EE4329B03516E6AF CRC64;
     MRSRNQGGES ASDGHISCPK PSIIGNAGEK SLSEDAKKKK KSNRKEDDVM ASGTVKRHLK
     TSGECERKTK KSLELSKEDL IQLLSIMEGE LQAREDVIHM LKTEKTKPEV LEAHYGSAEP
     EKVLRVLHRD AILAQEKSIG EDVYEKPISE LDRLEEKQKE TYRRMLEQLL LAEKCHRRTV
     YELENEKHKH TDYMNKSDDF TNLLEQERER LKKLLEQEKA YQARKEKENA KRLNKLRDEL
     VKLKSFALML VDERQMHIEQ LGLQSQKVQD LTQKLREEEE KLKAITSKSK EDRQKLLKLE
     VDFEHKASRF SQEHEEMNAK LANQESHNRQ LRLKLVGLTQ RIEELEETNK NLQKAEEELQ
     ELRDKIAKGE CGNSSLMAEV ENLRKRVLEM EGKDEEITKT ESQCRELRKK LQEEEHHSKE
     LRLEVEKLQK RMSELEKLEE AFSKSKSECT QLHLNLEKEK NLTKDLLNEL EVVKSRVKEL
     ECSESRLEKA ELSLKDDLTK LKSFTVMLVD ERKNMMEKIK QEERKVDGLN KNFKVEQGKV
     MDVTEKLIEE SKKLLKLKSE MEEKVYNLTR ERDELIGKLK SEEEKSSELS CSVDLLKKRL
     DGIEEVEREI TRGRSRKGSE LTCPEDNKIK ELTLEIERLK KRLQQLEVVE GDLMKTEDEY
     DQLEQKFRTE QDKANFLSQQ LEEIKHQIAK NKAIEKGEVV SQEAELRHRF RLEEAKSRDL
     KAEVQALKEK IHELMNKEDQ LSQLQVDYSV LQQRFMEEEN KNKNMGQEVL NLTKELELSK
     RYSRALRPSV NGRRMVDVPV TSTGVQTDAV SGEAAEEETP AVFIRKSFQE ENHIMSNLRQ
     VGLKKPVERS SVLDRYPPAA NELTMRKSWI PWMRKRENGP SITQEKGPRT NSSPGHPGEV
     VLSPKQGQPL HIRVTPDHEN STATLEITSP TSEEFFSSTT VIPTLGNQKP RITIIPSPNV
     MPQKQKSGDT TLGPERAMSP VTITTFSREK TPESGRGAFA DRPTSPIQIM TVSTSAAPAE
     IAVSPESQEM PMGRTILKVT PEKQTVPTPV RKYNSNANII TTEDNKIHIH LGSQFKRSPG
     TSGEGVSPVI TVRPVNVTAE KEVSTGTVLR SPRNHLSSRP GASKVTSTIT ITPVTTSSAR
     GTQSVSGQDG SSQRPTPTRI PMSKGMKAGK PVVAAPGAGN LTKFEPRAET QSMKIELKKS
     AASSTTSLGG GKG
//