ID   RFIP4_HUMAN             Reviewed;         637 AA.
AC   Q86YS3; Q52LI1; Q8N829; Q8NDT7; Q969D8;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 166.
DE   RecName: Full=Rab11 family-interacting protein 4;
DE            Short=FIP4-Rab11;
DE            Short=Rab11-FIP4;
DE   AltName: Full=Arfophilin-2;
GN   Name=RAB11FIP4; Synonyms=ARFO2, KIAA1821;
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), FUNCTION IN ENDOSOMAL TRAFFICKING,
RP   SUBUNIT, AND INTERACTION WITH RAB11A.
RX   PubMed=12470645; DOI=10.1016/s0006-291x(02)02720-1;
RA   Wallace D.M., Lindsay A.J., Hendrick A.G., McCaffrey M.W.;
RT   "Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its
RT   overexpression condenses the Rab11 positive compartment in HeLa cells.";
RL   Biochem. Biophys. Res. Commun. 299:770-779(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
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] (ISOFORM 1).
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 29-637 (ISOFORM 1).
RX   PubMed=12696059; DOI=10.1002/gcc.10206;
RA   Jenne D.E., Tinschert S., Dorschner M.O., Hameister H., Stephens K.,
RA   Kehrer-Sawatzki H.;
RT   "Complete physical map and gene content of the human NF1 tumor suppressor
RT   region in human and mouse.";
RL   Genes Chromosomes Cancer 37:111-120(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-637 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA   Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XX. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 8:85-95(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 342-637 (ISOFORM 1).
RC   TISSUE=Brain;
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   [7]
RP   SUBUNIT.
RX   PubMed=11944901; DOI=10.1006/bbrc.2002.6736;
RA   Wallace D.M., Lindsay A.J., Hendrick A.G., McCaffrey M.W.;
RT   "The novel Rab11-FIP/Rip/RCP family of proteins displays extensive
RT   homo- and hetero-interacting abilities.";
RL   Biochem. Biophys. Res. Commun. 292:909-915(2002).
RN   [8]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12857874; DOI=10.1091/mbc.e03-03-0160;
RA   Hickson G.R., Matheson J., Riggs B., Maier V.H., Fielding A.B.,
RA   Prekeris R., Sullivan W., Barr F.A., Gould G.W.;
RT   "Arfophilins are dual Arf/Rab 11 binding proteins that regulate recycling
RT   endosome distribution and are related to Drosophila nuclear fallout.";
RL   Mol. Biol. Cell 14:2908-2920(2003).
RN   [9]
RP   SUBCELLULAR LOCATION, INTERACTION WITH RAB11A AND ARF6, AND MUTAGENESIS OF
RP   ASP-627.
RX   PubMed=16148947; DOI=10.1038/sj.emboj.7600803;
RA   Fielding A.B., Schonteich E., Matheson J., Wilson G., Yu X., Hickson G.R.,
RA   Srivastava S., Baldwin S.A., Prekeris R., Gould G.W.;
RT   "Rab11-FIP3 and FIP4 interact with Arf6 and the exocyst to control membrane
RT   traffic in cytokinesis.";
RL   EMBO J. 24:3389-3399(2005).
RN   [10]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH RAB11A.
RX   PubMed=15601896; DOI=10.1091/mbc.e04-10-0927;
RA   Wilson G.M., Fielding A.B., Simon G.C., Yu X., Andrews P.D., Hames R.S.,
RA   Frey A.M., Peden A.A., Gould G.W., Prekeris R.;
RT   "The FIP3-Rab11 protein complex regulates recycling endosome targeting to
RT   the cleavage furrow during late cytokinesis.";
RL   Mol. Biol. Cell 16:849-860(2005).
RN   [11]
RP   INTERACTION WITH HUMAN CYTOMEGALOVIRUS GM/UL100 (MICROBIAL INFECTION).
RX   PubMed=19761540; DOI=10.1111/j.1600-0854.2009.00967.x;
RA   Krzyzaniak M.A., Mach M., Britt W.J.;
RT   "HCMV-encoded glycoprotein M (UL100) interacts with Rab11 effector protein
RT   FIP4.";
RL   Traffic 10:1439-1457(2009).
RN   [12]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH ECPAS.
RX   PubMed=20682791; DOI=10.1074/jbc.m110.154120;
RA   Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E.,
RA   Rechsteiner M.;
RT   "A protein interaction network for Ecm29 links the 26 S proteasome to
RT   molecular motors and endosomal components.";
RL   J. Biol. Chem. 285:31616-31633(2010).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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).
CC   -!- FUNCTION: Acts as a regulator of endocytic traffic by participating in
CC       membrane delivery. Required for the abcission step in cytokinesis,
CC       possibly by acting as an 'address tag' delivering recycling endosome
CC       membranes to the cleavage furrow during late cytokinesis. In case of
CC       infection by HCMV (human cytomegalovirus), may participate in egress of
CC       the virus out of nucleus; this function is independent of ARF6.
CC       {ECO:0000269|PubMed:12470645}.
CC   -!- SUBUNIT: Homodimer. Forms a complex with Rab11 (RAB11A or RAB11B) and
CC       ARF6. Interacts with RAB11A; the interaction is direct. Forms a
CC       heterooligomeric complex with RAB11FIP2, RAB11FIP3 and RAB11FIP5.
CC       Interacts with ECPAS. {ECO:0000269|PubMed:11944901,
CC       ECO:0000269|PubMed:12470645, ECO:0000269|PubMed:15601896,
CC       ECO:0000269|PubMed:16148947, ECO:0000269|PubMed:19761540,
CC       ECO:0000269|PubMed:20682791}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with human
CC       cytomegalovirus/HHV-5 protein gM/UL100. {ECO:0000269|PubMed:19761540}.
CC   -!- INTERACTION:
CC       Q86YS3; Q9UI95: MAD2L2; NbExp=3; IntAct=EBI-949727, EBI-77889;
CC       Q86YS3; P62331: Arf6; Xeno; NbExp=2; IntAct=EBI-949727, EBI-988682;
CC       Q86YS3-1; P62491: RAB11A; NbExp=2; IntAct=EBI-15605259, EBI-745098;
CC   -!- SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:20682791}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12857874}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000269|PubMed:12857874}. Recycling endosome membrane
CC       {ECO:0000269|PubMed:15601896}; Peripheral membrane protein. Cleavage
CC       furrow {ECO:0000269|PubMed:15601896}. Midbody
CC       {ECO:0000269|PubMed:12857874, ECO:0000269|PubMed:15601896}. Cytoplasmic
CC       vesicle {ECO:0000269|PubMed:15601896}. Note=Recruited to the cleavage
CC       furrow and the midbody during cytokinesis.
CC       {ECO:0000269|PubMed:15601896}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q86YS3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q86YS3-2; Sequence=VSP_013724, VSP_013725;
CC   -!- TISSUE SPECIFICITY: Present at high level in testis (at protein level).
CC       Weakly expressed in other tissues. {ECO:0000269|PubMed:12857874}.
CC   -!- DOMAIN: The RBD-FIP domain mediates the interaction with Rab11 (RAB11A
CC       or RAB11B). {ECO:0000250}.
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DR   EMBL; AY169244; AAO21970.1; -; mRNA.
DR   EMBL; AK097424; BAC05045.1; -; mRNA.
DR   EMBL; BC093914; AAH93914.1; -; mRNA.
DR   EMBL; BC101517; AAI01518.1; -; mRNA.
DR   EMBL; AJ314646; CAC44535.1; -; mRNA.
DR   EMBL; AB058724; BAB47450.1; -; mRNA.
DR   EMBL; AL831830; CAD38543.1; -; mRNA.
DR   CCDS; CCDS11267.1; -. [Q86YS3-1]
DR   CCDS; CCDS76985.1; -. [Q86YS3-2]
DR   RefSeq; NP_001290471.2; NM_001303542.2. [Q86YS3-2]
DR   RefSeq; NP_001333677.1; NM_001346748.1.
DR   RefSeq; NP_001333678.1; NM_001346749.1.
DR   RefSeq; NP_116321.2; NM_032932.5. [Q86YS3-1]
DR   AlphaFoldDB; Q86YS3; -.
DR   SMR; Q86YS3; -.
DR   BioGRID; 124079; 24.
DR   DIP; DIP-47495N; -.
DR   IntAct; Q86YS3; 17.
DR   MINT; Q86YS3; -.
DR   STRING; 9606.ENSP00000482620; -.
DR   iPTMnet; Q86YS3; -.
DR   PhosphoSitePlus; Q86YS3; -.
DR   BioMuta; RAB11FIP4; -.
DR   DMDM; 67472134; -.
DR   EPD; Q86YS3; -.
DR   jPOST; Q86YS3; -.
DR   MassIVE; Q86YS3; -.
DR   MaxQB; Q86YS3; -.
DR   PaxDb; 9606-ENSP00000482620; -.
DR   PeptideAtlas; Q86YS3; -.
DR   ProteomicsDB; 70461; -. [Q86YS3-1]
DR   ProteomicsDB; 70462; -. [Q86YS3-2]
DR   Antibodypedia; 54771; 139 antibodies from 20 providers.
DR   DNASU; 84440; -.
DR   Ensembl; ENST00000394744.6; ENSP00000378227.2; ENSG00000131242.18. [Q86YS3-2]
DR   Ensembl; ENST00000621161.5; ENSP00000482620.1; ENSG00000131242.18. [Q86YS3-1]
DR   GeneID; 84440; -.
DR   KEGG; hsa:84440; -.
DR   MANE-Select; ENST00000621161.5; ENSP00000482620.1; NM_032932.6; NP_116321.2.
DR   UCSC; uc032fao.2; human. [Q86YS3-1]
DR   AGR; HGNC:30267; -.
DR   CTD; 84440; -.
DR   DisGeNET; 84440; -.
DR   GeneCards; RAB11FIP4; -.
DR   HGNC; HGNC:30267; RAB11FIP4.
DR   HPA; ENSG00000131242; Tissue enhanced (brain, testis).
DR   MIM; 611999; gene.
DR   neXtProt; NX_Q86YS3; -.
DR   OpenTargets; ENSG00000131242; -.
DR   PharmGKB; PA134978007; -.
DR   VEuPathDB; HostDB:ENSG00000131242; -.
DR   eggNOG; KOG0982; Eukaryota.
DR   GeneTree; ENSGT00440000033742; -.
DR   HOGENOM; CLU_018925_1_1_1; -.
DR   InParanoid; Q86YS3; -.
DR   OMA; RQYMDKV; -.
DR   OrthoDB; 5312348at2759; -.
DR   PhylomeDB; Q86YS3; -.
DR   TreeFam; TF327221; -.
DR   PathwayCommons; Q86YS3; -.
DR   SignaLink; Q86YS3; -.
DR   BioGRID-ORCS; 84440; 22 hits in 1159 CRISPR screens.
DR   ChiTaRS; RAB11FIP4; human.
DR   GeneWiki; RAB11FIP4; -.
DR   GenomeRNAi; 84440; -.
DR   Pharos; Q86YS3; Tbio.
DR   PRO; PR:Q86YS3; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q86YS3; Protein.
DR   Bgee; ENSG00000131242; Expressed in prefrontal cortex and 142 other cell types or tissues.
DR   ExpressionAtlas; Q86YS3; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB.
DR   GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR   GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR   GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR   GO; GO:0032456; P:endocytic recycling; IBA:GO_Central.
DR   GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
DR   Gene3D; 1.20.5.2440; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR037245; FIP-RBD_C_sf.
DR   InterPro; IPR019018; Rab-bd_FIP-RBD.
DR   PANTHER; PTHR15726:SF5; RAB11 FAMILY-INTERACTING PROTEIN 4; 1.
DR   PANTHER; PTHR15726; RAB11-FAMILY INTERACTING PROTEIN; 1.
DR   Pfam; PF09457; RBD-FIP; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF144270; Eferin C-derminal domain-like; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
DR   PROSITE; PS51511; FIP_RBD; 1.
DR   Genevisible; Q86YS3; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW   Cytoskeleton; Endosome; Host-virus interaction; Membrane; Metal-binding;
KW   Reference proteome; Transport.
FT   CHAIN           1..637
FT                   /note="Rab11 family-interacting protein 4"
FT                   /id="PRO_0000073880"
FT   DOMAIN          49..84
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          574..636
FT                   /note="FIP-RBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00844"
FT   REGION          82..637
FT                   /note="Necessary for interaction with RAB11A, subcellular
FT                   location, homo- or heterooligomerization"
FT   REGION          138..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          219..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          280..617
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        155..169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         62
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000305"
FT   BINDING         64
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000305"
FT   BINDING         68
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000305"
FT   BINDING         73
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000305"
FT   VAR_SEQ         1..102
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_013724"
FT   VAR_SEQ         103..111
FT                   /note="APEIPDCVE -> MRTPPALGS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_013725"
FT   MUTAGEN         627
FT                   /note="D->A: Abolishes Rab11-binding."
FT                   /evidence="ECO:0000269|PubMed:16148947"
FT   CONFLICT        417
FT                   /note="T -> I (in Ref. 2; BAC05045)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        518
FT                   /note="E -> G (in Ref. 2; BAC05045)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   637 AA;  71928 MW;  8A5CDB9799383342 CRC64;
     MAGGAGWSGA PAALLRSVRR LREVFEVCGR DPDGFLRVER VAALGLRFGQ GEEVEKLVKY
     LDPNDLGRIN FKDFCRGVFA MKGCEELLKD VLSVESAGTL PCAPEIPDCV EQGSEVTGPT
     FADGELIPRE PGFFPEDEEE AMTLAPPEGP QELYTDSPME STQSLEGSVG SPAEKDGGLG
     GLFLPEDKSL VHTPSMTTSD LSTHSTTSLI SNEEQFEDYG EGDDVDCAPS SPCPDDETRT
     NVYSDLGSSV SSSAGQTPRK MRHVYNSELL DVYCSQCCKK INLLNDLEAR LKNLKANSPN
     RKISSTAFGR QLMHSSNFSS SNGSTEDLFR DSIDSCDNDI TEKVSFLEKK VTELENDSLT
     NGDLKSKLKQ ENTQLVHRVH ELEEMVKDQE TTAEQALEEE ARRHREAYGK LEREKATEVE
     LLNARVQQLE EENTELRTTV TRLKSQTEKL DEERQRMSDR LEDTSLRLKD EMDLYKRMMD
     KLRQNRLEFQ KEREATQELI EDLRKELEHL QMYKLDCERP GRGRSASSGL GEFNARAREV
     ELEHEVKRLK QENYKLRDQN DDLNGQILSL SLYEAKNLFA AQTKAQSLAA EIDTASRDEL
     MEALKEQEEI NFRLRQYMDK IILAILDHNP SILEIKH
//