CKAP4_HUMAN
ID CKAP4_HUMAN Reviewed; 602 AA.
AC Q07065; Q504S5; Q53ES6;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Cytoskeleton-associated protein 4;
DE AltName: Full=63-kDa cytoskeleton-linking membrane protein;
DE Short=Climp-63;
DE Short=p63;
GN Name=CKAP4;
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], PROTEIN SEQUENCE OF 312-326; 413-429 AND
RP 491-504, SUBCELLULAR LOCATION, AND PALMITOYLATION.
RC TISSUE=Placenta;
RX PubMed=8314870; DOI=10.1242/jcs.104.3.685;
RA Schweizer A., Rohrer J., Jenoe P., De Maio A., Buchman T.G., Hauri H.-P.;
RT "A reversibly palmitoylated resident protein(p63) of an ER-Golgi
RT intermediate compartment is related to a circulatory shock resuscitation
RT protein.";
RL J. Cell Sci. 104:685-694(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Pancreas;
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 FUNCTION IN CYTOSKELETON ANCHORING, AND PHOSPHORYLATION AT SER-3; SER-17
RP AND SER-19.
RX PubMed=15703217; DOI=10.1091/mbc.e04-07-0554;
RA Vedrenne C., Klopfenstein D.R., Hauri H.P.;
RT "Phosphorylation controls CLIMP-63-mediated anchoring of the endoplasmic
RT reticulum to microtubules.";
RL Mol. Biol. Cell 16:1928-1937(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP FUNCTION AS APF RECEPTOR, AND SUBCELLULAR LOCATION.
RX PubMed=17030514; DOI=10.1074/jbc.m604581200;
RA Conrads T.P., Tocci G.M., Hood B.L., Zhang C.O., Guo L., Koch K.R.,
RA Michejda C.J., Veenstra T.D., Keay S.K.;
RT "CKAP4/p63 is a receptor for the frizzled-8 protein-related
RT antiproliferative factor from interstitial cystitis patients.";
RL J. Biol. Chem. 281:37836-37843(2006).
RN [8]
RP FUNCTION IN CYTOSKELETON ANCHORING, AND SUBCELLULAR LOCATION.
RX PubMed=17567679; DOI=10.1242/jcs.008979;
RA Nikonov A.V., Hauri H.P., Lauring B., Kreibich G.;
RT "Climp-63-mediated binding of microtubules to the ER affects the lateral
RT mobility of translocon complexes.";
RL J. Cell Sci. 120:2248-2258(2007).
RN [9]
RP PROTEIN SEQUENCE OF 79-102, SUBCELLULAR LOCATION, AND PALMITOYLATION AT
RP CYS-100.
RX PubMed=18296695; DOI=10.1074/mcp.m800069-mcp200;
RA Zhang J., Planey S.L., Ceballos C., Stevens S.M. Jr., Keay S.K.,
RA Zacharias D.A.;
RT "Identification of CKAP4/p63 as a major substrate of the palmitoyl
RT acyltransferase DHHC2, a putative tumor suppressor, using a novel
RT proteomics method.";
RL Mol. Cell. Proteomics 7:1378-1388(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND PALMITOYLATION AT CYS-100 BY ZDHHC2.
RX PubMed=19144824; DOI=10.1091/mbc.e08-08-0849;
RA Planey S.L., Keay S.K., Zhang C.O., Zacharias D.A.;
RT "Palmitoylation of cytoskeleton associated protein 4 by DHHC2 regulates
RT antiproliferative factor-mediated signaling.";
RL Mol. Biol. Cell 20:1454-1463(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
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 [15]
RP PHOSPHORYLATION AT SER-232.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP INTERACTION WITH REEP5.
RX PubMed=32075961; DOI=10.1038/s41467-019-14143-9;
RA Lee S.H., Hadipour-Lakmehsari S., Murthy H.R., Gibb N., Miyake T.,
RA Teng A.C.T., Cosme J., Yu J.C., Moon M., Lim S., Wong V., Liu P.,
RA Billia F., Fernandez-Gonzalez R., Stagljar I., Sharma P., Kislinger T.,
RA Scott I.C., Gramolini A.O.;
RT "REEP5 depletion causes sarco-endoplasmic reticulum vacuolization and
RT cardiac functional defects.";
RL Nat. Commun. 11:965-965(2020).
CC -!- FUNCTION: Mediates the anchoring of the endoplasmic reticulum to
CC microtubules. {ECO:0000269|PubMed:15703217}.
CC -!- FUNCTION: High-affinity epithelial cell surface receptor for the FZD8-
CC related low molecular weight sialoglycopeptide APF/antiproliferative
CC factor. Mediates the APF antiproliferative signaling within cells.
CC {ECO:0000269|PubMed:17030514, ECO:0000269|PubMed:19144824}.
CC -!- SUBUNIT: Interacts with REEP5. {ECO:0000269|PubMed:32075961}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:18296695, ECO:0000269|PubMed:19144824}; Single-pass
CC type II membrane protein. Cell membrane {ECO:0000269|PubMed:18296695,
CC ECO:0000269|PubMed:19144824}; Single-pass type II membrane protein.
CC Cytoplasm, cytoskeleton. Cytoplasm, perinuclear region.
CC Note=Translocates to the perinuclear region upon APF-stimulation.
CC -!- PTM: Reversibly palmitoylated. Palmitoylation at Cys-100 by ZDHHC2 is
CC required for its trafficking from the ER to the plasma membrane and for
CC its perinuclear localization. Palmitoylation by ZDHHC2 is also required
CC for its function in APF-mediated antiproliferative signaling
CC (PubMed:19144824). {ECO:0000269|PubMed:18296695,
CC ECO:0000269|PubMed:19144824, ECO:0000269|PubMed:8314870}.
CC -!- PTM: Increased phosphorylation during mitosis prevents binding to
CC microtubules. {ECO:0000269|PubMed:15703217}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH94824.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; X69910; CAA49535.2; -; mRNA.
DR EMBL; AK223563; BAD97283.1; -; mRNA.
DR EMBL; AC079174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC082972; AAH82972.1; -; mRNA.
DR EMBL; BC094824; AAH94824.1; ALT_SEQ; mRNA.
DR CCDS; CCDS9103.1; -.
DR PIR; S33377; S33377.
DR RefSeq; NP_006816.2; NM_006825.3.
DR AlphaFoldDB; Q07065; -.
DR SMR; Q07065; -.
DR BioGRID; 116167; 575.
DR IntAct; Q07065; 137.
DR MINT; Q07065; -.
DR STRING; 9606.ENSP00000367265; -.
DR ChEMBL; CHEMBL4296025; -.
DR TCDB; 8.A.149.1.1; the cytoskeleton-associated protein 4 (ckap4) family.
DR GlyGen; Q07065; 3 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q07065; -.
DR PhosphoSitePlus; Q07065; -.
DR SwissPalm; Q07065; -.
DR BioMuta; CKAP4; -.
DR DMDM; 74735614; -.
DR CPTAC; CPTAC-335; -.
DR CPTAC; CPTAC-336; -.
DR EPD; Q07065; -.
DR jPOST; Q07065; -.
DR MassIVE; Q07065; -.
DR MaxQB; Q07065; -.
DR PaxDb; Q07065; -.
DR PeptideAtlas; Q07065; -.
DR PRIDE; Q07065; -.
DR ProteomicsDB; 58501; -.
DR Antibodypedia; 613; 303 antibodies from 34 providers.
DR DNASU; 10970; -.
DR Ensembl; ENST00000378026.5; ENSP00000367265.4; ENSG00000136026.14.
DR GeneID; 10970; -.
DR KEGG; hsa:10970; -.
DR MANE-Select; ENST00000378026.5; ENSP00000367265.4; NM_006825.4; NP_006816.2.
DR UCSC; uc001tlk.4; human.
DR CTD; 10970; -.
DR DisGeNET; 10970; -.
DR GeneCards; CKAP4; -.
DR HGNC; HGNC:16991; CKAP4.
DR HPA; ENSG00000136026; Low tissue specificity.
DR MIM; 618595; gene.
DR neXtProt; NX_Q07065; -.
DR OpenTargets; ENSG00000136026; -.
DR PharmGKB; PA26527; -.
DR VEuPathDB; HostDB:ENSG00000136026; -.
DR eggNOG; ENOG502QVCP; Eukaryota.
DR GeneTree; ENSGT00390000015968; -.
DR HOGENOM; CLU_032481_0_0_1; -.
DR InParanoid; Q07065; -.
DR OMA; EAADTEH; -.
DR OrthoDB; 1255457at2759; -.
DR PhylomeDB; Q07065; -.
DR TreeFam; TF332395; -.
DR PathwayCommons; Q07065; -.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-5683826; Surfactant metabolism.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR SignaLink; Q07065; -.
DR BioGRID-ORCS; 10970; 15 hits in 1075 CRISPR screens.
DR ChiTaRS; CKAP4; human.
DR GeneWiki; CKAP4; -.
DR GenomeRNAi; 10970; -.
DR Pharos; Q07065; Tbio.
DR PRO; PR:Q07065; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q07065; protein.
DR Bgee; ENSG00000136026; Expressed in tibia and 209 other tissues.
DR ExpressionAtlas; Q07065; baseline and differential.
DR Genevisible; Q07065; HS.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0042599; C:lamellar body; TAS:Reactome.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; TAS:ProtInc.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR InterPro; IPR028428; Ckap4.
DR PANTHER; PTHR45161; PTHR45161; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Endoplasmic reticulum; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..602
FT /note="Cytoskeleton-associated protein 4"
FT /id="PRO_0000252417"
FT TOPO_DOM 1..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..602
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 130..214
FT /evidence="ECO:0000255"
FT COILED 256..460
FT /evidence="ECO:0000255"
FT COILED 533..602
FT /evidence="ECO:0000255"
FT COMPBIAS 36..54
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15703217"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15703217,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15703217"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMK4"
FT MOD_RES 232
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT LIPID 100
FT /note="S-palmitoyl cysteine; by ZDHHC2"
FT /evidence="ECO:0000269|PubMed:18296695,
FT ECO:0000269|PubMed:19144824"
FT VARIANT 348
FT /note="A -> T (in dbSNP:rs3088113)"
FT /id="VAR_027853"
FT CONFLICT 60
FT /note="Q -> R (in Ref. 2; BAD97283)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="S -> P (in Ref. 4; AAH94824)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 602 AA; 66022 MW; 216E6A92ED5E058A CRC64;
MPSAKQRGSK GGHGAASPSE KGAHPSGGAD DVAKKPPPAP QQPPPPPAPH PQQHPQQHPQ
NQAHGKGGHR GGGGGGGKSS SSSSASAAAA AAAASSSASC SRRLGRALNF LFYLALVAAA
AFSGWCVHHV LEEVQQVRRS HQDFSRQREE LGQGLQGVEQ KVQSLQATFG TFESILRSSQ
HKQDLTEKAV KQGESEVSRI SEVLQKLQNE ILKDLSDGIH VVKDARERDF TSLENTVEER
LTELTKSIND NIAIFTEVQK RSQKEINDMK AKVASLEESE GNKQDLKALK EAVKEIQTSA
KSREWDMEAL RSTLQTMESD IYTEVRELVS LKQEQQAFKE AADTERLALQ ALTEKLLRSE
ESVSRLPEEI RRLEEELRQL KSDSHGPKED GGFRHSEAFE ALQQKSQGLD SRLQHVEDGV
LSMQVASARQ TESLESLLSK SQEHEQRLAA LQGRLEGLGS SEADQDGLAS TVRSLGETQL
VLYGDVEELK RSVGELPSTV ESLQKVQEQV HTLLSQDQAQ AARLPPQDFL DRLSSLDNLK
ASVSQVEADL KMLRTAVDSL VAYSVKIETN ENNLESAKGL LDDLRNDLDR LFVKVEKIHE
KV
