CLIP1_RAT
ID CLIP1_RAT Reviewed; 1320 AA.
AC Q9JK25; A0A0G2K3T3;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=CAP-Gly domain-containing linker protein 1;
DE AltName: Full=Cytoplasmic linker protein 170 {ECO:0000303|PubMed:11290329, ECO:0000303|PubMed:20519438, ECO:0000303|PubMed:26972003};
DE Short=CLIP-170 {ECO:0000303|PubMed:11290329, ECO:0000303|PubMed:20519438, ECO:0000303|PubMed:26972003};
DE AltName: Full=Restin;
GN Name=Clip1; Synonyms=Cyln1, Rsn;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Hippocampus;
RX PubMed=11290329; DOI=10.1016/s0092-8674(01)00288-4;
RA Akhmanova A., Hoogenraad C.C., Drabek K., Stepanova T., Dortland B.,
RA Verkerk T., Vermeulen W., Burgering B.M., de Zeeuw C.I., Grosveld F.,
RA Galjart N.;
RT "Clasps are CLIP-115 and -170 associating proteins involved in the regional
RT regulation of microtubule dynamics in motile fibroblasts.";
RL Cell 104:923-935(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP PHOSPHORYLATION AT SER-309; SER-311; SER-314 AND SER-347, MUTAGENESIS OF
RP SER-309; SER-311; SER-313; SER-319 AND SER-320, AND INTERACTION WITH DCTN1.
RX PubMed=20519438; DOI=10.1091/mbc.e09-12-1036;
RA Lee H.S., Komarova Y.A., Nadezhdina E.S., Anjum R., Peloquin J.G.,
RA Schober J.M., Danciu O., van Haren J., Galjart N., Gygi S.P., Akhmanova A.,
RA Borisy G.G.;
RT "Phosphorylation controls autoinhibition of cytoplasmic linker protein-
RT 170.";
RL Mol. Biol. Cell 21:2661-2673(2010).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; SER-199; SER-203;
RP SER-309; SER-1116 AND SER-1246, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP PHOSPHORYLATION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-309; SER-311;
RP SER-313; SER-319 AND SER-320, INTERACTION WITH DCTN1, AND ASSOCIATION WITH
RP MICROTUBULES.
RX PubMed=26972003; DOI=10.1016/j.celrep.2016.02.046;
RA Nirschl J.J., Magiera M.M., Lazarus J.E., Janke C., Holzbaur E.L.;
RT "Alpha-tubulin tyrosination and CLIP-170 phosphorylation regulate the
RT initiation of dynein-driven transport in neurons.";
RL Cell Rep. 14:2637-2652(2016).
CC -!- FUNCTION: Binds to the plus end of microtubules and regulates the
CC dynamics of the microtubule cytoskeleton. Promotes microtubule growth
CC and microtubule bundling. Links cytoplasmic vesicles to microtubules
CC and thereby plays an important role in intracellular vesicle
CC trafficking. Plays a role macropinocytosis and endosome trafficking.
CC {ECO:0000250|UniProtKB:P30622}.
CC -!- SUBUNIT: Interacts with MTOR; phosphorylates and regulates CLIP1.
CC Interacts (via CAP-Gly domains) with tubulin and TUBA1B. Interacts with
CC SLAIN2. Interacts with MAPRE1 and MAPRE3 (By similarity). Interacts
CC (via zinc finger) with DCTN1 (PubMed:20519438, PubMed:26972003). Binds
CC preferentially to tyrosinated microtubules, and only marginally to
CC detyrosinated microtubules (PubMed:26972003).
CC {ECO:0000250|UniProtKB:P30622, ECO:0000269|PubMed:20519438,
CC ECO:0000269|PubMed:26972003}.
CC -!- INTERACTION:
CC Q9JK25; Q7Z460: CLASP1; Xeno; NbExp=2; IntAct=EBI-908338, EBI-913476;
CC Q9JK25; P67870: CSNK2B; Xeno; NbExp=2; IntAct=EBI-908338, EBI-348169;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P30622}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26972003}. Cytoplasmic
CC vesicle membrane {ECO:0000250|UniProtKB:P30622}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection,
CC ruffle {ECO:0000250|UniProtKB:P30622}. Note=Localizes to microtubule
CC plus ends. Localizes preferentially to the ends of tyrosinated
CC microtubules (PubMed:26972003). Accumulates in plasma membrane regions
CC with ruffling and protrusions. Associates with the membranes of
CC intermediate macropinocytic vesicles (By similarity).
CC {ECO:0000250|UniProtKB:P30622, ECO:0000269|PubMed:26972003}.
CC -!- DOMAIN: Intramolecular interaction between the zinc finger domain and
CC the CAP-Gly domains may inhibit interaction with tubulin.
CC {ECO:0000250|UniProtKB:P30622}.
CC -!- PTM: Phosphorylated. Phosphorylation induces conformational changes by
CC increasing the affinity of the N-terminus for C-terminus, resulting in
CC inhibition of its function thus decreasing its binding to microtubules
CC and DCTN1. Exhibits a folded, autoinhibited conformation when
CC phosphorylated and an open conformation when dephosphorylated with
CC increased binding affinity to microtubules and DCTN1. Phosphorylation
CC regulates its recruitment to tyrosinated microtubules and the
CC recruitment of vesicular cargo to microtubules in neurons
CC (PubMed:20519438, PubMed:26972003). Phosphorylation by MTOR may
CC positively regulate CLIP1 association with microtubules (By
CC similarity). {ECO:0000250|UniProtKB:P30622,
CC ECO:0000269|PubMed:20519438, ECO:0000269|PubMed:26972003}.
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DR EMBL; AJ237670; CAB92974.1; -; mRNA.
DR EMBL; AC117299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_113933.2; NM_031745.2.
DR AlphaFoldDB; Q9JK25; -.
DR SMR; Q9JK25; -.
DR IntAct; Q9JK25; 9.
DR MINT; Q9JK25; -.
DR STRING; 10116.ENSRNOP00000001685; -.
DR iPTMnet; Q9JK25; -.
DR PhosphoSitePlus; Q9JK25; -.
DR jPOST; Q9JK25; -.
DR PRIDE; Q9JK25; -.
DR Ensembl; ENSRNOT00000001685; ENSRNOP00000001685; ENSRNOG00000001247.
DR GeneID; 65201; -.
DR KEGG; rno:65201; -.
DR UCSC; RGD:67404; rat.
DR CTD; 6249; -.
DR RGD; 67404; Clip1.
DR eggNOG; KOG4568; Eukaryota.
DR GeneTree; ENSGT00940000155122; -.
DR OrthoDB; 1110101at2759; -.
DR PhylomeDB; Q9JK25; -.
DR PRO; PR:Q9JK25; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001247; Expressed in esophagus and 19 other tissues.
DR ExpressionAtlas; Q9JK25; baseline and differential.
DR Genevisible; Q9JK25; RN.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; ISO:RGD.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:RGD.
DR GO; GO:0035371; C:microtubule plus-end; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; ISO:RGD.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0001578; P:microtubule bundle formation; ISO:RGD.
DR GO; GO:1900006; P:positive regulation of dendrite development; IMP:RGD.
DR GO; GO:0031116; P:positive regulation of microtubule polymerization; ISO:RGD.
DR GO; GO:0044861; P:protein transport into plasma membrane raft; ISO:RGD.
DR Gene3D; 2.30.30.190; -; 2.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR032108; CLIP1_ZNF.
DR Pfam; PF01302; CAP_GLY; 2.
DR Pfam; PF16641; CLIP1_ZNF; 2.
DR SMART; SM01052; CAP_GLY; 2.
DR SUPFAM; SSF74924; SSF74924; 2.
DR PROSITE; PS00845; CAP_GLY_1; 2.
DR PROSITE; PS50245; CAP_GLY_2; 2.
PE 1: Evidence at protein level;
KW Cell projection; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Membrane; Metal-binding; Microtubule; Phosphoprotein; Reference proteome;
KW Repeat; Transport; Zinc; Zinc-finger.
FT CHAIN 1..1320
FT /note="CAP-Gly domain-containing linker protein 1"
FT /id="PRO_0000438322"
FT DOMAIN 78..120
FT /note="CAP-Gly 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT DOMAIN 231..273
FT /note="CAP-Gly 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00045"
FT ZN_FING 1299..1316
FT /note="CCHC-type"
FT /evidence="ECO:0000250|UniProtKB:P30622"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..101
FT /note="Important for tubulin binding"
FT /evidence="ECO:0000250|UniProtKB:P30622"
FT REGION 156..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30622"
FT MOD_RES 50
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30622"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30622"
FT MOD_RES 181
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P30622"
FT MOD_RES 194
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P30622"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20519438,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 311
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:20519438"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20519438"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:20519438"
FT MOD_RES 1116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MUTAGEN 309
FT /note="S->A: Phosphodeficient mutant which exhibits an open
FT conformation with a high affinity for microtubules and
FT DCTN1; when associated with A-311; A-313; A-319 and A-320."
FT /evidence="ECO:0000269|PubMed:20519438,
FT ECO:0000269|PubMed:26972003"
FT MUTAGEN 309
FT /note="S->E: Phosphomimetic mutant which exhibits a closed
FT autoinhibited conformation with a low affinity for
FT microtubules and DCTN1; when associated with E-311; E-313;
FT E-319 and E-320."
FT /evidence="ECO:0000269|PubMed:20519438,
FT ECO:0000269|PubMed:26972003"
FT MUTAGEN 311
FT /note="S->A: Phosphodeficient mutant which exhibits an open
FT conformation with a high affinity for microtubules and
FT DCTN1; when associated with A-309; A-313; A-319 and A-320."
FT /evidence="ECO:0000269|PubMed:20519438,
FT ECO:0000269|PubMed:26972003"
FT MUTAGEN 311
FT /note="S->E: Phosphomimetic mutant which exhibits a closed
FT autoinhibited conformation with a low affinity for
FT microtubules and DCTN1; when associated with E-309; E-313;
FT E-319 and E-320."
FT /evidence="ECO:0000269|PubMed:20519438,
FT ECO:0000269|PubMed:26972003"
FT MUTAGEN 313
FT /note="S->A: Phosphodeficient mutant which exhibits an open
FT conformation with a high affinity for microtubules and
FT DCTN1; when associated with A-309; A-311; A-319 and A-320."
FT /evidence="ECO:0000269|PubMed:20519438,
FT ECO:0000269|PubMed:26972003"
FT MUTAGEN 313
FT /note="S->E: Phosphomimetic mutant which exhibits a closed
FT autoinhibited conformation with a low affinity for
FT microtubules and DCTN1; when associated with E-309; E-311;
FT E-319 and E-320."
FT /evidence="ECO:0000269|PubMed:20519438,
FT ECO:0000269|PubMed:26972003"
FT MUTAGEN 319
FT /note="S->A: Phosphodeficient mutant which exhibits an open
FT conformation with a high affinity for microtubules and
FT DCTN1; when associated with A-309; A-311; A-313 and A-320."
FT /evidence="ECO:0000269|PubMed:20519438,
FT ECO:0000269|PubMed:26972003"
FT MUTAGEN 319
FT /note="S->E: Phosphomimetic mutant which exhibits a closed
FT autoinhibited conformation with a low affinity for
FT microtubules and DCTN1; when associated with E-30; E-311;
FT E-313 and E-320."
FT /evidence="ECO:0000269|PubMed:20519438,
FT ECO:0000269|PubMed:26972003"
FT MUTAGEN 320
FT /note="S->A: Phosphodeficient mutant which exhibits an open
FT conformation with a high affinity for microtubules and
FT DCTN1; when associated with A-309; A-311; A-313 and A-319."
FT /evidence="ECO:0000269|PubMed:20519438,
FT ECO:0000269|PubMed:26972003"
FT MUTAGEN 320
FT /note="S->E: Phosphomimetic mutant, exhibits a closed
FT autoinhibited conformation with a low affinity for
FT microtubules and DCTN1; when associated with E-309; E-311;
FT E-313 and E-319."
FT /evidence="ECO:0000269|PubMed:20519438,
FT ECO:0000269|PubMed:26972003"
FT CONFLICT 1232
FT /note="A -> G (in Ref. 1; CAB92974)"
SQ SEQUENCE 1320 AA; 148279 MW; 81D8096405D4689D CRC64;
MSMLKPSGLK APTKILKPGS TALKTPAAAA APLEKTVPSE KASGPPSSET QEEFVDDFRV
GERVWVNGNK PGFIQFLGET QFAPGQWAGI VLDEPIGKND GSVAGVRYFQ CEPLKGIFTR
PSKLTRKVQA EDEANGLQTA HARAASPLST AAATMVSSSP ATPSNIPQKP SQPVAKETSA
TPQISNLTKT ASESISNLSE AGSVKKGERE LKIGDRVLVG GTKAGVVRFL GETDFAKGEW
CGVELDEPLG KNDGAVAGTR YFQCQPKYGL FAPVHKVTKI GFPSTTPAKA KAAAVRRVMA
TTPASLKRSP SASSLSSMSS VASSVSSKPS RTGLLTETSS RYARKISGTT ALQEALKEKQ
QHIEQLLAER DLERAEVAKA TSHVGEIEQE LALARDGHDQ HVLELEAKMD QLRTMVEAAD
REKVELLNQL EEEKRKVEDL QFRVEEESIT KGDLETQTKL EHARIKELEQ SLLFEKTKAD
KLQRELEDTR VATVSEKSRI MELEKDLALR VQEVAELRRR LESSKPPGDV DMSLSLLQEI
SALQEKLEVT HTDHQNEVTS LKDHFGTREE MFQKEIKALH AATEKLSKEN ESLRSKLDHA
NKENSDVIAL WKSKLETAIA SHQQAMEELK VSFSKGIGTD SAEFAELKTQ IERLRLDYQH
EIESLQSKQD SERSAHAKEM ESMKAKLMKI IKEKEDSLEA VKARLDTAED QHLVEMEEML
SKLQEAEIKK EKFASASEEA VSTQTSMQDT VNKLHQKEEQ FNMLSSELEK LRENLTDMEA
KFKEKDERED QLVKAKEKLE NDIAEIMKMS GDNSSQLTKM NDELRLKERS VEELQLKLTK
ANENASLLQK SIGEVTLKAE QSQQEAAKKH EEEKKELENK LLELEKKMET SHYQCQDLKA
KYEKASSETK IKHEEILQNF QKMLVDTEDK LKAAQEANRD LMQDMEELKS QADKAKAAQT
AEDAMQIMEQ MTKEKTETLA SLEDTKQTNA KLQSELDTLK ENNLKTVEEL NKSKELLNEE
NQKMEEFKKE IETLKQAAAQ KSQQLSALQE ENVKLAEELG RTRDEVTSHQ KLEEERSVLN
NQLLEMKKSL PSNTLRESEY RKDADEEKAS LQKSISLTSA LLTEKDAELE KLRNEVTVLR
GENASAKSLH SVVQTLESDK VKLELKVKNL ELQLKENKRQ LSSSSGNTDV QTEEDERAQE
SQQMIDFLNS VIVDLQRKNQ DLKMKVEMMS EAALNGNGED PNSYDSDDQE KQSKKKPRLF
CDICDCFDLH DTEDCPTQAQ MSEDPPHSTH HGSRSEERPY CEICEMFGHW ATNCNDDETF
