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CLIP-associating protein 2 (Cytoplasmic linker-associated protein 2) (Protein Orbit homolog 2) (hOrbit2)

 CLAP2_HUMAN             Reviewed;        1294 AA.
O75122; B2RTR1; F5H604; Q7L8F6; Q8N6R6; Q9BQT3; Q9BQT4; Q9H7A3;
Q9NSZ2;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
11-OCT-2005, sequence version 2.
30-AUG-2017, entry version 151.
RecName: Full=CLIP-associating protein 2;
AltName: Full=Cytoplasmic linker-associated protein 2;
AltName: Full=Protein Orbit homolog 2;
Short=hOrbit2;
Name=CLASP2; Synonyms=KIAA0627;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9734811; DOI=10.1093/dnares/5.3.169;
Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. X.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 5:169-176(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-9 (ISOFORM 1), NUCLEOTIDE SEQUENCE
[MRNA] OF 1-15 (ISOFORM 2), FUNCTION, ALTERNATIVE SPLICING,
SUBCELLULAR LOCATION, AND INTERACTION WITH CLIP2; MICROTUBULES AND
RSN.
TISSUE=Brain;
PubMed=11290329; DOI=10.1016/S0092-8674(01)00288-4;
Akhmanova A., Hoogenraad C.C., Drabek K., Stepanova T., Dortland B.,
Verkerk T., Vermeulen W., Burgering B.M., de Zeeuw C.I., Grosveld F.,
Galjart N.;
"Clasps are CLIP-115 and -170 associating proteins involved in the
regional regulation of microtubule dynamics in motile fibroblasts.";
Cell 104:923-935(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 939-1294 (ISOFORM 1).
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1128-1294 (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
SUBCELLULAR LOCATION.
PubMed=15207236; DOI=10.1016/j.neuron.2004.05.020;
Lee H., Engel U., Rusch J., Scherrer S., Sheard K., Van Vactor D.;
"The microtubule plus end tracking protein Orbit/MAST/CLASP acts
downstream of the tyrosine kinase Abl in mediating axon guidance.";
Neuron 42:913-926(2004).
[8]
FUNCTION, INTERACTION WITH MAPRE1; MAPRE3; MICROTUBULES AND RSN, AND
SUBCELLULAR LOCATION.
PubMed=15631994; DOI=10.1083/jcb.200405094;
Mimori-Kiyosue Y., Grigoriev I., Lansbergen G., Sasaki H., Matsui C.,
Severin F., Galjart N., Grosveld F., Vorobjev I., Tsukita S.,
Akhmanova A.;
"CLASP1 and CLASP2 bind to EB1 and regulate microtubule plus-end
dynamics at the cell cortex.";
J. Cell Biol. 168:141-153(2005).
[9]
INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION, AND
PHOSPHORYLATION BY GSK3B.
PubMed=15955847; DOI=10.1083/jcb.200412114;
Wittmann T., Waterman-Storer C.M.;
"Spatial regulation of CLASP affinity for microtubules by Rac1 and
GSK3beta in migrating epithelial cells.";
J. Cell Biol. 169:929-939(2005).
[10]
ERRATUM.
Wittmann T., Waterman-Storer C.M.;
J. Cell Biol. 171:393-393(2005).
[11]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERC1;
PHLDB2 AND RSN, AND SUBCELLULAR LOCATION.
PubMed=16824950; DOI=10.1016/j.devcel.2006.05.012;
Lansbergen G., Grigoriev I., Mimori-Kiyosue Y., Ohtsuka T., Higa S.,
Kitajima I., Demmers J., Galjart N., Houtsmuller A.B., Grosveld F.,
Akhmanova A.;
"CLASPs attach microtubule plus ends to the cell cortex through a
complex with LL5beta.";
Dev. Cell 11:21-32(2006).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16866869; DOI=10.1111/j.1365-2443.2006.00990.x;
Mimori-Kiyosue Y., Grigoriev I., Sasaki H., Matsui C., Akhmanova A.,
Tsukita S., Vorobjev I.;
"Mammalian CLASPs are required for mitotic spindle organization and
kinetochore alignment.";
Genes Cells 11:845-857(2006).
[13]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16914514; DOI=10.1091/mbc.E06-07-0579;
Pereira A.L., Pereira A.J., Maia A.R.R., Drabek K., Sayas C.L.,
Hergert P.J., Lince-Faria M., Matos I., Duque C., Stepanova T.,
Rieder C.L., Earnshaw W.C., Galjart N., Maiato H.;
"Mammalian CLASP1 and CLASP2 cooperate to ensure mitotic fidelity by
regulating spindle and kinetochore function.";
Mol. Biol. Cell 17:4526-4542(2006).
[14]
FUNCTION, INTERACTION WITH GCC2, AND SUBCELLULAR LOCATION.
PubMed=17543864; DOI=10.1016/j.devcel.2007.04.002;
Efimov A., Kharitonov A., Efimova N., Loncarek J., Miller P.M.,
Andreyeva N., Gleeson P., Galjart N., Maia A.R., McLeod I.X.,
Yates J.R. III, Maiato H., Khodjakov A., Akhmanova A., Kaverina I.;
"Asymmetric CLASP-dependent nucleation of noncentrosomal microtubules
at the trans-Golgi network.";
Dev. Cell 12:917-930(2007).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-525; SER-529;
SER-596 AND SER-1029, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[19]
INTERACTION WITH MAPRE1, SUBCELLULAR LOCATION, DOMAIN MICROTUBULE TIP
LOCALIZATION SIGNAL, AND MUTAGENESIS OF 496-ILE-PRO-497 AND
519-ILE-PRO-520.
PubMed=19632184; DOI=10.1016/j.cell.2009.04.065;
Honnappa S., Gouveia S.M., Weisbrich A., Damberger F.F., Bhavesh N.S.,
Jawhari H., Grigoriev I., van Rijssel F.J., Buey R.M., Lawera A.,
Jelesarov I., Winkler F.K., Wuthrich K., Akhmanova A., Steinmetz M.O.;
"An EB1-binding motif acts as a microtubule tip localization signal.";
Cell 138:366-376(2009).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-596 AND
SER-1029, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[21]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20937854; DOI=10.1073/pnas.1000975107;
Zaoui K., Benseddik K., Daou P., Salaun D., Badache A.;
"ErbB2 receptor controls microtubule capture by recruiting ACF7 to the
plasma membrane of migrating cells.";
Proc. Natl. Acad. Sci. U.S.A. 107:18517-18522(2010).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-370; SER-455 AND
SER-596, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327; SER-330; SER-360;
SER-370; SER-459; SER-463; SER-478; SER-489; SER-507; SER-525;
SER-529; SER-585; SER-587; SER-596; SER-621; THR-787; SER-892;
SER-952; SER-955; SER-1013 AND SER-1029, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[27]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 60-310, FUNCTION, SUBUNIT,
INTERACTION WITH MAPRE1, DOMAIN, AND MUTAGENESIS OF TRP-106; LYS-191;
496-ILE-PRO-497; SER-499; SER-507; 519-ILE-PRO-520; SER-525; SER-529;
SER-533; SER-537; SER-541; TRP-667; LYS-833; ARG-838 AND LYS-839.
PubMed=26003921; DOI=10.1016/j.jmb.2015.05.012;
Maki T., Grimaldi A.D., Fuchigami S., Kaverina I., Hayashi I.;
"CLASP2 has two distinct TOG domains that contribute differently to
microtubule dynamics.";
J. Mol. Biol. 427:2379-2395(2015).
-!- FUNCTION: Microtubule plus-end tracking protein that promotes the
stabilization of dynamic microtubules (PubMed:26003921). Involved
in the nucleation of noncentrosomal microtubules originating from
the trans-Golgi network (TGN). Required for the polarization of
the cytoplasmic microtubule arrays in migrating cells towards the
leading edge of the cell. May act at the cell cortex to enhance
the frequency of rescue of depolymerizing microtubules by
attaching their plus-ends to cortical platforms composed of ERC1
and PHLDB2 (PubMed:16824950). This cortical microtubule
stabilizing activity is regulated at least in part by
phosphatidylinositol 3-kinase signaling. Also performs a similar
stabilizing function at the kinetochore which is essential for the
bipolar alignment of chromosomes on the mitotic spindle
(PubMed:16866869, PubMed:16914514). Acts as a mediator of ERBB2-
dependent stabilization of microtubules at the cell cortex.
{ECO:0000269|PubMed:11290329, ECO:0000269|PubMed:15631994,
ECO:0000269|PubMed:16824950, ECO:0000269|PubMed:16866869,
ECO:0000269|PubMed:16914514, ECO:0000269|PubMed:17543864,
ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:26003921}.
-!- SUBUNIT: Interacts with microtubules (PubMed:11290329,
PubMed:15631994, PubMed:15955847, PubMed:26003921). Interacts with
MAPRE1; probably required for targeting to the growing microtubule
plus ends (PubMed:15631994, PubMed:19632184, PubMed:26003921).
Interacts with CLIP2, ERC1, MAPRE3, PHLDB2 and RSN
(PubMed:11290329, PubMed:15631994). The interaction with ERC1 may
be mediated by PHLDB2 (PubMed:16824950). Interacts with GCC2;
recruits CLASP2 to Golgi membranes (PubMed:17543864). Interacts
with MACF1 (By similarity). {ECO:0000250|UniProtKB:Q8BRT1,
ECO:0000269|PubMed:11290329, ECO:0000269|PubMed:15631994,
ECO:0000269|PubMed:15955847, ECO:0000269|PubMed:16824950,
ECO:0000269|PubMed:17543864, ECO:0000269|PubMed:19632184}.
-!- INTERACTION:
O55156:Clip2 (xeno); NbExp=3; IntAct=EBI-913524, EBI-349416;
Q15691:MAPRE1; NbExp=3; IntAct=EBI-913524, EBI-1004115;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:15631994, ECO:0000269|PubMed:20937854}.
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
{ECO:0000269|PubMed:16914514}. Chromosome, centromere, kinetochore
{ECO:0000269|PubMed:16866869, ECO:0000269|PubMed:16914514}.
Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16866869,
ECO:0000269|PubMed:16914514}. Golgi apparatus
{ECO:0000250|UniProtKB:Q8BRT1}. Golgi apparatus, trans-Golgi
network {ECO:0000269|PubMed:17543864}. Cell membrane
{ECO:0000269|PubMed:20937854}. Cell projection, ruffle membrane
{ECO:0000269|PubMed:20937854}. Note=Localizes to microtubule plus
ends (PubMed:15631994). Localizes to centrosomes, kinetochores and
the mitotic spindle from prometaphase. Subsequently localizes to
the spindle midzone from anaphase and to the midbody from
telophase (PubMed:16866869, PubMed:16914514). In migrating cells
localizes to the plus ends of microtubules within the cell body
and to the entire microtubule lattice within the lamella.
Localizes to the cell cortex and this requires ERC1 and PHLDB2
(PubMed:16824950). The MEMO1-RHOA-DIAPH1 signaling pathway
controls localization of the phosphorylated form to the cell
membrane. {ECO:0000269|PubMed:15631994,
ECO:0000269|PubMed:16824950, ECO:0000269|PubMed:16866869,
ECO:0000269|PubMed:16914514, ECO:0000269|PubMed:20937854}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional isoforms exist.;
Name=1; Synonyms=CLASP2 gamma;
IsoId=O75122-1; Sequence=Displayed;
Name=2; Synonyms=CLASP2 beta;
IsoId=O75122-2; Sequence=VSP_015805, VSP_015806, VSP_015807;
Name=3;
IsoId=O75122-3; Sequence=VSP_057273, VSP_057274, VSP_057275,
VSP_057276;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Brain-specific.
-!- DOMAIN: The two SXIP sequence motifs mediate interaction with
MAPRE1; this is necessary for targeting to growing microtubule
plus ends. {ECO:0000269|PubMed:19632184}.
-!- DOMAIN: Two TOG regions display structural characteristics similar
to HEAT repeat domains and mediate interaction with microtubules.
{ECO:0000269|PubMed:26003921}.
-!- PTM: Phosphorylated by GSK3B. Phosphorylation reduces MAPRE1
binding (PubMed:26003921). Phosphorylation by GSK3B may negatively
regulate binding to microtubule lattices in lamella.
{ECO:0000269|PubMed:15955847, ECO:0000305|PubMed:26003921}.
-!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA31602.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=BAB14995.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AB014527; BAA31602.2; ALT_INIT; mRNA.
EMBL; AC093114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC113170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC132515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC029035; AAH29035.1; -; mRNA.
EMBL; BC140778; AAI40779.1; -; mRNA.
EMBL; AJ288058; CAC35157.1; -; mRNA.
EMBL; AJ288059; CAC35158.1; -; mRNA.
EMBL; AL137636; CAB70852.1; -; mRNA.
EMBL; AK024770; BAB14995.1; ALT_INIT; mRNA.
PIR; T00386; T00386.
RefSeq; NP_001193973.1; NM_001207044.1.
RefSeq; NP_055912.2; NM_015097.2.
UniGene; Hs.108614; -.
PDB; 3WOY; X-ray; 2.10 A; A=60-310.
PDBsum; 3WOY; -.
ProteinModelPortal; O75122; -.
SMR; O75122; -.
BioGrid; 116743; 46.
DIP; DIP-36804N; -.
IntAct; O75122; 27.
MINT; MINT-4526878; -.
STRING; 9606.ENSP00000419974; -.
iPTMnet; O75122; -.
PhosphoSitePlus; O75122; -.
BioMuta; CLASP2; -.
EPD; O75122; -.
MaxQB; O75122; -.
PaxDb; O75122; -.
PeptideAtlas; O75122; -.
PRIDE; O75122; -.
DNASU; 23122; -.
Ensembl; ENST00000313350; ENSP00000324364; ENSG00000163539.
Ensembl; ENST00000359576; ENSP00000352581; ENSG00000163539.
GeneID; 23122; -.
KEGG; hsa:23122; -.
UCSC; uc003cfv.4; human. [O75122-1]
CTD; 23122; -.
DisGeNET; 23122; -.
GeneCards; CLASP2; -.
HGNC; HGNC:17078; CLASP2.
HPA; HPA067071; -.
MIM; 605853; gene.
neXtProt; NX_O75122; -.
PharmGKB; PA38435; -.
eggNOG; KOG2956; Eukaryota.
eggNOG; ENOG410ZMY0; LUCA.
HOGENOM; HOG000236347; -.
HOVERGEN; HBG079692; -.
InParanoid; O75122; -.
KO; K16578; -.
OrthoDB; EOG091G0GTV; -.
PhylomeDB; O75122; -.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-428890; Role of Abl in Robo-Slit signaling.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-68877; Mitotic Prometaphase.
ChiTaRS; CLASP2; human.
GeneWiki; CLASP2; -.
GenomeRNAi; 23122; -.
PRO; PR:O75122; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000163539; -.
CleanEx; HS_CLASP2; -.
ExpressionAtlas; O75122; baseline and differential.
Genevisible; O75122; HS.
GO; GO:0044295; C:axonal growth cone; IDA:UniProtKB.
GO; GO:0045180; C:basal cortex; IDA:UniProtKB.
GO; GO:0005938; C:cell cortex; IDA:MGI.
GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:1903754; C:cortical microtubule plus-end; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005828; C:kinetochore microtubule; TAS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005874; C:microtubule; IDA:UniProtKB.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
GO; GO:0002162; F:dystroglycan binding; IPI:UniProtKB.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
GO; GO:1990782; F:protein tyrosine kinase binding; IPI:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0090002; P:establishment of protein localization to plasma membrane; IMP:UniProtKB.
GO; GO:0007163; P:establishment or maintenance of cell polarity; TAS:UniProtKB.
GO; GO:0010458; P:exit from mitosis; IMP:UniProtKB.
GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
GO; GO:0034453; P:microtubule anchoring; IMP:UniProtKB.
GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
GO; GO:0007020; P:microtubule nucleation; IMP:UniProtKB.
GO; GO:0031023; P:microtubule organizing center organization; IMP:UniProtKB.
GO; GO:0007052; P:mitotic spindle organization; IMP:UniProtKB.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; IMP:UniProtKB.
GO; GO:0007026; P:negative regulation of microtubule depolymerization; NAS:UniProtKB.
GO; GO:0051497; P:negative regulation of stress fiber assembly; IMP:UniProtKB.
GO; GO:1903690; P:negative regulation of wound healing, spreading of epidermal cells; IMP:UniProtKB.
GO; GO:0035791; P:platelet-derived growth factor receptor-beta signaling pathway; IDA:UniProtKB.
GO; GO:1904261; P:positive regulation of basement membrane assembly involved in embryonic body morphogenesis; IMP:UniProtKB.
GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:UniProtKB.
GO; GO:0045921; P:positive regulation of exocytosis; IMP:UniProtKB.
GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; IMP:UniProtKB.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; IDA:UniProtKB.
GO; GO:0030516; P:regulation of axon extension; IDA:UniProtKB.
GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
GO; GO:0010470; P:regulation of gastrulation; IMP:UniProtKB.
GO; GO:0031113; P:regulation of microtubule polymerization; IDA:UniProtKB.
GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IMP:UniProtKB.
GO; GO:0032886; P:regulation of microtubule-based process; IMP:UniProtKB.
GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome.
GO; GO:0006903; P:vesicle targeting; IMP:UniProtKB.
Gene3D; 1.25.10.10; -; 2.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR024395; CLASP_N_dom.
InterPro; IPR034085; TOG.
Pfam; PF12348; CLASP_N; 1.
SMART; SM01349; TOG; 3.
SUPFAM; SSF48371; SSF48371; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Cell division;
Cell membrane; Cell projection; Centromere; Chromosome;
Complete proteome; Cytoplasm; Cytoskeleton; Golgi apparatus;
Kinetochore; Membrane; Microtubule; Mitosis; Phosphoprotein;
Reference proteome; Repeat.
CHAIN 1 1294 CLIP-associating protein 2.
/FTId=PRO_0000089849.
REPEAT 173 208 HEAT 1. {ECO:0000255}.
REPEAT 209 245 HEAT 2. {ECO:0000255}.
REPEAT 250 287 HEAT 3. {ECO:0000255}.
REPEAT 710 747 HEAT 4. {ECO:0000255}.
REPEAT 772 809 HEAT 5. {ECO:0000255}.
REPEAT 1054 1091 HEAT 6. {ECO:0000255}.
REPEAT 1098 1135 HEAT 7. {ECO:0000255}.
REPEAT 1216 1253 HEAT 8. {ECO:0000255}.
REGION 60 311 TOG 1. {ECO:0000269|PubMed:26003921}.
REGION 444 580 Interaction with microtubules, MAPRE1 and
MAPRE3. {ECO:0000269|PubMed:15631994}.
REGION 649 881 TOG 2. {ECO:0000269|PubMed:26003921}.
REGION 872 1294 Interaction with RSN and localization to
the Golgi and kinetochores.
REGION 1017 1294 Required for cortical localization.
MOTIF 494 497 SXIP motif 1; mediates interaction with
MAPRE1 and targeting to microtubule plus
ends. {ECO:0000269|PubMed:19632184,
ECO:0000269|PubMed:26003921}.
MOTIF 517 520 SXIP motif 2; mediates interaction with
MAPRE1 and targeting to microtubule plus
ends. {ECO:0000269|PubMed:19632184,
ECO:0000269|PubMed:26003921}.
COMPBIAS 310 587 Ser-rich.
COMPBIAS 1104 1108 Poly-Leu.
MOD_RES 8 8 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 14 14 Phosphoserine.
{ECO:0000250|UniProtKB:Q99JD4}.
MOD_RES 316 316 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 327 327 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 330 330 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 360 360 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 368 368 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BRT1}.
MOD_RES 370 370 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 407 407 Phosphoserine.
{ECO:0000250|UniProtKB:Q99JD4}.
MOD_RES 455 455 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 459 459 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 463 463 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 478 478 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 489 489 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 507 507 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 525 525 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 529 529 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 585 585 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 587 587 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 596 596 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 621 621 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 627 627 Phosphoserine.
{ECO:0000250|UniProtKB:Q8BRT1}.
MOD_RES 787 787 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 892 892 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 952 952 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 955 955 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1013 1013 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1029 1029 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 6 MAMGDD -> MRRLICKRICDY (in isoform 2).
{ECO:0000303|PubMed:11290329,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_015805.
VAR_SEQ 1 5 MAMGD -> MEPRSMEYFCAQVQQKDVGGRLQVGQELLLYL
GAPGAISDLEEDLGRLGKTVDALTGWVGSSNYRVSLMGLEI
LSAFVDRLSTRFKSYVAMVIVALIDRMGDAKDKVRDEAQTL
ILKLMDQVAPPMYIWEQLASGFKHKNFRSREGVCLCLIETL
NIFGAQPLVISKLIPHLCILFGDSNSQVRDAAILAIVEIYR
HVGEKVRMDLYKRGIPPARLEMIFAKFDEVQSSGGMILSVC
K (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_057273.
VAR_SEQ 54 54 G -> GA (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_057274.
VAR_SEQ 410 425 DTSDKLDGTASEDGRV -> CEAFWRSGRTAKLYSV (in
isoform 2). {ECO:0000303|PubMed:11290329,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_015806.
VAR_SEQ 426 1294 Missing (in isoform 2).
{ECO:0000303|PubMed:11290329,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_015807.
VAR_SEQ 550 570 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_057275.
VAR_SEQ 606 606 L -> LLLGDIRTK (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_057276.
MUTAGEN 106 106 W->E: Decreases affinity for
microtubules; when associated with A-191;
E-667; E-833; A-838 and A-839.
{ECO:0000269|PubMed:26003921}.
MUTAGEN 191 191 K->A: Decreases affinity for
microtubules; when associated with E-106;
E-667; E-833; A-838 and A-839.
{ECO:0000269|PubMed:26003921}.
MUTAGEN 496 497 IP->AA: No effect on MAPRE1 binding.
Abolishes interaction with MAPRE1; when
associated with 519-A-A-520.
{ECO:0000269|PubMed:26003921}.
MUTAGEN 496 497 IP->SS: Reduced targeting to the growing
microtubule plus ends. Loss of
interaction with MAPRE1 and targeting to
the growing microtubule plus ends; when
associated with 519-S-S-520.
{ECO:0000269|PubMed:19632184}.
MUTAGEN 499 499 S->D: Phosphomimetic mutant that reduces
MAPRE1 binding; when associated with D-
503; D-507; D-525; D-529; D-533; D-537
and D-541. {ECO:0000269|PubMed:26003921}.
MUTAGEN 503 503 S->D: Phosphomimetic mutant that reduces
MAPRE1 binding; when associated with D-
499; D-507; D-525; D-529; D-533; D-537
and D-541. {ECO:0000269|PubMed:26003921}.
MUTAGEN 507 507 S->D: Phosphomimetic mutant that reduces
MAPRE1 binding; when associated with D-
499; D-503; D-525; D-529; D-533; D-537
and D-541. {ECO:0000269|PubMed:26003921}.
MUTAGEN 519 520 IP->AA: No effect on MAPRE1 binding.
Abolishes interaction with MAPRE1; when
associated with 496-A-A-497.
{ECO:0000269|PubMed:26003921}.
MUTAGEN 519 520 IP->SS: Reduced targeting to the growing
microtubule plus ends. Loss of
interaction with MAPRE1 and targeting to
the growing microtubule plus ends; when
associated with 496-S-S-497.
{ECO:0000269|PubMed:19632184}.
MUTAGEN 525 525 S->D: Phosphomimetic mutant that reduces
MAPRE1 binding; when associated with D-
499; D-503; D-507; D-529; D-533; D-537
and D-541. {ECO:0000269|PubMed:26003921}.
MUTAGEN 529 529 S->D: Phosphomimetic mutant that reduces
MAPRE1 binding; when associated with D-
499; D-503; D-507; D-525; D-533; D-537
and D-541. {ECO:0000269|PubMed:26003921}.
MUTAGEN 533 533 S->D: Phosphomimetic mutant that reduces
MAPRE1 binding; when associated with D-
499; D-503; D-507; D-525; D-529; D-537
and D-541. {ECO:0000269|PubMed:26003921}.
MUTAGEN 537 537 S->D: Phosphomimetic mutant that reduces
MAPRE1 binding; when associated with D-
499; D-503; D-507; D-525; D-529; D-533
and D-541. {ECO:0000269|PubMed:26003921}.
MUTAGEN 541 541 S->D: Phosphomimetic mutant that reduces
MAPRE1 binding; when associated with D-
499; D-503; D-507; D-525; D-529; D-533
and D-537. {ECO:0000269|PubMed:26003921}.
MUTAGEN 667 667 W->E: Decreases affinity for
microtubules; when associated with E-106;
A-191; E-833; A-838 and A-839.
{ECO:0000269|PubMed:26003921}.
MUTAGEN 833 833 K->E: Decreases affinity for
microtubules; when associated with E-106;
A-191; E-667; A-838 and A-839.
{ECO:0000269|PubMed:26003921}.
MUTAGEN 838 838 R->A: Decreases affinity for
microtubules; when associated with E-106;
A-191; E-667; E-833 and A-839.
{ECO:0000269|PubMed:26003921}.
MUTAGEN 839 839 K->A: Decreases affinity for
microtubules; when associated with E-106;
A-191; E-667; E-833 and A-838.
{ECO:0000269|PubMed:26003921}.
CONFLICT 392 392 R -> S (in Ref. 1; BAA31602 and 3;
AAH29035/AAI40779). {ECO:0000305}.
HELIX 64 75 {ECO:0000244|PDB:3WOY}.
HELIX 85 100 {ECO:0000244|PDB:3WOY}.
HELIX 106 121 {ECO:0000244|PDB:3WOY}.
HELIX 124 126 {ECO:0000244|PDB:3WOY}.
HELIX 128 136 {ECO:0000244|PDB:3WOY}.
HELIX 138 144 {ECO:0000244|PDB:3WOY}.
HELIX 150 167 {ECO:0000244|PDB:3WOY}.
HELIX 168 171 {ECO:0000244|PDB:3WOY}.
HELIX 172 185 {ECO:0000244|PDB:3WOY}.
HELIX 191 207 {ECO:0000244|PDB:3WOY}.
HELIX 213 220 {ECO:0000244|PDB:3WOY}.
HELIX 226 242 {ECO:0000244|PDB:3WOY}.
HELIX 245 248 {ECO:0000244|PDB:3WOY}.
HELIX 249 251 {ECO:0000244|PDB:3WOY}.
HELIX 252 263 {ECO:0000244|PDB:3WOY}.
HELIX 268 284 {ECO:0000244|PDB:3WOY}.
HELIX 286 294 {ECO:0000244|PDB:3WOY}.
HELIX 298 303 {ECO:0000244|PDB:3WOY}.
SEQUENCE 1294 AA; 141133 MW; E4FF7E06049E65E5 CRC64;
MAMGDDKSFD DEESVDGNRP SSAASAFKVP APKTSGNPAN SARKPGSAGG PKVGGASKEG
GAGAVDEDDF IKAFTDVPSI QIYSSRELEE TLNKIREILS DDKHDWDQRA NALKKIRSLL
VAGAAQYDCF FQHLRLLDGA LKLSAKDLRS QVVREACITV AHLSTVLGNK FDHGAEAIVP
TLFNLVPNSA KVMATSGCAA IRFIIRHTHV PRLIPLITSN CTSKSVPVRR RSFEFLDLLL
QEWQTHSLER HAAVLVETIK KGIHDADAEA RVEARKTYMG LRNHFPGEAE TLYNSLEPSY
QKSLQTYLKS SGSVASLPQS DRSSSSSQES LNRPFSSKWS TANPSTVAGR VSAGSSKASS
LPGSLQRSRS DIDVNAAAGA KAHHAAGQSV RRGRLGAGAL NAGSYASLED TSDKLDGTAS
EDGRVRAKLS APLAGMGNAK ADSRGRSRTK MVSQSQPGSR SGSPGRVLTT TALSTVSSGV
QRVLVNSASA QKRSKIPRSQ GCSREASPSR LSVARSSRIP RPSVSQGCSR EASRESSRDT
SPVRSFQPLA SRHHSRSTGA LYAPEVYGAS GPGYGISQSS RLSSSVSAMR VLNTGSDVEE
AVADALKKPA RRRYESYGMH SDDDANSDAS SACSERSYSS RNGSIPTYMR QTEDVAEVLN
RCASSNWSER KEGLLGLQNL LKNQRTLSRV ELKRLCEIFT RMFADPHGKR VFSMFLETLV
DFIQVHKDDL QDWLFVLLTQ LLKKMGADLL GSVQAKVQKA LDVTRESFPN DLQFNILMRF
TVDQTQTPSL KVKVAILKYI ETLAKQMDPG DFINSSETRL AVSRVITWTT EPKSSDVRKA
AQSVLISLFE LNTPEFTMLL GALPKTFQDG ATKLLHNHLR NTGNGTQSSM GSPLTRPTPR
SPANWSSPLT SPTNTSQNTL SPSAFDYDTE NMNSEDIYSS LRGVTEAIQN FSFRSQEDMN
EPLKRDSKKD DGDSMCGGPG MSDPRAGGDA TDSSQTALDN KASLLHSMPT HSSPRSRDYN
PYNYSDSISP FNKSALKEAM FDDDADQFPD DLSLDHSDLV AELLKELSNH NERVEERKIA
LYELMKLTQE ESFSVWDEHF KTILLLLLET LGDKEPTIRA LALKVLREIL RHQPARFKNY
AELTVMKTLE AHKDPHKEVV RSAEEAASVL ATSISPEQCI KVLCPIIQTA DYPINLAAIK
MQTKVIERVS KETLNLLLPE IMPGLIQGYD NSESSVRKAC VFCLVAVHAV IGDELKPHLS
QLTGSKMKLL NLYIKRAQTG SGGADPTTDV SGQS


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