ID   CLAP1_HUMAN             Reviewed;        1538 AA.
AC   Q7Z460; A2RU21; B7ZLX3; F5GWS0; O75118; Q2KHQ9; Q5H9P0; Q8N5B8; Q9BQT5;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 192.
DE   RecName: Full=CLIP-associating protein 1;
DE   AltName: Full=Cytoplasmic linker-associated protein 1;
DE   AltName: Full=Multiple asters homolog 1;
DE   AltName: Full=Protein Orbit homolog 1;
DE            Short=hOrbit1;
GN   Name=CLASP1; Synonyms=KIAA0622, MAST1;
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   Maiato H., Sunkel C.E., Earnshaw W.C.;
RT   "Full length cDNA of a human homologue of Drosophila melanogaster multiple
RT   asters (MAST) gene.";
RL   Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5), AND
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1332-1538 (ISOFORMS 1/2).
RC   TISSUE=Eye;
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 1-266, FUNCTION, SUBCELLULAR LOCATION,
RP   ALTERNATIVE SPLICING, AND INTERACTION WITH CLIP2; MICROTUBULES AND RSN.
RC   TISSUE=Brain;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 221-1538 (ISOFORM 3).
RC   TISSUE=Testis;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 250-1538.
RC   TISSUE=Brain;
RX   PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA   Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA   Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. X. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 5:169-176(1998).
RN   [7]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12837247; DOI=10.1016/s0092-8674(03)00465-3;
RA   Maiato H., Fairley E.A., Rieder C.L., Swedlow J.R., Sunkel C.E.,
RA   Earnshaw W.C.;
RT   "Human CLASP1 is an outer kinetochore component that regulates spindle
RT   microtubule dynamics.";
RL   Cell 113:891-904(2003).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT   "Proteomic characterization of the human centrosome by protein correlation
RT   profiling.";
RL   Nature 426:570-574(2003).
RN   [9]
RP   INTERACTION WITH MICROTUBULES, AND SUBCELLULAR LOCATION.
RX   PubMed=16145243; DOI=10.1247/csf.30.7;
RA   Aonuma M., Miyamoto M., Inoue Y.H., Tamai K., Sakai H., Kamasawa N.,
RA   Matsukage A.;
RT   "Microtubule bundle formation and cell death induced by the human
RT   CLASP/Orbit N-terminal fragment.";
RL   Cell Struct. Funct. 30:7-13(2005).
RN   [10]
RP   FUNCTION, INTERACTION WITH MAPRE1; MAPRE3; MICROTUBULES AND RSN, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=15631994; DOI=10.1083/jcb.200405094;
RA   Mimori-Kiyosue Y., Grigoriev I., Lansbergen G., Sasaki H., Matsui C.,
RA   Severin F., Galjart N., Grosveld F., Vorobjev I., Tsukita S., Akhmanova A.;
RT   "CLASP1 and CLASP2 bind to EB1 and regulate microtubule plus-end dynamics
RT   at the cell cortex.";
RL   J. Cell Biol. 168:141-153(2005).
RN   [11]
RP   INTERACTION WITH ERC1 AND PHLDB2, AND SUBCELLULAR LOCATION.
RX   PubMed=16824950; DOI=10.1016/j.devcel.2006.05.012;
RA   Lansbergen G., Grigoriev I., Mimori-Kiyosue Y., Ohtsuka T., Higa S.,
RA   Kitajima I., Demmers J., Galjart N., Houtsmuller A.B., Grosveld F.,
RA   Akhmanova A.;
RT   "CLASPs attach microtubule plus ends to the cell cortex through a complex
RT   with LL5beta.";
RL   Dev. Cell 11:21-32(2006).
RN   [12]
RP   FUNCTION.
RX   PubMed=16866869; DOI=10.1111/j.1365-2443.2006.00990.x;
RA   Mimori-Kiyosue Y., Grigoriev I., Sasaki H., Matsui C., Akhmanova A.,
RA   Tsukita S., Vorobjev I.;
RT   "Mammalian CLASPs are required for mitotic spindle organization and
RT   kinetochore alignment.";
RL   Genes Cells 11:845-857(2006).
RN   [13]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16914514; DOI=10.1091/mbc.e06-07-0579;
RA   Pereira A.L., Pereira A.J., Maia A.R.R., Drabek K., Sayas C.L.,
RA   Hergert P.J., Lince-Faria M., Matos I., Duque C., Stepanova T.,
RA   Rieder C.L., Earnshaw W.C., Galjart N., Maiato H.;
RT   "Mammalian CLASP1 and CLASP2 cooperate to ensure mitotic fidelity by
RT   regulating spindle and kinetochore function.";
RL   Mol. Biol. Cell 17:4526-4542(2006).
RN   [14]
RP   FUNCTION, INTERACTION WITH GCC2, AND SUBCELLULAR LOCATION.
RX   PubMed=17543864; DOI=10.1016/j.devcel.2007.04.002;
RA   Efimov A., Kharitonov A., Efimova N., Loncarek J., Miller P.M.,
RA   Andreyeva N., Gleeson P., Galjart N., Maia A.R., McLeod I.X.,
RA   Yates J.R. III, Maiato H., Khodjakov A., Akhmanova A., Kaverina I.;
RT   "Asymmetric CLASP-dependent nucleation of noncentrosomal microtubules at
RT   the trans-Golgi network.";
RL   Dev. Cell 12:917-930(2007).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1196, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-646; SER-649;
RP   THR-656; SER-688; SER-695; THR-711; SER-714; SER-1091 AND THR-1099, AND
RP   IDENTIFICATION BY 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   [18]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-646; SER-688;
RP   SER-797 AND SER-1091, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646 AND SER-1223, AND
RP   IDENTIFICATION BY 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   [21]
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   [22]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600; SER-646 AND SER-684, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-545; SER-558;
RP   SER-559; SER-568; SER-600; SER-636; SER-646; SER-647; SER-649; SER-695;
RP   SER-705; SER-787; SER-797; SER-823; SER-1091 AND SER-1196, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and 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).
RN   [24]
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   [25]
RP   INTERACTION WITH MTCL2 AND MTCL1.
RX   PubMed=33587225; DOI=10.1007/s10577-021-09651-8;
RA   Ferreira L.T., Logarinho E., Macedo J.C., Maia A.R.R., Maiato H.;
RT   "SOGA1 and SOGA2/MTCL1 are CLASP-interacting proteins required for faithful
RT   chromosome segregation in human cells.";
RL   Chromosome Res. 29:159-173(2021).
CC   -!- FUNCTION: Microtubule plus-end tracking protein that promotes the
CC       stabilization of dynamic microtubules. Involved in the nucleation of
CC       noncentrosomal microtubules originating from the trans-Golgi network
CC       (TGN). Required for the polarization of the cytoplasmic microtubule
CC       arrays in migrating cells towards the leading edge of the cell. May act
CC       at the cell cortex to enhance the frequency of rescue of depolymerizing
CC       microtubules by attaching their plus-ends to cortical platforms
CC       composed of ERC1 and PHLDB2. This cortical microtubule stabilizing
CC       activity is regulated at least in part by phosphatidylinositol 3-kinase
CC       signaling. Also performs a similar stabilizing function at the
CC       kinetochore which is essential for the bipolar alignment of chromosomes
CC       on the mitotic spindle. {ECO:0000269|PubMed:11290329,
CC       ECO:0000269|PubMed:12837247, ECO:0000269|PubMed:15631994,
CC       ECO:0000269|PubMed:16866869, ECO:0000269|PubMed:16914514,
CC       ECO:0000269|PubMed:17543864}.
CC   -!- SUBUNIT: Interacts with CLIP2, ERC1, MAPRE1, MAPRE3, microtubules,
CC       PHLDB2 and RSN (PubMed:11290329, PubMed:16145243, PubMed:15631994,
CC       PubMed:16824950). The interaction with ERC1 may be mediated by PHLDB2
CC       (PubMed:16824950). Interacts with GCC2; recruits CLASP1 to Golgi
CC       membranes (PubMed:17543864). Interacts with MACF1 (By similarity).
CC       Interacts with mtcl2 and MTCL1 (PubMed:33587225).
CC       {ECO:0000250|UniProtKB:Q80TV8, ECO:0000269|PubMed:11290329,
CC       ECO:0000269|PubMed:15631994, ECO:0000269|PubMed:16145243,
CC       ECO:0000269|PubMed:16824950, ECO:0000269|PubMed:17543864,
CC       ECO:0000269|PubMed:33587225}.
CC   -!- INTERACTION:
CC       Q7Z460; O60333: KIF1B; NbExp=3; IntAct=EBI-913476, EBI-465633;
CC       Q7Z460; P31947: SFN; NbExp=3; IntAct=EBI-913476, EBI-476295;
CC       Q7Z460; Q96R06: SPAG5; NbExp=3; IntAct=EBI-913476, EBI-413317;
CC       Q7Z460; P62258: YWHAE; NbExp=5; IntAct=EBI-913476, EBI-356498;
CC       Q7Z460; Q9JK25: Clip1; Xeno; NbExp=2; IntAct=EBI-913476, EBI-908338;
CC       Q7Z460; O55156: Clip2; Xeno; NbExp=3; IntAct=EBI-913476, EBI-349416;
CC       Q7Z460-2; Q9NX95-5: SYBU; NbExp=3; IntAct=EBI-10967515, EBI-12816095;
CC       Q7Z460-4; Q96AA8: JAKMIP2; NbExp=3; IntAct=EBI-10257534, EBI-752007;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, centrosome
CC       {ECO:0000269|PubMed:14654843}. Chromosome, centromere, kinetochore.
CC       Cytoplasm, cytoskeleton, spindle. Golgi apparatus, trans-Golgi network
CC       {ECO:0000305}. Note=Localizes to microtubule plus ends. Localizes to
CC       centrosomes, kinetochores and the mitotic spindle from prometaphase.
CC       Subsequently localizes to the spindle midzone from anaphase and to the
CC       midbody from telophase. In migrating cells localizes to the plus ends
CC       of microtubules within the cell body and to the entire microtubule
CC       lattice within the lamella. Localizes to the cell cortex and this
CC       requires ERC1 and PHLDB2.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q7Z460-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7Z460-2; Sequence=VSP_022386, VSP_022387, VSP_022389;
CC       Name=3;
CC         IsoId=Q7Z460-3; Sequence=VSP_022386, VSP_022387, VSP_022388,
CC                                  VSP_022389;
CC       Name=4;
CC         IsoId=Q7Z460-4; Sequence=VSP_054412, VSP_054413, VSP_022386,
CC                                  VSP_054414, VSP_022389;
CC       Name=5;
CC         IsoId=Q7Z460-5; Sequence=VSP_057272, VSP_022386, VSP_022387,
CC                                  VSP_022389;
CC   -!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH32563.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAX88872.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AF347693; AAQ15051.1; -; mRNA.
DR   EMBL; AC012447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC013399; AAX88872.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC018737; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC079449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC032563; AAH32563.1; ALT_INIT; mRNA.
DR   EMBL; BC112940; AAI12941.1; -; mRNA.
DR   EMBL; BC132723; AAI32724.1; -; mRNA.
DR   EMBL; BC144107; AAI44108.1; -; mRNA.
DR   EMBL; AJ288057; CAC35156.1; -; mRNA.
DR   EMBL; CR933722; CAI46251.1; -; mRNA.
DR   EMBL; AB014522; BAA31597.1; -; mRNA.
DR   CCDS; CCDS92851.1; -. [Q7Z460-2]
DR   CCDS; CCDS92852.1; -. [Q7Z460-1]
DR   CCDS; CCDS92854.1; -. [Q7Z460-4]
DR   PIR; T00387; T00387.
DR   RefSeq; NP_001135745.1; NM_001142273.1. [Q7Z460-5]
DR   RefSeq; NP_001135746.1; NM_001142274.1. [Q7Z460-2]
DR   RefSeq; NP_001193980.1; NM_001207051.1. [Q7Z460-4]
DR   RefSeq; NP_056097.1; NM_015282.2. [Q7Z460-1]
DR   RefSeq; XP_011509150.1; XM_011510848.1. [Q7Z460-3]
DR   PDB; 4K92; X-ray; 2.00 A; A/B=284-552.
DR   PDB; 6MQ5; X-ray; 2.15 A; A/B=1-257.
DR   PDB; 6MQ7; X-ray; 1.78 A; A/B=284-552.
DR   PDBsum; 4K92; -.
DR   PDBsum; 6MQ5; -.
DR   PDBsum; 6MQ7; -.
DR   AlphaFoldDB; Q7Z460; -.
DR   SMR; Q7Z460; -.
DR   BioGRID; 116919; 116.
DR   IntAct; Q7Z460; 53.
DR   MINT; Q7Z460; -.
DR   STRING; 9606.ENSP00000263710; -.
DR   DrugBank; DB12010; Fostamatinib.
DR   GlyCosmos; Q7Z460; 1 site, 1 glycan.
DR   GlyGen; Q7Z460; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; Q7Z460; -.
DR   MetOSite; Q7Z460; -.
DR   PhosphoSitePlus; Q7Z460; -.
DR   SwissPalm; Q7Z460; -.
DR   BioMuta; CLASP1; -.
DR   DMDM; 74723323; -.
DR   EPD; Q7Z460; -.
DR   jPOST; Q7Z460; -.
DR   MassIVE; Q7Z460; -.
DR   MaxQB; Q7Z460; -.
DR   PaxDb; 9606-ENSP00000263710; -.
DR   PeptideAtlas; Q7Z460; -.
DR   ProteomicsDB; 24199; -.
DR   ProteomicsDB; 69152; -. [Q7Z460-1]
DR   ProteomicsDB; 69153; -. [Q7Z460-2]
DR   ProteomicsDB; 69154; -. [Q7Z460-3]
DR   ProteomicsDB; 7239; -.
DR   Pumba; Q7Z460; -.
DR   Antibodypedia; 33401; 332 antibodies from 32 providers.
DR   DNASU; 23332; -.
DR   Ensembl; ENST00000263710.8; ENSP00000263710.4; ENSG00000074054.21. [Q7Z460-1]
DR   Ensembl; ENST00000409078.8; ENSP00000386442.3; ENSG00000074054.21. [Q7Z460-2]
DR   Ensembl; ENST00000541377.5; ENSP00000441625.1; ENSG00000074054.21. [Q7Z460-4]
DR   GeneID; 23332; -.
DR   KEGG; hsa:23332; -.
DR   UCSC; uc061nlf.1; human. [Q7Z460-1]
DR   AGR; HGNC:17088; -.
DR   CTD; 23332; -.
DR   DisGeNET; 23332; -.
DR   GeneCards; CLASP1; -.
DR   HGNC; HGNC:17088; CLASP1.
DR   HPA; ENSG00000074054; Low tissue specificity.
DR   MalaCards; CLASP1; -.
DR   MIM; 605852; gene.
DR   neXtProt; NX_Q7Z460; -.
DR   OpenTargets; ENSG00000074054; -.
DR   PharmGKB; PA38436; -.
DR   VEuPathDB; HostDB:ENSG00000074054; -.
DR   eggNOG; KOG2956; Eukaryota.
DR   GeneTree; ENSGT00940000154817; -.
DR   InParanoid; Q7Z460; -.
DR   OMA; LMEHKVQ; -.
DR   OrthoDB; 5478662at2759; -.
DR   PhylomeDB; Q7Z460; -.
DR   TreeFam; TF101155; -.
DR   PathwayCommons; Q7Z460; -.
DR   Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR   Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR   Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR   Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR   Reactome; R-HSA-428890; Role of ABL in ROBO-SLIT signaling.
DR   Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR   Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-HSA-68877; Mitotic Prometaphase.
DR   Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR   Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR   SignaLink; Q7Z460; -.
DR   SIGNOR; Q7Z460; -.
DR   BioGRID-ORCS; 23332; 19 hits in 398 CRISPR screens.
DR   ChiTaRS; CLASP1; human.
DR   GeneWiki; CLASP1; -.
DR   GenomeRNAi; 23332; -.
DR   Pharos; Q7Z460; Tbio.
DR   PRO; PR:Q7Z460; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q7Z460; Protein.
DR   Bgee; ENSG00000074054; Expressed in cortical plate and 203 other cell types or tissues.
DR   ExpressionAtlas; Q7Z460; baseline and differential.
DR   GO; GO:0045180; C:basal cortex; IDA:UniProtKB.
DR   GO; GO:0005938; C:cell cortex; IDA:MGI.
DR   GO; GO:0031592; C:centrosomal corona; IDA:UniProtKB.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0030981; C:cortical microtubule cytoskeleton; IDA:UniProtKB.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR   GO; GO:0005828; C:kinetochore microtubule; TAS:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR   GO; GO:0035371; C:microtubule plus-end; ISS:UniProtKB.
DR   GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR   GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB.
DR   GO; GO:0002162; F:dystroglycan binding; IPI:UniProtKB.
DR   GO; GO:0043515; F:kinetochore binding; IMP:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR   GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
DR   GO; GO:0030953; P:astral microtubule organization; IMP:UniProtKB.
DR   GO; GO:0051301; P:cell division; IDA:MGI.
DR   GO; GO:0090162; P:establishment of epithelial cell polarity; ISS:UniProtKB.
DR   GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:UniProtKB.
DR   GO; GO:0051294; P:establishment of spindle orientation; IDA:MGI.
DR   GO; GO:0007163; P:establishment or maintenance of cell polarity; NAS:UniProtKB.
DR   GO; GO:0010458; P:exit from mitosis; IMP:UniProtKB.
DR   GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR   GO; GO:0034453; P:microtubule anchoring; IMP:UniProtKB.
DR   GO; GO:0001578; P:microtubule bundle formation; IMP:UniProtKB.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
DR   GO; GO:0007020; P:microtubule nucleation; IMP:UniProtKB.
DR   GO; GO:0031023; P:microtubule organizing center organization; IMP:UniProtKB.
DR   GO; GO:0090307; P:mitotic spindle assembly; ISS:UniProtKB.
DR   GO; GO:0007052; P:mitotic spindle organization; IMP:UniProtKB.
DR   GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:UniProtKB.
DR   GO; GO:0031111; P:negative regulation of microtubule polymerization or depolymerization; IMP:UniProtKB.
DR   GO; GO:0051497; P:negative regulation of stress fiber assembly; IMP:UniProtKB.
DR   GO; GO:1903690; P:negative regulation of wound healing, spreading of epidermal cells; IMP:UniProtKB.
DR   GO; GO:1904261; P:positive regulation of basement membrane assembly involved in embryonic body morphogenesis; IMP:UniProtKB.
DR   GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:UniProtKB.
DR   GO; GO:0045921; P:positive regulation of exocytosis; IMP:UniProtKB.
DR   GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; IMP:UniProtKB.
DR   GO; GO:0031116; P:positive regulation of microtubule polymerization; ISS:UniProtKB.
DR   GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
DR   GO; GO:0051893; P:regulation of focal adhesion assembly; IMP:UniProtKB.
DR   GO; GO:0010470; P:regulation of gastrulation; IMP:UniProtKB.
DR   GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IGI:UniProtKB.
DR   GO; GO:0006903; P:vesicle targeting; IMP:UniProtKB.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 4.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR024395; CLASP_N_dom.
DR   InterPro; IPR021133; HEAT_type_2.
DR   InterPro; IPR034085; TOG.
DR   InterPro; IPR048491; XMAP215_CLASP_TOG.
DR   PANTHER; PTHR21567; CLASP; 1.
DR   PANTHER; PTHR21567:SF28; CLIP-ASSOCIATING PROTEIN 1; 1.
DR   Pfam; PF21040; CEP104-like_TOG; 1.
DR   Pfam; PF12348; CLASP_N; 1.
DR   Pfam; PF21041; XMAP215_CLASP_TOG; 1.
DR   SMART; SM01349; TOG; 4.
DR   SUPFAM; SSF48371; ARM repeat; 2.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
DR   Genevisible; Q7Z460; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell cycle; Cell division; Centromere;
KW   Chromosome; Coiled coil; Cytoplasm; Cytoskeleton; Golgi apparatus;
KW   Kinetochore; Microtubule; Mitosis; Phosphoprotein; Reference proteome;
KW   Repeat.
FT   CHAIN           1..1538
FT                   /note="CLIP-associating protein 1"
FT                   /id="PRO_0000089847"
FT   REPEAT          87..124
FT                   /note="HEAT 1"
FT   REPEAT          163..200
FT                   /note="HEAT 2"
FT   REPEAT          405..440
FT                   /note="HEAT 3"
FT   REPEAT          441..477
FT                   /note="HEAT 4"
FT   REPEAT          974..1011
FT                   /note="HEAT 5"
FT   REPEAT          1342..1379
FT                   /note="HEAT 6"
FT   REPEAT          1460..1497
FT                   /note="HEAT 7"
FT   REGION          235..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          543..783
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          662..785
FT                   /note="Interaction with microtubules, MAPRE1 and MAPRE3"
FT                   /evidence="ECO:0000269|PubMed:15631994"
FT   REGION          1080..1120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1136..1156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1215..1238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1254..1538
FT                   /note="Interaction with CLIP2"
FT                   /evidence="ECO:0000250"
FT   REGION          1254..1538
FT                   /note="Interaction with PHLDB2 and RSN"
FT                   /evidence="ECO:0000269|PubMed:16824950"
FT   REGION          1256..1538
FT                   /note="Localization to kinetochores"
FT   COILED          1299..1330
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        250..288
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        543..627
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..691
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        706..755
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         246
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         545
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         548
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80TV8"
FT   MOD_RES         558
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         559
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         568
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         600
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         636
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         646
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         647
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         649
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         656
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         684
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         688
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332"
FT   MOD_RES         695
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         705
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         711
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         714
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         787
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         797
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         823
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1091
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT   MOD_RES         1095
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80TV8"
FT   MOD_RES         1099
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1113
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q80TV8"
FT   MOD_RES         1196
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18088087,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1223
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   VAR_SEQ         637
FT                   /note="L -> LESRHMREDMEYIGLDS (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_054412"
FT   VAR_SEQ         637
FT                   /note="L -> LDGTTTKAE (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_057272"
FT   VAR_SEQ         673..682
FT                   /note="RSRSANPAGA -> P (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_054413"
FT   VAR_SEQ         737..772
FT                   /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT                   isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_022386"
FT   VAR_SEQ         808
FT                   /note="L -> LLLGDSRSK (in isoform 2, isoform 3 and isoform
FT                   5)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_022387"
FT   VAR_SEQ         808
FT                   /note="L -> LLLGDSRS (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_054414"
FT   VAR_SEQ         911
FT                   /note="K -> KIADSEAECEDKEGNLFPSEVSCT (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_022388"
FT   VAR_SEQ         1123..1161
FT                   /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT                   isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:17974005"
FT                   /id="VSP_022389"
FT   VARIANT         233
FT                   /note="I -> T (in dbSNP:rs17761055)"
FT                   /id="VAR_053818"
FT   CONFLICT        251
FT                   /note="R -> G (in Ref. 5; CAI46251)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        556
FT                   /note="S -> F (in Ref. 5; CAI46251)"
FT                   /evidence="ECO:0000305"
FT   HELIX           5..13
FT                   /evidence="ECO:0007829|PDB:6MQ5"
FT   HELIX           17..32
FT                   /evidence="ECO:0007829|PDB:6MQ5"
FT   TURN            34..42
FT                   /evidence="ECO:0007829|PDB:6MQ5"
FT   HELIX           44..56
FT                   /evidence="ECO:0007829|PDB:6MQ5"
FT   TURN            57..60
FT                   /evidence="ECO:0007829|PDB:6MQ5"
FT   HELIX           64..81
FT                   /evidence="ECO:0007829|PDB:6MQ5"
FT   HELIX           82..85
FT                   /evidence="ECO:0007829|PDB:6MQ5"
FT   HELIX           86..99
FT                   /evidence="ECO:0007829|PDB:6MQ5"
FT   HELIX           105..121
FT                   /evidence="ECO:0007829|PDB:6MQ5"
FT   HELIX           125..130
FT                   /evidence="ECO:0007829|PDB:6MQ5"
FT   HELIX           133..137
FT                   /evidence="ECO:0007829|PDB:6MQ5"
FT   STRAND          138..140
FT                   /evidence="ECO:0007829|PDB:6MQ5"
FT   HELIX           141..158
FT                   /evidence="ECO:0007829|PDB:6MQ5"
FT   HELIX           160..162
FT                   /evidence="ECO:0007829|PDB:6MQ5"
FT   HELIX           165..176
FT                   /evidence="ECO:0007829|PDB:6MQ5"
FT   HELIX           181..198
FT                   /evidence="ECO:0007829|PDB:6MQ5"
FT   HELIX           200..207
FT                   /evidence="ECO:0007829|PDB:6MQ5"
FT   HELIX           213..228
FT                   /evidence="ECO:0007829|PDB:6MQ5"
FT   HELIX           296..305
FT                   /evidence="ECO:0007829|PDB:6MQ7"
FT   HELIX           317..331
FT                   /evidence="ECO:0007829|PDB:6MQ7"
FT   HELIX           338..353
FT                   /evidence="ECO:0007829|PDB:6MQ7"
FT   HELIX           356..358
FT                   /evidence="ECO:0007829|PDB:6MQ7"
FT   HELIX           362..367
FT                   /evidence="ECO:0007829|PDB:6MQ7"
FT   HELIX           370..377
FT                   /evidence="ECO:0007829|PDB:6MQ7"
FT   HELIX           382..399
FT                   /evidence="ECO:0007829|PDB:6MQ7"
FT   HELIX           400..403
FT                   /evidence="ECO:0007829|PDB:6MQ7"
FT   HELIX           404..415
FT                   /evidence="ECO:0007829|PDB:6MQ7"
FT   TURN            416..419
FT                   /evidence="ECO:0007829|PDB:6MQ7"
FT   HELIX           423..439
FT                   /evidence="ECO:0007829|PDB:6MQ7"
FT   HELIX           445..450
FT                   /evidence="ECO:0007829|PDB:6MQ7"
FT   HELIX           451..454
FT                   /evidence="ECO:0007829|PDB:6MQ7"
FT   HELIX           458..474
FT                   /evidence="ECO:0007829|PDB:6MQ7"
FT   HELIX           477..479
FT                   /evidence="ECO:0007829|PDB:6MQ7"
FT   HELIX           481..483
FT                   /evidence="ECO:0007829|PDB:6MQ7"
FT   HELIX           484..495
FT                   /evidence="ECO:0007829|PDB:6MQ7"
FT   HELIX           500..516
FT                   /evidence="ECO:0007829|PDB:6MQ7"
FT   HELIX           518..525
FT                   /evidence="ECO:0007829|PDB:6MQ7"
FT   HELIX           530..537
FT                   /evidence="ECO:0007829|PDB:6MQ7"
SQ   SEQUENCE   1538 AA;  169451 MW;  6E03BD948C227F8D CRC64;
     MEPRMESCLA QVLQKDVGKR LQVGQELIDY FSDKQKSADL EHDQTMLDKL VDGLATSWVN
     SSNYKVVLLG MDILSALVTR LQDRFKAQIG TVLPSLIDRL GDAKDSVREQ DQTLLLKIMD
     QAANPQYVWD RMLGGFKHKN FRTREGICLC LIATLNASGA QTLTLSKIVP HICNLLGDPN
     SQVRDAAINS LVEIYRHVGE RVRADLSKKG LPQSRLNVIF TKFDEVQKSG NMIQSANDKN
     FDDEDSVDGN RPSSASSTSS KAPPSSRRNV GMGTTRRLGS STLGSKSSAA KEGAGAVDEE
     DFIKAFDDVP VVQIYSSRDL EESINKIREI LSDDKHDWEQ RVNALKKIRS LLLAGAAEYD
     NFFQHLRLLD GAFKLSAKDL RSQVVREACI TLGHLSSVLG NKFDHGAEAI MPTIFNLIPN
     SAKIMATSGV VAVRLIIRHT HIPRLIPVIT SNCTSKSVAV RRRCFEFLDL LLQEWQTHSL
     ERHISVLAET IKKGIHDADS EARIEARKCY WGFHSHFSRE AEHLYHTLES SYQKALQSHL
     KNSDSIVSLP QSDRSSSSSQ ESLNRPLSAK RSPTGSTTSR ASTVSTKSVS TTGSLQRSRS
     DIDVNAAASA KSKVSSSSGT TPFSSAAALP PGSYASLGRI RTRRQSSGSA TNVASTPDNR
     GRSRAKVVSQ SQRSRSANPA GAGSRSSSPG KLLGSGYGGL TGGSSRGPPV TPSSEKRSKI
     PRSQGCSRET SPNRIGLARS SRIPRPSMSQ GCSRDTSRES SRDTSPARGF PPLDRFGLGQ
     PGRIPGSVNA MRVLSTSTDL EAAVADALKK PVRRRYEPYG MYSDDDANSD ASSVCSERSY
     GSRNGGIPHY LRQTEDVAEV LNHCASSNWS ERKEGLLGLQ NLLKSQRTLS RVELKRLCEI
     FTRMFADPHS KRVFSMFLET LVDFIIIHKD DLQDWLFVLL TQLLKKMGAD LLGSVQAKVQ
     KALDVTRDSF PFDQQFNILM RFIVDQTQTP NLKVKVAILK YIESLARQMD PTDFVNSSET
     RLAVSRIITW TTEPKSSDVR KAAQIVLISL FELNTPEFTM LLGALPKTFQ DGATKLLHNH
     LKNSSNTSVG SPSNTIGRTP SRHTSSRTSP LTSPTNCSHG GLSPSRLWGW SADGLAKHPP
     PFSQPNSIPT APSHKALRRS YSPSMLDYDT ENLNSEEIYS SLRGVTEAIE KFSFRSQEDL
     NEPIKRDGKK ECDIVSRDGG AASPATEGRG GSEVEGGRTA LDNKTSLLNT QPPRAFPGPR
     ARDYNPYPYS DAINTYDKTA LKEAVFDDDM EQLRDVPIDH SDLVADLLKE LSNHNERVEE
     RKGALLELLK ITREDSLGVW EEHFKTILLL LLETLGDKDH SIRALALRVL REILRNQPAR
     FKNYAELTIM KTLEAHKDSH KEVVRAAEEA ASTLASSIHP EQCIKVLCPI IQTADYPINL
     AAIKMQTKVV ERIAKESLLQ LLVDIIPGLL QGYDNTESSV RKASVFCLVA IYSVIGEDLK
     PHLAQLTGSK MKLLNLYIKR AQTTNSNSSS SSDVSTHS
//