ID   DPYL1_HUMAN             Reviewed;         572 AA.
AC   Q14194; A0EJG6; Q13024; Q4W5F1; Q96TC8;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 214.
DE   RecName: Full=Dihydropyrimidinase-related protein 1;
DE            Short=DRP-1;
DE   AltName: Full=Collapsin response mediator protein 1;
DE            Short=CRMP-1;
DE   AltName: Full=Inactive dihydropyrimidinase {ECO:0000305};
DE   AltName: Full=Unc-33-like phosphoprotein 3;
DE            Short=ULIP-3;
GN   Name=CRMP1; Synonyms=DPYSL1, ULIP3;
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).
RC   TISSUE=Brain;
RX   PubMed=8973361; DOI=10.1016/s0378-1119(96)00445-3;
RA   Hamajima N., Matsuda K., Sakata S., Tamaki N., Sasaki M., Nonaka M.;
RT   "A novel gene family defined by human dihydropyrimidinase and three related
RT   proteins with differential tissue distribution.";
RL   Gene 180:157-163(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LCRMP-1), AND ALTERNATIVE SPLICING.
RC   TISSUE=Lung adenocarcinoma;
RX   PubMed=19362386; DOI=10.1016/j.lungcan.2009.03.006;
RA   Pan S.-H., Chao Y.-C., Chen H.Y., Hung P.F., Lin P.Y., Lin C.W.,
RA   Chang Y.L., Wu C.T., Lee Y.C., Yang S.-C., Hong T.-M., Yang P.-C.;
RT   "Long form collapsin response mediator protein-1 (LCRMP-1) expression is
RT   associated with clinical outcome and lymph node metastasis in non-small
RT   cell lung cancer patients.";
RL   Lung Cancer 67:93-100(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 14-572 (ISOFORM 1).
RX   PubMed=10048489; DOI=10.1093/dnares/5.6.393;
RA   Torres R., Polymeropoulos M.H.;
RT   "Genomic organization and localization of the human CRMP-1 gene.";
RL   DNA Res. 5:393-395(1998).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 64-572 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=7637782; DOI=10.1038/376509a0;
RA   Goshima Y., Nakamura F., Strittmatter P., Strittmatter S.M.;
RT   "Collapsin-induced growth cone collapse mediated by an intracellular
RT   protein related to UNC-33.";
RL   Nature 376:509-514(1995).
RN   [9]
RP   PROTEIN SEQUENCE OF 44-56; 190-210; 246-254; 259-268; 346-361; 391-397;
RP   452-463; 472-481; 488-511 AND 533-552, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA   Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [10]
RP   SUBUNIT, AND INTERACTION WITH DPYSL2 AND DPYSL4.
RX   PubMed=9375656; DOI=10.1046/j.1471-4159.1997.69062261.x;
RA   Wang L.H., Strittmatter S.M.;
RT   "Brain CRMP forms heterotetramers similar to liver dihydropyrimidinase.";
RL   J. Neurochem. 69:2261-2269(1997).
RN   [11]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11562390; DOI=10.1093/jnci/93.18.1392;
RA   Shih J.-Y., Yang S.-C., Hong T.-M., Yuan A., Chen J.J.W., Yu C.-J.,
RA   Chang Y.-L., Lee Y.-C., Peck K., Wu C.-W., Yang P.-C.;
RT   "Collapsin response mediator protein-1 and the invasion and metastasis of
RT   cancer cells.";
RL   J. Natl. Cancer Inst. 93:1392-1400(2001).
RN   [12]
RP   FUNCTION, PHOSPHORYLATION AT THR-101 AND THR-102, AND MUTAGENESIS OF
RP   101-THR-THR-102.
RX   PubMed=19799413; DOI=10.1021/pr900325f;
RA   Chen T.C., Lee S.A., Hong T.M., Shih J.Y., Lai J.M., Chiou H.Y., Yang S.C.,
RA   Chan C.H., Kao C.Y., Yang P.C., Huang C.Y.;
RT   "From midbody protein-protein interaction network construction to novel
RT   regulators in cytokinesis.";
RL   J. Proteome Res. 8:4943-4953(2009).
RN   [13]
RP   FUNCTION, INTERACTION WITH FLNA, MOTIF, AND PHOSPHORYLATION AT SER-522.
RX   PubMed=25358863; DOI=10.1038/ncomms6325;
RA   Nakamura F., Kumeta K., Hida T., Isono T., Nakayama Y.,
RA   Kuramata-Matsuoka E., Yamashita N., Uchida Y., Ogura K., Gengyo-Ando K.,
RA   Mitani S., Ogino T., Goshima Y.;
RT   "Amino- and carboxyl-terminal domains of Filamin-A interact with CRMP1 to
RT   mediate Sema3A signalling.";
RL   Nat. Commun. 5:5325-5325(2014).
RN   [14] {ECO:0007744|PDB:4B3Z}
RP   X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS).
RX   PubMed=26249678; DOI=10.1107/s2053230x15009243;
RA   Liu S.H., Huang S.F., Hsu Y.L., Pan S.H., Chen Y.J., Lin Y.H.;
RT   "Structure of human collapsin response mediator protein 1: a possible role
RT   of its C-terminal tail.";
RL   Acta Crystallogr. F 71:938-945(2015).
CC   -!- FUNCTION: Necessary for signaling by class 3 semaphorins and subsequent
CC       remodeling of the cytoskeleton (PubMed:25358863). Plays a role in axon
CC       guidance (PubMed:25358863). During the axon guidance process, acts
CC       downstream of SEMA3A to promote FLNA dissociation from F-actin which
CC       results in the rearrangement of the actin cytoskeleton and the collapse
CC       of the growth cone (PubMed:25358863). Involved in invasive growth and
CC       cell migration (PubMed:11562390). May participate in cytokinesis
CC       (PubMed:19799413). {ECO:0000269|PubMed:11562390,
CC       ECO:0000269|PubMed:19799413, ECO:0000269|PubMed:25358863}.
CC   -!- SUBUNIT: Homotetramer, and heterotetramer with DPYSL2, DPYSL3, DPYSL4
CC       or DPYSL5 (By similarity). Interacts with PLXNA1 (By similarity).
CC       Interacts with FLNA (via calponin-homology (CH) domain 1 and filamin
CC       repeat 24); the interaction alters FLNA ternary structure and thus
CC       promotes FLNA dissociation from F-actin (PubMed:25358863).
CC       {ECO:0000250|UniProtKB:P97427, ECO:0000269|PubMed:25358863}.
CC   -!- INTERACTION:
CC       Q14194; Q9Y2T2: AP3M1; NbExp=6; IntAct=EBI-473101, EBI-2371151;
CC       Q14194; O15169: AXIN1; NbExp=2; IntAct=EBI-473101, EBI-710484;
CC       Q14194; P23560-2: BDNF; NbExp=3; IntAct=EBI-473101, EBI-12275524;
CC       Q14194; Q14194: CRMP1; NbExp=3; IntAct=EBI-473101, EBI-473101;
CC       Q14194; P02511: CRYAB; NbExp=3; IntAct=EBI-473101, EBI-739060;
CC       Q14194; Q16555: DPYSL2; NbExp=5; IntAct=EBI-473101, EBI-1104711;
CC       Q14194; Q14195-2: DPYSL3; NbExp=6; IntAct=EBI-473101, EBI-10232496;
CC       Q14194; P04406: GAPDH; NbExp=3; IntAct=EBI-473101, EBI-354056;
CC       Q14194; P07900: HSP90AA1; NbExp=3; IntAct=EBI-473101, EBI-296047;
CC       Q14194; P42858: HTT; NbExp=14; IntAct=EBI-473101, EBI-466029;
CC       Q14194; P63244: RACK1; NbExp=3; IntAct=EBI-473101, EBI-296739;
CC       Q14194; P08670: VIM; NbExp=3; IntAct=EBI-473101, EBI-353844;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11562390}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000269|PubMed:11562390}. Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000269|PubMed:11562390}. Cell projection, growth cone
CC       {ECO:0000250|UniProtKB:P97427}. Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:P97427}. Perikaryon
CC       {ECO:0000250|UniProtKB:P97427}. Note=Associated with centrosomes and
CC       the mitotic spindle during metaphase (PubMed:11562390). Colocalizes
CC       with FLNA and tubulin in the central region of DRG neuron growth cone
CC       (By similarity). Following SEMA3A stimulation of DRG neurons,
CC       colocalizes with F-actin (By similarity).
CC       {ECO:0000250|UniProtKB:P97427, ECO:0000269|PubMed:11562390}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q14194-1; Sequence=Displayed;
CC       Name=LCRMP-1;
CC         IsoId=Q14194-2; Sequence=VSP_042545;
CC   -!- TISSUE SPECIFICITY: Brain.
CC   -!- PTM: Phosphorylation at Ser-522 enhances CRMP1-mediated alteration of
CC       FLNA ternary structure and FLNA dissociation from F-actin.
CC       {ECO:0000269|PubMed:25358863}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Hydantoinase/dihydropyrimidinase family. {ECO:0000305}.
CC   -!- CAUTION: Lacks most of the conserved residues that are essential for
CC       binding the metal cofactor and hence for dihydropyrimidinase activity.
CC       Its enzyme activity is therefore unsure. {ECO:0000305}.
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DR   EMBL; D78012; BAA11190.1; -; mRNA.
DR   EMBL; DQ206871; ABB22046.1; -; mRNA.
DR   EMBL; BT006806; AAP35452.1; -; mRNA.
DR   EMBL; AC105915; AAY40959.1; -; Genomic_DNA.
DR   EMBL; CH471131; EAW82405.1; -; Genomic_DNA.
DR   EMBL; CH471131; EAW82407.1; -; Genomic_DNA.
DR   EMBL; BC000252; AAH00252.1; -; mRNA.
DR   EMBL; BC007613; AAH07613.1; -; mRNA.
DR   EMBL; AH010780; AAK55500.1; -; Genomic_DNA.
DR   EMBL; U17278; AAA93201.1; -; mRNA.
DR   CCDS; CCDS33950.1; -. [Q14194-2]
DR   CCDS; CCDS43207.1; -. [Q14194-1]
DR   PIR; JC5316; JC5316.
DR   RefSeq; NP_001014809.1; NM_001014809.2. [Q14194-2]
DR   RefSeq; NP_001275590.1; NM_001288661.1.
DR   RefSeq; NP_001275591.1; NM_001288662.1.
DR   RefSeq; NP_001304.1; NM_001313.4. [Q14194-1]
DR   PDB; 4B3Z; X-ray; 3.05 A; A/B/C/D=1-572.
DR   PDBsum; 4B3Z; -.
DR   AlphaFoldDB; Q14194; -.
DR   SMR; Q14194; -.
DR   BioGRID; 107790; 129.
DR   CORUM; Q14194; -.
DR   IntAct; Q14194; 98.
DR   MINT; Q14194; -.
DR   STRING; 9606.ENSP00000321606; -.
DR   MEROPS; M38.974; -.
DR   GlyCosmos; Q14194; 1 site, 1 glycan.
DR   GlyGen; Q14194; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q14194; -.
DR   PhosphoSitePlus; Q14194; -.
DR   SwissPalm; Q14194; -.
DR   BioMuta; CRMP1; -.
DR   DMDM; 3122031; -.
DR   EPD; Q14194; -.
DR   jPOST; Q14194; -.
DR   MassIVE; Q14194; -.
DR   MaxQB; Q14194; -.
DR   PaxDb; 9606-ENSP00000321606; -.
DR   PeptideAtlas; Q14194; -.
DR   ProteomicsDB; 59915; -. [Q14194-1]
DR   ProteomicsDB; 59916; -. [Q14194-2]
DR   Pumba; Q14194; -.
DR   ABCD; Q14194; 1 sequenced antibody.
DR   Antibodypedia; 9351; 467 antibodies from 36 providers.
DR   DNASU; 1400; -.
DR   Ensembl; ENST00000324989.12; ENSP00000321606.7; ENSG00000072832.15. [Q14194-2]
DR   Ensembl; ENST00000397890.7; ENSP00000380987.2; ENSG00000072832.15. [Q14194-1]
DR   GeneID; 1400; -.
DR   KEGG; hsa:1400; -.
DR   MANE-Select; ENST00000324989.12; ENSP00000321606.7; NM_001014809.3; NP_001014809.1. [Q14194-2]
DR   UCSC; uc003giq.5; human. [Q14194-1]
DR   AGR; HGNC:2365; -.
DR   CTD; 1400; -.
DR   DisGeNET; 1400; -.
DR   GeneCards; CRMP1; -.
DR   HGNC; HGNC:2365; CRMP1.
DR   HPA; ENSG00000072832; Tissue enhanced (brain, pituitary gland, retina).
DR   MIM; 602462; gene.
DR   neXtProt; NX_Q14194; -.
DR   OpenTargets; ENSG00000072832; -.
DR   PharmGKB; PA26885; -.
DR   VEuPathDB; HostDB:ENSG00000072832; -.
DR   eggNOG; KOG2584; Eukaryota.
DR   GeneTree; ENSGT01030000234527; -.
DR   InParanoid; Q14194; -.
DR   OMA; IANRINC; -.
DR   OrthoDB; 1772494at2759; -.
DR   PhylomeDB; Q14194; -.
DR   TreeFam; TF314706; -.
DR   PathwayCommons; Q14194; -.
DR   Reactome; R-HSA-399956; CRMPs in Sema3A signaling.
DR   SignaLink; Q14194; -.
DR   SIGNOR; Q14194; -.
DR   BioGRID-ORCS; 1400; 15 hits in 1138 CRISPR screens.
DR   ChiTaRS; CRMP1; human.
DR   GeneWiki; CRMP1; -.
DR   GenomeRNAi; 1400; -.
DR   Pharos; Q14194; Tbio.
DR   PRO; PR:Q14194; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q14194; Protein.
DR   Bgee; ENSG00000072832; Expressed in cortical plate and 146 other cell types or tissues.
DR   ExpressionAtlas; Q14194; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IDA:HPA.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR   GO; GO:0030496; C:midbody; IDA:HGNC.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0031005; F:filamin binding; IPI:WormBase.
DR   GO; GO:0016812; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0010977; P:negative regulation of neuron projection development; IGI:WormBase.
DR   GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
DR   CDD; cd01314; D-HYD; 1.
DR   DisProt; DP02620; -.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   NCBIfam; TIGR02033; D-hydantoinase; 1.
DR   PANTHER; PTHR11647:SF54; DIHYDROPYRIMIDINASE-RELATED PROTEIN 1; 1.
DR   PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 2.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   Genevisible; Q14194; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell projection; Cytoplasm;
KW   Cytoskeleton; Direct protein sequencing; Nitration; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..572
FT                   /note="Dihydropyrimidinase-related protein 1"
FT                   /id="PRO_0000165909"
FT   REGION          513..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           246..247
FT                   /note="Required for interaction with FLNA"
FT                   /evidence="ECO:0000269|PubMed:25358863"
FT   COMPBIAS        515..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62950"
FT   MOD_RES         101
FT                   /note="Phosphothreonine; by AURKA"
FT                   /evidence="ECO:0000269|PubMed:19799413"
FT   MOD_RES         102
FT                   /note="Phosphothreonine; by AURKA"
FT                   /evidence="ECO:0000269|PubMed:19799413"
FT   MOD_RES         316
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P97427"
FT   MOD_RES         504
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P97427"
FT   MOD_RES         509
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P97427"
FT   MOD_RES         521
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62950"
FT   MOD_RES         522
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000305|PubMed:25358863"
FT   MOD_RES         537
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97427"
FT   MOD_RES         540
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97427"
FT   MOD_RES         542
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P97427"
FT   VAR_SEQ         1..13
FT                   /note="MSYQGKKSIPHIT -> MADRRRAWNTEDDLPVYLARPGSAAQTPRQKYGGM
FT                   FAAVEGAYENKTIDFDAYSVGRRGSARTPRSAGRPDAVGLPGPGGSEDTASDVSEPSGS
FT                   AVSSPGERDERPPTLRIRRPAPRDLPLGRDNGQ (in isoform LCRMP-1)"
FT                   /evidence="ECO:0000303|PubMed:19362386"
FT                   /id="VSP_042545"
FT   VARIANT         461
FT                   /note="V -> I (in dbSNP:rs34611001)"
FT                   /id="VAR_037745"
FT   MUTAGEN         101..102
FT                   /note="TT->AA: 2.5-fold increase in cells with a defect of
FT                   cytokinesis."
FT                   /evidence="ECO:0000269|PubMed:19799413"
FT   CONFLICT        351..370
FT                   /note="Missing (in Ref. 7; AAK55500)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        504
FT                   /note="Y -> H (in Ref. 8; AAA93201)"
FT                   /evidence="ECO:0000305"
FT   STRAND          16..25
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   STRAND          30..38
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   STRAND          41..48
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   STRAND          53..59
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   STRAND          64..67
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   STRAND          69..74
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   HELIX           89..99
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   STRAND          101..108
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   HELIX           116..130
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   STRAND          132..140
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   HELIX           148..157
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   STRAND          163..170
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   TURN            171..174
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   HELIX           178..190
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   STRAND          194..198
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   HELIX           202..213
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   TURN            214..216
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   HELIX           221..225
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   HELIX           229..246
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   STRAND          250..255
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   HELIX           258..270
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   STRAND          274..279
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   HELIX           280..284
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   HELIX           288..291
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   HELIX           295..300
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   HELIX           313..322
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   HELIX           338..341
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   HELIX           342..344
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   HELIX           348..350
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   TURN            358..360
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   HELIX           361..369
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   TURN            370..373
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   HELIX           377..384
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   HELIX           386..391
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   TURN            395..397
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   STRAND          409..419
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   STRAND          426..430
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   TURN            433..436
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   STRAND          438..448
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   STRAND          451..455
FT                   /evidence="ECO:0007829|PDB:4B3Z"
FT   HELIX           476..489
FT                   /evidence="ECO:0007829|PDB:4B3Z"
SQ   SEQUENCE   572 AA;  62184 MW;  A5385FCC79328A30 CRC64;
     MSYQGKKSIP HITSDRLLIK GGRIINDDQS LYADVYLEDG LIKQIGENLI VPGGVKTIEA
     NGRMVIPGGI DVNTYLQKPS QGMTAADDFF QGTRAALVGG TTMIIDHVVP EPGSSLLTSF
     EKWHEAADTK SCCDYSLHVD ITSWYDGVRE ELEVLVQDKG VNSFQVYMAY KDVYQMSDSQ
     LYEAFTFLKG LGAVILVHAE NGDLIAQEQK RILEMGITGP EGHALSRPEE LEAEAVFRAI
     TIAGRINCPV YITKVMSKSA ADIIALARKK GPLVFGEPIA ASLGTDGTHY WSKNWAKAAA
     FVTSPPLSPD PTTPDYLTSL LACGDLQVTG SGHCPYSTAQ KAVGKDNFTL IPEGVNGIEE
     RMTVVWDKAV ATGKMDENQF VAVTSTNAAK IFNLYPRKGR IAVGSDADVV IWDPDKLKTI
     TAKSHKSAVE YNIFEGMECH GSPLVVISQG KIVFEDGNIN VNKGMGRFIP RKAFPEHLYQ
     RVKIRNKVFG LQGVSRGMYD GPVYEVPATP KYATPAPSAK SSPSKHQPPP IRNLHQSNFS
     LSGAQIDDNN PRRTGHRIVA PPGGRSNITS LG
//