ID   KC1D_RAT                Reviewed;         415 AA.
AC   Q06486; Q99KK4;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   27-MAR-2024, entry version 195.
DE   RecName: Full=Casein kinase I isoform delta;
DE            Short=CKI-delta;
DE            EC=2.7.11.1 {ECO:0000269|PubMed:15961172};
DE   AltName: Full=Tau-protein kinase CSNK1D;
DE            EC=2.7.11.26 {ECO:0000250|UniProtKB:P48730};
GN   Name=Csnk1d; Synonyms=Hckid;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PROTEIN SEQUENCE OF 1-6.
RC   TISSUE=Testis;
RX   PubMed=8454611; DOI=10.1016/s0021-9258(18)53265-8;
RA   Graves P.R., Haas D.W., Hagedorn C.H., Depaoli-Roach A.A., Roach P.J.;
RT   "Molecular cloning, expression, and characterization of a 49-kilodalton
RT   casein kinase I isoform from rat testis.";
RL   J. Biol. Chem. 268:6394-6401(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Takano A., Nagai K.;
RT   "Casein kinase 1 delta rat.";
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   AUTOPHOSPHORYLATION, AND AUTOINHIBITORY DOMAIN.
RX   PubMed=7665585; DOI=10.1074/jbc.270.37.21689;
RA   Graves P.R., Roach P.J.;
RT   "Role of COOH-terminal phosphorylation in the regulation of casein kinase I
RT   delta.";
RL   J. Biol. Chem. 270:21689-21694(1995).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=11165242; DOI=10.1016/s0014-5793(00)02434-0;
RA   Camacho F., Cilio M., Guo Y., Virshup D.M., Patel K., Khorkova O.,
RA   Styren S., Morse B., Yao Z., Keesler G.A.;
RT   "Human casein kinase Idelta phosphorylation of human circadian clock
RT   proteins period 1 and 2.";
RL   FEBS Lett. 489:159-165(2001).
RN   [5]
RP   FUNCTION AS MAP1A KINASE, INTERACTION WITH MAP1A, AND CATALYTIC ACTIVITY.
RX   PubMed=15961172; DOI=10.1016/j.bbamcr.2005.05.004;
RA   Wolff S., Xiao Z., Wittau M., Suessner N., Stoeter M., Knippschild U.;
RT   "Interaction of casein kinase 1 delta (CK1 delta) with the light chain LC2
RT   of microtubule associated protein 1A (MAP1A).";
RL   Biochim. Biophys. Acta 1745:196-206(2005).
RN   [6]
RP   PHOSPHORYLATION AT SER-370 BY PKA.
RX   PubMed=17594292; DOI=10.1042/bj20070091;
RA   Giamas G., Hirner H., Shoshiashvili L., Grothey A., Gessert S., Kuehl M.,
RA   Henne-Bruns D., Vorgias C.E., Knippschild U.;
RT   "Phosphorylation of CK1delta: identification of Ser370 as the major
RT   phosphorylation site targeted by PKA in vitro and in vivo.";
RL   Biochem. J. 406:389-398(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-317, AND ACTIVE SITE.
RX   PubMed=8648628; DOI=10.1006/jmbi.1996.0189;
RA   Longenecker K.L., Roach P.J., Hurley T.D.;
RT   "Three-dimensional structure of mammalian casein kinase I: molecular basis
RT   for phosphate recognition.";
RL   J. Mol. Biol. 257:618-631(1996).
CC   -!- FUNCTION: Essential serine/threonine-protein kinase that regulates
CC       diverse cellular growth and survival processes including Wnt signaling,
CC       DNA repair and circadian rhythms. It can phosphorylate a large number
CC       of proteins. Casein kinases are operationally defined by their
CC       preferential utilization of acidic proteins such as caseins as
CC       substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU,
CC       TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1,
CC       PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In
CC       balance with PP1, determines the circadian period length through the
CC       regulation of the speed and rhythmicity of PER1 and PER2
CC       phosphorylation. Controls PER1 and PER2 nuclear transport and
CC       degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3
CC       ubiquitin ligase-mediated ubiquitination and subsequent degradation.
CC       DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation
CC       of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation.
CC       Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that
CC       controls neurite outgrowth. Phosphorylates NEDD9/HEF1 (By similarity).
CC       EIF6 phosphorylation promotes its nuclear export. Triggers down-
CC       regulation of dopamine receptors in the forebrain. Activates DCK in
CC       vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable
CC       complex formation. May regulate the formation of the mitotic spindle
CC       apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap
CC       junction assembly by phosphorylation. Probably involved in lymphocyte
CC       physiology. Regulates fast synaptic transmission mediated by glutamate
CC       (By similarity). {ECO:0000250|UniProtKB:P48730,
CC       ECO:0000250|UniProtKB:Q9DC28, ECO:0000269|PubMed:15961172}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC         Evidence={ECO:0000269|PubMed:15961172};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC         Evidence={ECO:0000305|PubMed:15961172};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1; Evidence={ECO:0000269|PubMed:15961172};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC         Evidence={ECO:0000305|PubMed:15961172};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-
CC         COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26;
CC         Evidence={ECO:0000250|UniProtKB:P48730};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12802;
CC         Evidence={ECO:0000250|UniProtKB:P48730};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[tau protein]; Xref=Rhea:RHEA:53904, Rhea:RHEA-COMP:13703,
CC         Rhea:RHEA-COMP:13704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.26; Evidence={ECO:0000250|UniProtKB:P48730};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53905;
CC         Evidence={ECO:0000250|UniProtKB:P48730};
CC   -!- ACTIVITY REGULATION: Drug-mediated inhibition leads to a delay of the
CC       oscillations with the magnitude of this effect dependent upon the
CC       timing of drug administration. Inhibited by phosphorylation (By
CC       similarity). Exhibits substrate-dependent heparin activation.
CC       {ECO:0000250|UniProtKB:P48730}.
CC   -!- SUBUNIT: Monomer (By similarity). Component of the circadian core
CC       oscillator, which includes the CRY proteins, CLOCK, or NPAS2,
CC       ARTNL/BMAL1 or ARTNL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS and the PER
CC       proteins (By similarity). Interacts with DNMT1 (By similarity).
CC       Interacts directly with PER1 and PER2 which may lead to their
CC       degradation (By similarity). Interacts with MAPT/TAU, SNAPIN, DBNDD2,
CC       AIB1/NCOA3 and ESR1 (By similarity). Interacts with AKAP9/AKAP450; this
CC       interaction promotes centrosomal subcellular location (By similarity).
CC       Binds to tubulins in mitotic cells upon DNA damage (By similarity).
CC       Interacts with GJA1 (By similarity). Interacts with MAP1A
CC       (PubMed:15961172). Interacts with DDX3X; this interaction enhances
CC       CSNK1D kinase activity in vitro, but it is unclear whether this
CC       interaction is physiologically relevant (By similarity).
CC       {ECO:0000250|UniProtKB:P48730, ECO:0000250|UniProtKB:Q9DC28,
CC       ECO:0000269|PubMed:15961172}.
CC   -!- INTERACTION:
CC       Q06486; Q00987: MDM2; Xeno; NbExp=2; IntAct=EBI-2910316, EBI-389668;
CC       Q06486-2; Q9Z266: Snapin; Xeno; NbExp=4; IntAct=EBI-7088890, EBI-6170320;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Cell
CC       membrane {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
CC       Golgi apparatus {ECO:0000250}. Note=Localized at mitotic spindle
CC       microtubules, and at the centrosomes and interphase in interphase
CC       cells. Recruited to the spindle apparatus and the centrosomes in
CC       response to DNA-damage. Correct subcellular localization requires
CC       kinase activity (By similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q06486-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q06486-2; Sequence=VSP_010255;
CC   -!- TISSUE SPECIFICITY: Expressed in most tissues, including heart, brain,
CC       testis, kidney, spleen and lung. {ECO:0000269|PubMed:11165242}.
CC   -!- DOMAIN: The autoinhibitory domain is involved in regulating enzyme
CC       activity through autophosphorylation and possibly, through heparin
CC       binding.
CC   -!- PTM: Autophosphorylated on serine and threonine residues; this
CC       autophosphorylation represses activity. Reactivated by phosphatase-
CC       mediated dephosphorylation. May be dephosphorylated by PP1.
CC       {ECO:0000269|PubMed:17594292}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CK1 Ser/Thr
CC       protein kinase family. Casein kinase I subfamily. {ECO:0000305}.
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DR   EMBL; L07578; AAA40934.1; -; mRNA.
DR   EMBL; AB063114; BAB60852.1; -; mRNA.
DR   PIR; A46002; A46002.
DR   RefSeq; NP_620691.2; NM_139060.3. [Q06486-1]
DR   PDB; 1CKI; X-ray; 2.30 A; A/B=1-317.
DR   PDB; 1CKJ; X-ray; 2.46 A; A/B=1-317.
DR   PDBsum; 1CKI; -.
DR   PDBsum; 1CKJ; -.
DR   AlphaFoldDB; Q06486; -.
DR   SMR; Q06486; -.
DR   BioGRID; 249077; 14.
DR   IntAct; Q06486; 12.
DR   MINT; Q06486; -.
DR   STRING; 10116.ENSRNOP00000015178; -.
DR   BindingDB; Q06486; -.
DR   ChEMBL; CHEMBL4484; -.
DR   iPTMnet; Q06486; -.
DR   PhosphoSitePlus; Q06486; -.
DR   jPOST; Q06486; -.
DR   PaxDb; 10116-ENSRNOP00000015178; -.
DR   Ensembl; ENSRNOT00000015178.8; ENSRNOP00000015178.5; ENSRNOG00000036676.6. [Q06486-2]
DR   Ensembl; ENSRNOT00055056589; ENSRNOP00055046695; ENSRNOG00055032733. [Q06486-1]
DR   Ensembl; ENSRNOT00060015745; ENSRNOP00060012276; ENSRNOG00060009315. [Q06486-1]
DR   Ensembl; ENSRNOT00065007050; ENSRNOP00065004863; ENSRNOG00065004851. [Q06486-1]
DR   GeneID; 64462; -.
DR   KEGG; rno:64462; -.
DR   AGR; RGD:71031; -.
DR   CTD; 1453; -.
DR   RGD; 71031; Csnk1d.
DR   VEuPathDB; HostDB:ENSRNOG00000036676; -.
DR   eggNOG; KOG1164; Eukaryota.
DR   GeneTree; ENSGT00940000153536; -.
DR   HOGENOM; CLU_019279_2_2_1; -.
DR   InParanoid; Q06486; -.
DR   OMA; IFDWTFL; -.
DR   OrthoDB; 1534388at2759; -.
DR   PhylomeDB; Q06486; -.
DR   BRENDA; 2.7.11.1; 5301.
DR   Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR   Reactome; R-RNO-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR   Reactome; R-RNO-380259; Loss of Nlp from mitotic centrosomes.
DR   Reactome; R-RNO-380270; Recruitment of mitotic centrosome proteins and complexes.
DR   Reactome; R-RNO-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR   Reactome; R-RNO-380320; Recruitment of NuMA to mitotic centrosomes.
DR   Reactome; R-RNO-5620912; Anchoring of the basal body to the plasma membrane.
DR   Reactome; R-RNO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR   Reactome; R-RNO-8854518; AURKA Activation by TPX2.
DR   EvolutionaryTrace; Q06486; -.
DR   PRO; PR:Q06486; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000036676; Expressed in testis and 19 other cell types or tissues.
DR   GO; GO:0005813; C:centrosome; IDA:RGD.
DR   GO; GO:0036064; C:ciliary basal body; ISO:RGD.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0005819; C:spindle; ISO:RGD.
DR   GO; GO:0005876; C:spindle microtubule; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IDA:RGD.
DR   GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; ISO:RGD.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0050321; F:tau-protein kinase activity; ISO:RGD.
DR   GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEP:RGD.
DR   GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0007030; P:Golgi organization; ISO:RGD.
DR   GO; GO:0007020; P:microtubule nucleation; ISO:RGD.
DR   GO; GO:1904948; P:midbrain dopaminergic neuron differentiation; ISO:RGD.
DR   GO; GO:1905515; P:non-motile cilium assembly; ISO:RGD.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:RGD.
DR   GO; GO:2000052; P:positive regulation of non-canonical Wnt signaling pathway; ISO:RGD.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR   GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISO:RGD.
DR   GO; GO:0071539; P:protein localization to centrosome; ISO:RGD.
DR   GO; GO:0061512; P:protein localization to cilium; ISO:RGD.
DR   GO; GO:0034067; P:protein localization to Golgi apparatus; ISO:RGD.
DR   GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR   GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   GO; GO:0051225; P:spindle assembly; ISO:RGD.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd14125; STKc_CK1_delta_epsilon; 1.
DR   DisProt; DP03052; -.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR11909:SF18; CASEIN KINASE I ISOFORM DELTA; 1.
DR   PANTHER; PTHR11909; CASEIN KINASE-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; Q06486; RN.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Biological rhythms;
KW   Cell membrane; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW   Golgi apparatus; Kinase; Membrane; Methylation; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
FT   CHAIN           1..415
FT                   /note="Casein kinase I isoform delta"
FT                   /id="PRO_0000192836"
FT   DOMAIN          9..277
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          278..364
FT                   /note="Centrosomal localization signal (CLS)"
FT                   /evidence="ECO:0000250"
FT   REGION          301..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..342
FT                   /note="Autoinhibitory"
FT   COMPBIAS        301..320
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..359
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..415
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        128
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027,
FT                   ECO:0000269|PubMed:8648628"
FT   BINDING         15..23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         38
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         328
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48730"
FT   MOD_RES         331
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48730"
FT   MOD_RES         370
FT                   /note="Phosphoserine; by PKA"
FT                   /evidence="ECO:0000269|PubMed:17594292"
FT   MOD_RES         375
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DC28"
FT   MOD_RES         382
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         383
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48730"
FT   MOD_RES         384
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48730"
FT   MOD_RES         407
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48730"
FT   MOD_RES         411
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P48730"
FT   VAR_SEQ         400..415
FT                   /note="IPGRVASSGLQSVVHR -> RSRDMASLRLHAARQGARCRPQRPRRTTY
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8454611"
FT                   /id="VSP_010255"
FT   TURN            6..8
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   STRAND          9..17
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   STRAND          19..28
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   TURN            29..31
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   STRAND          34..42
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   HELIX           49..58
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   STRAND          68..74
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   STRAND          77..83
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   HELIX           89..95
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   TURN            96..98
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   HELIX           102..121
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   HELIX           131..133
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   HELIX           139..141
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   STRAND          145..147
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   TURN            159..161
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   STRAND          177..179
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   HELIX           182..185
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   HELIX           192..208
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   STRAND          220..222
FT                   /evidence="ECO:0007829|PDB:1CKJ"
FT   HELIX           225..234
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   HELIX           237..240
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   TURN            241..243
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   HELIX           246..257
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   HELIX           266..279
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   HELIX           289..292
FT                   /evidence="ECO:0007829|PDB:1CKI"
FT   HELIX           293..295
FT                   /evidence="ECO:0007829|PDB:1CKI"
SQ   SEQUENCE   415 AA;  47316 MW;  B97F04AF9EB466D2 CRC64;
     MELRVGNRYR LGRKIGSGSF GDIYLGTDIA AGEEVAIKLE CVKTKHPQLH IESKIYKMMQ
     GGVGIPTIRW CGAEGDYNVM VMELLGPSLE DLFNFCSRKF SLKTVLLLAD QMISRIEYIH
     SKNFIHRDVK PDNFLMGLGK KGNLVYIIDF GLAKKYRDAR THQHIPYREN KNLTGTARYA
     SINTHLGIEQ SRRDDLESLG YVLMYFNLGS LPWQGLKAAT KRQKYERISE KKMSTPIEVL
     CKGYPSEFAT YLNFCRSLRF DDKPDYSYLR QLFRNLFHRQ GFSYDYVFDW NMLKFGASRA
     ADDAERERRD REERLRHSRN PATRGLPSTA SGRLRGTQEV APPTPLTPTS HTANTSPRPV
     SGMERERKVS MRLHRGAPVN VSSSDLTGRQ DTSRMSTSQI PGRVASSGLQ SVVHR
//