(data stored in ACNUC5448 zone)

HOGENOM: MOUSE16_PE822

ID   MOUSE16_PE822                        STANDARD;      PRT;   1654 AA.
AC   MOUSE16_PE822;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Kalirin; EC=2.7.11 1;AltName: Full=Protein Duo;AltName:
DE   Full=Serine/threonine-protein kinase with Dbl- and pleckstrin homology
DE   domain; (MOUSE16.PE822).
GN   Name=Kalrn;
OS   MUS MUSCULUS.
OC   Eukaryota; Metazoa; Eumetazoa; Bilateria; Coelomata; Deuterostomia;
OC   Chordata; Craniata; Vertebrata; Gnathostomata; Teleostomi; Euteleostomi;
OC   Sarcopterygii; Tetrapoda; Amniota; Mammalia; Theria; Eutheria;
OC   Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae;
OC   Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MOUSE16.PE822.
CC       Mus musculus chromosome 16 NCBIM37  sequence 1..98319150 annotated by
CC       Ensembl
CC   -!- ANNOTATIONS ORIGIN:KALRN_MOUSE
CC   -!- FUNCTION: Promotes the exchange of GDP by GTP. Activates specific
CC       Rho GTPase family members, thereby inducing various signaling
CC       mechanisms that regulate neuronal shape, growth, and plasticity,
CC       through their effects on the actin cytoskeleton. Induces
CC       lamellipodia independent of its GEF activity (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBUNIT: Interacts with the C-terminal of peptidylglycine alpha-
CC       amidating monooxygenase (PAM) and with the huntingtin-associated
CC       protein 1 (HAP1). Interacts with FASLG (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Cytoplasm,
CC       cytoskeleton (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing, Alternative initiation; Named isoforms=9;
CC       Name=1;
CC         IsoId=A2CG49-1; Sequence=Displayed;
CC         Note=Produced by alternative splicing;
CC       Name=2;
CC         IsoId=A2CG49-2; Sequence=VSP_052576, VSP_052579;
CC         Note=Produced by alternative splicing. No experimental
CC         confirmation available;
CC       Name=3;
CC         IsoId=A2CG49-3; Sequence=VSP_052562;
CC         Note=Produced by alternative splicing. No experimental
CC         confirmation available;
CC       Name=4;
CC         IsoId=A2CG49-4; Sequence=VSP_052563, VSP_052570, VSP_052571,
CC                                  VSP_052573, VSP_052577, VSP_052578;
CC         Note=Produced by alternative splicing. No experimental
CC         confirmation available;
CC       Name=5;
CC         IsoId=A2CG49-5; Sequence=VSP_052564, VSP_052567, VSP_052568,
CC                                  VSP_052569;
CC         Note=Produced by alternative initiation at Met-624 of isoform 1.
CC         Inferred by similarity. Ref.1 (BAE34776) sequence is in conflict
CC         in position: 711:E->K;
CC       Name=6;
CC         IsoId=A2CG49-6; Sequence=VSP_052563, VSP_052570, VSP_052573,
CC                                  VSP_052574, VSP_052575;
CC         Note=Produced by alternative splicing. No experimental
CC         confirmation available;
CC       Name=7;
CC         IsoId=A2CG49-7; Sequence=VSP_052565, VSP_052572;
CC         Note=Produced by alternative splicing;
CC       Name=8;
CC         IsoId=A2CG49-8; Sequence=VSP_052566, VSP_052567, VSP_052568,
CC                                  VSP_052569;
CC         Note=Produced by alternative splicing. No experimental
CC         confirmation available;
CC       Name=9;
CC         IsoId=A2CG49-9; Sequence=VSP_052566, VSP_052568, VSP_052569;
CC         Note=Produced by alternative splicing;
CC   -!- DOMAIN: The two GEF domains catalyze nucleotide exchange for RAC1
CC       and RhoA which are bound by DH1 and DH2 respectively. The two GEF
CC       domains appear to play differing roles in neuronal development and
CC       axonal outgrowth. SH3 1 binds to the first GEF domain inhibiting
CC       GEF activity only when in the presence of a PXXP peptide,
CC       suggesting that the SH3 domain/peptide interaction mediates
CC       binding to GEF1. CRK1 SH3 domain binds to and inhibits GEF1
CC       activity (By similarity).
CC   -!- PTM: Autophosphorylated (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family.
CC   -!- SIMILARITY: Contains 1 CRAL-TRIO domain.
CC   -!- SIMILARITY: Contains 2 DH (DBL-homology) domains.
CC   -!- SIMILARITY: Contains 1 fibronectin type-III domain.
CC   -!- SIMILARITY: Contains 1 Ig-like C2-type (immunoglobulin-like)
CC       domain.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 2 SH3 domains.
CC   -!- SIMILARITY: Contains 5 spectrin repeats.
CC   -!- GENE_FAMILY: HOG000044462 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Mus_musculus;ENSMUSG00000061751;ENSMUST00000114960;ENSMUSP00000110611.
DR   EMBL; AC154524; - ;
DR   EMBL; AC154588; - ;
DR   EMBL; AC155257; - ;
DR   EMBL; AC165079; - ;
DR   EMBL; AK008844; - ;
DR   EMBL; AK081504; - ;
DR   EMBL; AK088732; - ;
DR   EMBL; AK139581; - ;
DR   EMBL; AK158544; - ;
DR   EMBL; AK159031; - ;
DR   EMBL; BC058850; - ;
DR   EMBL; BC157950; - ;
DR   EMBL; BC172101; - ;
DR   EMBL; CT010573; - ;
DR   UniProtKB/Swiss-Prot; A2CG49; A2CG50; A2CG51; A2CG52; A2CG53; B2RXR5; Q3TXY8; Q3TYL1; -.
DR   UniProtKB/Swiss-Prot; Q3UTA5; Q8BTT9; Q8C4Q2; Q9CVA9; -.
DR   EMBL; AK008844; BAB25925.1; -; mRNA.
DR   EMBL; AK081504; BAC38239.1; -; mRNA.
DR   EMBL; AK088732; BAC40535.1; -; mRNA.
DR   EMBL; AK139581; BAE24075.1; -; mRNA.
DR   EMBL; AK158544; BAE34552.1; -; mRNA.
DR   EMBL; AK159031; BAE34776.1; -; mRNA.
DR   EMBL; CT010573; CAM18305.1; -; Genomic_DNA.
DR   EMBL; AC154524; CAM18305.1; JOINED; Genomic_DNA.
DR   EMBL; AC155257; CAM18305.1; JOINED; Genomic_DNA.
DR   EMBL; AC165079; CAM18305.1; JOINED; Genomic_DNA.
DR   EMBL; CT010573; CAM18306.1; -; Genomic_DNA.
DR   EMBL; AC154524; CAM18306.1; JOINED; Genomic_DNA.
DR   EMBL; AC165079; CAM18306.1; JOINED; Genomic_DNA.
DR   EMBL; CT010573; CAM18307.1; -; Genomic_DNA.
DR   EMBL; AC154524; CAM18307.1; JOINED; Genomic_DNA.
DR   EMBL; AC154588; CAM18307.1; JOINED; Genomic_DNA.
DR   EMBL; CT010573; CAM18308.1; -; Genomic_DNA.
DR   EMBL; AC154524; CAM18308.1; JOINED; Genomic_DNA.
DR   EMBL; AC154588; CAM18308.1; JOINED; Genomic_DNA.
DR   EMBL; CT010573; CAM18309.1; -; Genomic_DNA.
DR   EMBL; AC154524; CAM18309.1; JOINED; Genomic_DNA.
DR   EMBL; AC154588; CAM18309.1; JOINED; Genomic_DNA.
DR   EMBL; BC157950; AAI57951.1; -; mRNA.
DR   EMBL; BC172101; AAI72101.1; -; mRNA.
DR   IPI; IPI00225550; -.
DR   IPI; IPI00620349; -.
DR   IPI; IPI00653391; -.
DR   IPI; IPI00660519; -.
DR   IPI; IPI00673239; -.
DR   IPI; IPI00762276; -.
DR   IPI; IPI00776346; -.
DR   IPI; IPI00848608; -.
DR   IPI; IPI00851092; -.
DR   RefSeq; NP_001157740.1; NM_001164268.1.
DR   UniGene; Mm.353103; -.
DR   UniGene; Mm.450612; -.
DR   UniGene; Mm.82274; -.
DR   PDB; 1WFW; NMR; -; A=2295-2354.
DR   PDBsum; 1WFW; -.
DR   ProteinModelPortal; A2CG49; -.
DR   SMR; A2CG49; 166-398, 719-977, 1252-1555, 1618-1684, 1890-2219, 2296-2361, 2439-2636, 2649-2943.
DR   IntAct; A2CG49; 4.
DR   STRING; A2CG49; -.
DR   PhosphoSite; A2CG49; -.
DR   PRIDE; A2CG49; -.
DR   Ensembl; ENSMUST00000023522; ENSMUSP00000023522; ENSMUSG00000061751.
DR   Ensembl; ENSMUST00000076810; ENSMUSP00000076088; ENSMUSG00000061751.
DR   Ensembl; ENSMUST00000089655; ENSMUSP00000087084; ENSMUSG00000061751.
DR   Ensembl; ENSMUST00000114953; ENSMUSP00000110603; ENSMUSG00000061751.
DR   Ensembl; ENSMUST00000114954; ENSMUSP00000110604; ENSMUSG00000061751.
DR   Ensembl; ENSMUST00000114960; ENSMUSP00000110611; ENSMUSG00000061751.
DR   GeneID; 545156; -.
DR   KEGG; mmu:545156; -.
DR   UCSC; uc007zar.2; mouse.
DR   UCSC; uc007zas.1; mouse.
DR   UCSC; uc007zat.1; mouse.
DR   UCSC; uc007zav.1; mouse.
DR   UCSC; uc007zax.2; mouse.
DR   UCSC; uc012aew.1; mouse.
DR   CTD; 8997; -.
DR   MGI; MGI:2685385; Kalrn.
DR   GeneTree; ENSGT00560000076675; -.
DR   OrthoDB; EOG4H462T; -.
DR   Bgee; A2CG49; -.
DR   CleanEx; MM_KALRN; -.
DR   Genevestigator; A2CG49; -.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
DR   InterPro; IPR001251; CRAL-bd_TRIO_C.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR003961; FN_III.
DR   InterPro; IPR007110; Ig-like.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR001849; Pleckstrin_homology.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_kinase_dom.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR018159; Spectrin/alpha-actinin.
DR   InterPro; IPR002017; Spectrin_repeat.
DR   Gene3D; G3DSA:3.40.525.10; CRAL_bd_TRIO_C; 1.
DR   Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 2.
DR   Gene3D; G3DSA:2.30.29.30; PH_type; 2.
DR   Gene3D; G3DSA:1.20.900.10; RhoGEF; 2.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00621; RhoGEF; 2.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF00435; Spectrin; 4.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00325; RhoGEF; 2.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00516; SEC14; 1.
DR   SMART; SM00326; SH3; 2.
DR   SMART; SM00150; SPEC; 7.
DR   SUPFAM; SSF52087; CRAL_TRIO_C; 1.
DR   SUPFAM; SSF48065; DH-domain; 2.
DR   SUPFAM; SSF49265; FN_III-like; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   SUPFAM; SSF50044; SH3; 2.
DR   PROSITE; PS50191; CRAL_TRIO; 1.
DR   PROSITE; PS50010; DH_2; 2.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   HOGENOMDNA; MOUSE16.PE822; -.
KW   ENSMUSG000000617515old_1320000031; ENSMUSP000001106111old_1320000031;
KW   D3Z559_MOUSE; Q6PD97_MOUSE; AC154524; AC154588; AC155257; AC165079;
KW   AK081504; AK088732; AK139581; AK158544; AK159031; BC058850; BC157950;
KW   CT010573;
KW   3D-structure; Alternative initiation; Alternative splicing;
KW   ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Disulfide bond;
KW   Guanine-nucleotide releasing factor; Immunoglobulin domain; Kinase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Repeat; Serine/threonine-protein kinase;
KW   SH3 domain; Transferase.
SQ   SEQUENCE   1654 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTDRFWDQWY LWYLRLLRLL DRGSFRNDGL KASDVLPILK EKVAFVSGGR DKRGGPILTF
     PARSNHDRIR QEDLRKLVTY LASVPSEDVC KRGFTVIIDM RGSKWDLIKP LLKTLQEAFP
     AEIHVALIIK PDNFWQKQKT NFGSSKFIFE TSMVSVEGLT KLVDPSQLTE EFDGSLDYNH
     EEWIELRLSL EEFFNSAVHL LSRLEDLQEM LARKEFPVDV EGSRRLIDEH TQLKKKVLKA
     PVEELDREGQ RLLQCIRCSD GFSGRNCIPG SADFQSLVPK ITSLLDKLHS TRQHLHQMWH
     VRKLKLDQCF QLRLFEQDAE KMFDWISHNK ELFLQSHTEI GVSYQHALDL QTQHNHFAMN
     SMNAYVNINR IMSVASRLSE AGHYASQQIK QISTQLDQEW KSFAAALDER STILAMSAVF
     HQKAEQFLSG VDAWCKMCSE GGLPSEMQDL ELAIHHHQSL YEQVTQAYTE VSQDGKALLD
     VLQRPLSPGN SESLTATANY SKAVHQVLDV VHEVLHHQRR LESIWQHRKV RLHQRLQLCV
     FQQDVQQVLD WIENHGEAFL SKHTGVGKSL HRARALQKRH DDFEEVAQNT YTNADKLLEA
     AEQLAQTGEC DPEEIYKAAR HLEVRIQDFV RRVEQRKLLL DMSVSFHTHT KELWTWMEDL
     QKEVLEDVCA DSVDAVQELI KQFQQQQTAT LDATLNVIKE GEDLIQQLRS APPSLGEPTE
     ARDSAMSNNK TPHSSSISHI ESVLQQLDDA QVQMEELFHE RKIKLDIFLQ LRIFEQYTIE
     VTAELDAWNE DLLRQMNDFN TEDLTLAEQR LQRHTERKLA MNNMTFEVIQ QGQDLHQYIM
     EVQASGIELI CEKDLDLAAQ VQELLEFLHE KQHELELNAE QTHKRLEQCL QLRHLQAEVK
     QVLGWIRNGE SMLNASLVNA SSLSEAEQLQ REHEQFQLAI EKTHQSALQV QQKAEALLQA
     GHYDADAIRE CAEKVALHWQ QLMLKMEDRL KLVNASVAFY KTSEQVCSVL ESLEQEYRRD
     EDWCGGRDKL GPAAEMDHVI PLLSKHLEQK EAFLKACTLA RRNAEVFLKY IHRNNVSMPS
     VASHTRGPEQ QVKAILSELL QRENRVLHFW TLKKRRLDQC QQYVVFERSA KQALDWIQET
     GEYYLSTHTS TGETTEETQE LLKEYGEFRV PAKQTKEKVK LLIQLADSFV EKGHIHATEI
     RKWVTTVDKH YRDFSLRMGK YRYSLEKALG VNTEDNKDLE LDIIPASLSD REVKLRDANH
     EINEEKRKSA RKKEFIMAEL LQTEKAYVRD LHECLETYLW EMTSGVEEIP PGILNKEHII
     FGNIQEIYDF HNNIFLKELE KYEQLPEDVG HCFVTWADKF QMYVTYCKNK PDSNQLILEH
     AGTFFDEIQQ RHGLANSISS YLIKPVQRVT KYQLLLKELL TCCEEGKGEL KDGLEVMLSV
     PKKANDAMHV SMLEGFDENL DVQGELILQD AFQVWDPKSL IRKGRERHLF LFEISLVFSK
     EIKDSSGHTK YVYKNKLLTS ELGVTEHVEG DPCKFALWSG RTPSSDNKTV LKASNIETKQ
     EWIKNIREVI QERIIHLKGA LKEPIQLPKT PAKLRNNSKR DGVEDGDSQG DGSSQPDTIS
     IASRTSQNTV ESDKDGNLVP RWHLGPGDPF STYV
//

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