(data stored in ACNUC5448 zone)

HOGENOM: MOUSE16_PE816

ID   MOUSE16_PE816                        STANDARD;      PRT;   2964 AA.
AC   MOUSE16_PE816;
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.PE816).
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.PE816.
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;ENSMUST00000076810;ENSMUSP00000076088.
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; 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.PE816; -.
KW   ENSMUSG000000617515old_1320000031; ENSMUSP000000760881old_1320000031;
KW   AC154524; AC154588; AC155257; AC165079; AK008844; AK081504; AK088732;
KW   AK158544; AK159031; BC157950; BC172101; 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   2964 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVLSGSFRND GLKASDVLPI LKEKVAFVSG GRDKRGGPIL TFPARSNHDR IRQEDLRKLV
     TYLASVPSED VCKRGFTVII DMRGSKWDLI KPLLKTLQEA FPAEIHVALI IKPDNFWQKQ
     KTNFGSSKFI FETSMVSVEG LTKLVDPSQL TEEFDGSLDY NHEEWIELRL SLEEFFNSAV
     HLLSRLEDLQ EMLARKEFPV DVEGSRRLID EHTQLKKKVL KAPVEELDRE GQRLLQCIRC
     SDGFSGRNCI PGSADFQSLV PKITSLLDKL HSTRQHLHQM WHVRKLKLDQ CFQLRLFEQD
     AEKMFDWISH NKELFLQSHT EIGVSYQHAL DLQTQHNHFA MNSMNAYVNI NRIMSVASRL
     SEAGHYASQQ IKQISTQLDQ EWKSFAAALD ERSTILAMSA VFHQKAEQFL SGVDAWCKMC
     SEGGLPSEMQ DLELAIHHHQ SLYEQVTQAY TEVSQDGKAL LDVLQRPLSP GNSESLTATA
     NYSKAVHQVL DVVHEVLHHQ RRLESIWQHR KVRLHQRLQL CVFQQDVQQV LDWIENHGEA
     FLSKHTGVGK SLHRARALQK RHDDFEEVAQ NTYTNADKLL EAAEQLAQTG ECDPEEIYKA
     ARHLEVRIQD FVRRVEQRKL LLDMSVSFHT HTKELWTWME DLQKEVLEDV CADSVDAVQE
     LIKQFQQQQT ATLDATLNVI KEGEDLIQQL RSAPPSLGEP TEARDSAMSN NKTPHSSSIS
     HIESVLQQLD DAQVQMEELF HERKIKLDIF LQLRIFEQYT IEVTAELDAW NEDLLRQMND
     FNTEDLTLAE QRLQRHTERK LAMNNMTFEV IQQGQDLHQY IMEVQASGIE LICEKDLDLA
     AQVQELLEFL HEKQHELELN AEQTHKRLEQ CLQLRHLQAE VKQVLGWIRN GESMLNASLV
     NASSLSEAEQ LQREHEQFQL AIEKTHQSAL QVQQKAEALL QAGHYDADAI RECAEKVALH
     WQQLMLKMED RLKLVNASVA FYKTSEQVCS VLESLEQEYR RDEDWCGGRD KLGPAAEMDH
     VIPLLSKHLE QKEAFLKACT LARRNAEVFL KYIHRNNVSM PSVASHTRGP EQQVKAILSE
     LLQRENRVLH FWTLKKRRLD QCQQYVVFER SAKQALDWIQ ETGEYYLSTH TSTGETTEET
     QELLKEYGEF RVPAKQTKEK VKLLIQLADS FVEKGHIHAT EIRKWVTTVD KHYRDFSLRM
     GKYRYSLEKA LGVNTEDNKD LELDIIPASL SDREVKLRDA NHEINEEKRK SARKKEFIMA
     ELLQTEKAYV RDLHECLETY LWEMTSGVEE IPPGILNKEH IIFGNIQEIY DFHNNIFLKE
     LEKYEQLPED VGHCFVTWAD KFQMYVTYCK NKPDSNQLIL EHAGTFFDEI QQRHGLANSI
     SSYLIKPVQR VTKYQLLLKE LLTCCEEGKG ELKDGLEVML SVPKKANDAM HVSMLEGFDE
     NLDVQGELIL QDAFQVWDPK SLIRKGRERH LFLFEISLVF SKEIKDSSGH TKYVYKNKLL
     TSELGVTEHV EGDPCKFALW SGRTPSSDNK TVLKASNIET KQEWIKNIRE VIQERIIHLK
     GALKEPIQLP KTPAKLRNNS KRDGVEDGDS QGDGSSQPDT ISIASRTSQN TVESDKLSGG
     CELTVVLQDF SAGHSSELSI QVGQTVELLE RPSERPGWCL VRTTERSPPQ EGLVPSSALC
     ISHSRSSVEM DCFFPLKDSY SHSSSENGGK SESVAHLQSQ PSLNSIHSSP GPKRSTNTLK
     KWLTSPVRRL NSGKADGNIK KQKKVRDGRK SFDLGSPKPG DETTPQGDSA DEKSKKGWGE
     DEPDEESHTP LPPPMKIFDN DPTQDEMSSL LAARQAPPDV PTAADLVSAI EKLVKNKLTL
     EGGSYRGSLK DPTGCLNEGM TPPTPPRNLE EEQKAKALRG RMFVLNELVQ TEKDYVKDLG
     IVVEGFMKRI EEKGVPEDMR GKEKIVFGNI HQIYDWHKDF FLAELEKCIQ EQDRLAQLFI
     KHERKLHIYV WYCQNKPRSE YIVAEYDAYF EEVKQEINQR LTLSDFLIKP IQRITKYQLL
     LKDFLRYSEK AGLECSDIEK AVELMCLVPK RCNDMMNLGR LQGFEGTLTA QGKLLQQDTF
     YVIELDAGMQ SRTKERRVFL FEQIVIFSEL LRKGSLTPGY MFKRSIKMNY LVLEDNVDGD
     PCKFALMNRE TSERVILQAA NSDIQQAWVQ DINQVLETQR DFLNALQSPI EYQRKERSTA
     VIRSQPPRVP QASPRPYSSG PVGSEKPPKG SSYNPPLPPL KISTSNGSPG FDYHQPGDKF
     DASKQNDLGG CNGTSTMTVI KDYYALKENE ICVSQGEVVQ VLAVNQQNMC LVYQPASDHS
     PAAEGWVPGS ILAPLAKATA AAESSDGSIK KSCSWHTLRM RKRADVENSG KNEATGPRKP
     KDILGNKVSV KETNSSEESE CDDLDPNTSM EILNPNFIQE VAPEFLVPLV DVTCLLGDTV
     LLQCKACGRP KPSITWKGPD QNILDTDNSS ATYTISSCDS GESTLKICNL MPQDSGIYTC
     IAANDHGTAS TSATVKVQGV PAAPNRPIAQ ERSCTSVILR WLPPASTGNC TISGYTVEYR
     EEGSQVWQQS VASTLDTYLV IEDLSPGCPY QFRVSASNPW GISLPSEPSE FVRLPEYDAA
     ADGATISWKE NFDSAYTELN EIGRGRFSIV KKCIHKATRK DVAVKFVSKK MKKKEQAAHE
     AALLQHLQHP QYVTLHDTYE SPTSYILILE LMDDGRLLDY LMNHDELMEE KVAFYIRDIM
     EALQYLHNCR VAHLDIKPEN LLIDLRIPVP RVKLIDLEDA VQISGHFHIH HLLGNPEFAA
     PEVIQGIPVS LGTDIWSIGV LTYVMLSGVS PFLDESKEET CINVCRVDFS FPHEYFCGVS
     NAARDFINVI LQEDFRRRPT AATCLQHPWL QPHNGSYSKI PLDTSRLACF IERRKHQNDV
     RPIPNVKSYI VNRVNQGTSL SHNP
//

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