(data stored in ACNUC5448 zone)

HOGENOM: RAT11_PE528

ID   RAT11_PE528                          STANDARD;      PRT;   2948 AA.
AC   RAT11_PE528;
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   Flags: Fragments;
DE   RecName: Full=Kalirin; EC=2.7.11 1;AltName: Full=Huntingtin-associated
DE   protein-interacting protein;AltName: Full=PAM COOH-terminal interactor
DE   protein 10; Short=P-CIP10;AltName: Full=Protein Duo;AltName:
DE   Full=Serine/threonine-protein kinase with Dbl- and pleckstrin homology
DE   domain; (RAT11.PE528).
GN   Name=Kalrn; Synonyms=Duo, Hapip;
OS   RATTUS NORVEGICUS.
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; Rattus.
OX   NCBI_TaxID=10116;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS RAT11.PE528.
CC       Rattus norvegicus chromosome 11 RGSC3.4  sequence 1..87759784
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:KALRN_RAT
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. Isoforms 1 and 7 are
CC       necessary for neuronal development and axonal outgrowth. Isoform 6
CC       is required for dendritic spine formation.
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. Cytoplasm, cytoskeleton.
CC       Note=Isoform 6 is largely associated with synaptosomal membranes
CC       and to punctate structures in cortical neurons. Isoforms 1 and 7
CC       are expressed in neuronal cell bodies, isoform 7 is also found in
CC       neuronal processes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing, Alternative initiation; Named isoforms=8;
CC       Name=1; Synonyms=Kalirin-12A;
CC         IsoId=P97924-1; Sequence=Displayed;
CC         Note=Produced by alternative splicing;
CC       Name=2; Synonyms=Kalirin-8B, P-CIP10B;
CC         IsoId=P97924-2; Sequence=VSP_028891, VSP_028899, VSP_028900;
CC         Note=Produced by alternative splicing;
CC       Name=3; Synonyms=Kalirin-8A, P-CIP10A;
CC         IsoId=P97924-3; Sequence=VSP_028899, VSP_028900;
CC         Note=Produced by alternative splicing;
CC       Name=4;
CC         IsoId=P97924-4; Sequence=VSP_028896;
CC         Note=Produced by alternative splicing;
CC       Name=5; Synonyms=Delta Kalirin-7;
CC         IsoId=P97924-5; Sequence=VSP_028893, VSP_028897, VSP_028898;
CC         Note=Produced by alternative initiation at Met-624 of isoform 6;
CC       Name=6; Synonyms=Kalirin-7, HAPIP;
CC         IsoId=P97924-6; Sequence=VSP_028892, VSP_028897, VSP_028898;
CC         Note=Produced by alternative splicing;
CC       Name=7; Synonyms=Kalirin-9A;
CC         IsoId=P97924-7; Sequence=VSP_028901, VSP_028902;
CC         Note=Produced by alternative splicing;
CC       Name=8;
CC         IsoId=P97924-8; Sequence=VSP_028894, VSP_028895;
CC         Note=Produced by alternative splicing;
CC   -!- TISSUE SPECIFICITY: Highly expressed in the brain and nervous
CC       system. Isoform 6 is highly enriched in the postsynaptic density
CC       fraction of the cerebral cortex.
CC   -!- DEVELOPMENTAL STAGE: Isoforms 1 and 7 are prevelant 2 dpp, isoform
CC       6 is not detectable until 2 weeks after birth.
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.
CC   -!- PTM: Autophosphorylated (By similarity).
CC   -!- MISCELLANEOUS: Called DUO because the encoded protein is closely
CC       related to but shorter than TRIO.
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:Rattus_norvegicus;ENSRNOG00000001706;ENSRNOT00000064066;ENSRNOP00000062745.
DR   EMBL; AF229255; - ;
DR   EMBL; AF230644; - ;
DR   EMBL; AF232668; - ;
DR   EMBL; AF232669; - ;
DR   EMBL; AY621095; - ;
DR   EMBL; U88156; - ;
DR   EMBL; U88157; - ;
DR   EMBL; U94189; - ;
DR   UniProtKB/Swiss-Prot; P97924; O70135; Q6IV51; Q9JIF1; Q9JIF2; Q9JIG0; Q9JIH3; -.
DR   EMBL; U88156; AAB66366.1; -; mRNA.
DR   EMBL; U88157; AAB66367.1; -; mRNA.
DR   EMBL; AF230644; AAF69144.1; -; mRNA.
DR   EMBL; AF229255; AAF66014.1; -; mRNA.
DR   EMBL; AF232668; AAF66018.1; -; mRNA.
DR   EMBL; AF232669; AAF66019.1; -; mRNA.
DR   EMBL; AY621095; AAT39517.1; -; mRNA.
DR   EMBL; U94189; AAC15790.1; -; mRNA.
DR   IPI; IPI00200504; -.
DR   IPI; IPI00400488; -.
DR   IPI; IPI00476515; -.
DR   IPI; IPI00567732; -.
DR   IPI; IPI00869510; -.
DR   IPI; IPI00869788; -.
DR   IPI; IPI00870072; -.
DR   IPI; IPI00870649; -.
DR   PIR; T32732; T32732.
DR   PIR; T42098; T42098.
DR   RefSeq; NP_114451.2; NM_032062.2.
DR   UniGene; Rn.87882; -.
DR   PDB; 1U3O; NMR; -; A=1617-1686.
DR   PDB; 2KR9; NMR; -; A=1253-1432.
DR   PDBsum; 1U3O; -.
DR   PDBsum; 2KR9; -.
DR   ProteinModelPortal; P97924; -.
DR   SMR; P97924; 1252-1555, 1618-1684, 1891-2220, 2297-2361.
DR   IntAct; P97924; 2.
DR   STRING; P97924; -.
DR   PhosphoSite; P97924; -.
DR   PRIDE; P97924; -.
DR   GeneID; 84009; -.
DR   KEGG; rno:84009; -.
DR   CTD; 8997; -.
DR   RGD; 621865; Kalrn.
DR   eggNOG; maNOG15047; -.
DR   GeneTree; ENSGT00560000076675; -.
DR   InParanoid; P97924; -.
DR   OrthoDB; EOG4H462T; -.
DR   NextBio; 616533; -.
DR   ArrayExpress; P97924; -.
DR   Genevestigator; P97924; -.
DR   GermOnline; ENSRNOG00000001706; Rattus norvegicus.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0043005; C:neuron projection; IDA:RGD.
DR   GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
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:0007409; P:axonogenesis; IDA:RGD.
DR   GO; GO:0035556; P:intracellular signal transduction; IDA:HGNC.
DR   GO; GO:0050773; P:regulation of dendrite development; IDA:RGD.
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; PS00741; DH_1; FALSE_NEG.
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; RAT11.PE528; -.
KW   ENSRNOG00000001706820036002503210000011;
KW   Kalrn; KALRN_RAT; AF229255; AF230644; AF232668; AF232669; AY621095;
KW   U88157; U94189;
KW   3D-structure; Alternative initiation; Alternative splicing;
KW   ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Disulfide bond; Guanine-nucleotide releasing factor;
KW   Immunoglobulin domain; Kinase; Magnesium; Metal-binding;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; SH3 domain; Transferase.
SQ   SEQUENCE   2948 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     SVADFPDAFL NYPLSFPPGG RDKRGGPILT FPARSNHDRI RQEDLRKLVT YLASVPSEDV
     CKRGFTVIID MRGSKWDLIK PLLKTLQEAF PAEIHVALII KPDNFWQKQK TNFGSSKFIF
     ETSMVSVEGL TKLVDPSQLT EEFDGSLDYN HEEWIELRLS LEEFFNSAVH LLSRLEDLQE
     MLARKEFPVD VEGSRRLIDE HTQLKKKVLK APVEELDREG QRLLQCIRCS DGFSGRNCIP
     GSADFQSLVP KITSLLDKLH STRQHLHQMW HVRKLKLDQC FQLRLFEQDA EKMFDWISHN
     KELFLQSHTE IGVSYQHALD LQTQHNHFAM NSMNAYVNIN RIMSVASRLS EAGHYASQQI
     KQISTQLDQE WKSFAAALDE RSTILAMSAV FHQKAEQFLS GVDAWCKMCS EGGLPSEMQD
     LELAIHHHQS LYEQVTQAYT EVSQDGKALL DVLQRPLSPG NSESLTATAN YSKAVHQVLD
     VVHEVLHHQR RLESIWQHRK VRLHQRLQLC VFQQDVQQVL DWIENHGEAF LSKHTGVGKS
     LHRARALQKR HDDFEEVAQN TYTNADKLLE AAEQLAQTGE CDPEEIYKAA RHLEVRIQDF
     VRRVEQRKLL LDMSVSFHTH TKELWTWMED LQKEVLEDVC ADSVDAVQEL IKQFQQQQTA
     TLDATLNVIK EGEDLIQQLR SAPPSLGEPT EARDSAVSNN KTPHSSSISH IESVLQQLDD
     AQVQMEELFH ERKIKLDIFL QLRIFEQYTI EVTAELDAWN EDLLRQMNDF NTEDLTLAEQ
     RLQRHTERKL AMNNMTFEVI QQGQDLHQYI MEVQASGIEL ICEKDVDLAA QVQELLEFLH
     EKQHELELNA EQTHKRLEQC LQLRHLQAEV KQVLGWIRNG ESMLNASLVN ASSLSEAEQL
     QREHEQFQLA IEKTHQSALQ VQQKAEALLQ AGHYDADAIR ECAEKVALHW QQLMLKMEDR
     LKLVNASVAF YKTSEQVCSV LESLEQEYRR DEDWCGGRDK LGPAAEMDHV IPLLSKHLEQ
     KEAFLKACTL ARRNAEVFLK YIHRNNVSMP SVASHTRGPE QQVKAILSEL LQRENRVLHF
     WTLKKRRLDQ CQQYVVFERS AKQALDWIQE TGEYYLSTHT STGETTEETQ ELLKEYGEFR
     VPAKQTKEKV KLLIQLADSF VEKGHIHATE IRKWVTTVDK HYRDFSLRMG KYRYTLEKAL
     GVNTEDNKDL ELDIIPASLS DREVKLRDAN HEVNEEKRKS ARKKEFIMAE LLQTEKAYVR
     DLHECLETYL WEMTSGVEEI PPGILNKEHI IFGNIQEIYD FHNNIFLKEL EKYEQLPEDV
     GHCFVTWADK FQMYVTYCKN KPDSNQLILE HAGTFFDEIQ QRHGLANSIS SYLIKPVQRV
     TKYQLLLKEL LTCCEEGKGE LKDGLEVMLS VPKKANDAMH VSMLEGFDEN LDVQGELILQ
     DAFQVWDPKS LIRKGRERHL FLFEISLVFS KEIKDSSGHT KYVYKNKLLT SELGVTEHVE
     GDPCKFALWS GRTPSSDNKT VLKASNIETK QEWIKNIREV IQERIIHLKG ALKEPIQLPK
     TPAKLRNNSK RDGVEDGDSQ GDGSSQPDTI SIASRTSQNT VESDKLSGGC ELTVVLQDFS
     AAHSSELSIQ VGQTVELLER PSERPGWCLV RTTERSPPQE GLVPSSTLCI SHSRSSVEMD
     CFFPLVKDSY SHSSGENGGK SESVANLQSQ PSLNSIHSSP GPKRSTNTLK KWLTSPVRRL
     NSGKADGNIK KQKKVRDGRK SFDLGSPKPG DETTPQGDSA DEKSKKGWGE DEPDEESHTP
     LPPPMKIFDN DPTQDEMSSL LAARQAPTDV PTAADLVSAI EKLVKSKLTL EGGSYRGSLK
     DPTVCLNEGM APPTPPRNLE 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 LVLEEDVDDD PCKFALMNRE
     TSERVILQAA NPDIQQAWVQ DINQVLETQR DFLNALQSPI EYQRKERSTA VIRSQPPRVP
     QASPRPYSSV PVGSEKPPKG SSYNPPLPPL KISTSNGSPG FDYHQPGDKF DASKQNDLGG
     CNGTSTMAVI KDYYALKENE ICVSQGEVVQ VLAVNQQNMC LVYQPASDHS PAAEGWVPGS
     ILAPLTKATA PAESSDESIK KSCSWHTLRM RKRADVENTG KNEATGPRKP KDILGNKASV
     KETNSSEESE CDDLDPNTSM EILNPNFIQE VAPEFLVPLV DVTCLLGDTV LLQCKACGRP
     KPTITWKGPD QNILDTDNSS ATYTISSCDS GESTLKICNL MPQDSGIYTC IATNDHGTAS
     TSATVKVQGV PAAPNRPIAQ ERSCTSVILR WLPPASTGNC TISGYTVEYR EEGSQVWQQS
     VASTLDTYLV IEDLSPGCPY QFRVSASNPW GISLPSEPSE FVHLPEYDAA 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
     VNRVNQGT
//

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