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Database: UniProt
Entry: A0A1V4K5Q7_PATFA
LinkDB: A0A1V4K5Q7_PATFA
Original site: A0A1V4K5Q7_PATFA 
ID   A0A1V4K5Q7_PATFA        Unreviewed;      1287 AA.
AC   A0A1V4K5Q7;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   08-OCT-2025, entry version 36.
DE   SubName: Full=Kalirin isoform A {ECO:0000313|EMBL:OPJ79809.1};
GN   Name=KALRN {ECO:0000313|EMBL:OPJ79809.1};
GN   ORFNames=AV530_002282 {ECO:0000313|EMBL:OPJ79809.1};
OS   Patagioenas fasciata monilis.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Neoaves; Columbimorphae; Columbiformes;
OC   Columbidae; Patagioenas.
OX   NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ79809.1, ECO:0000313|Proteomes:UP000190648};
RN   [1] {ECO:0000313|EMBL:OPJ79809.1, ECO:0000313|Proteomes:UP000190648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ79809.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:OPJ79809.1};
RA   Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA   Shapiro B.;
RT   "Band-tailed pigeon sequencing and assembly.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OPJ79809.1}.
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DR   EMBL; LSYS01004331; OPJ79809.1; -; Genomic_DNA.
DR   OrthoDB; 10256089at2759; -.
DR   Proteomes; UP000190648; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019898; C:extrinsic component of membrane; IEA:TreeGrafter.
DR   GO; GO:0014069; C:postsynaptic density; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0007411; P:axon guidance; IEA:TreeGrafter.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:TreeGrafter.
DR   CDD; cd00063; FN3; 1.
DR   CDD; cd13241; PH2_Kalirin_Trio_p63RhoGEF; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   CDD; cd11853; SH3_Kalirin_2; 1.
DR   CDD; cd14115; STKc_Kalirin_C; 1.
DR   FunFam; 1.10.510.10:FF:000152; kalirin isoform X1; 1.
DR   FunFam; 2.30.29.30:FF:000091; kalirin isoform X1; 1.
DR   FunFam; 2.30.30.40:FF:000038; kalirin isoform X1; 1.
DR   FunFam; 2.60.40.10:FF:000325; kalirin isoform X1; 1.
DR   FunFam; 2.60.40.10:FF:000368; kalirin isoform X1; 1.
DR   FunFam; 1.20.900.10:FF:000008; rho guanine nucleotide exchange factor 25; 1.
DR   Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH_dom.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR047053; Kalirin_TRIO_SH3_2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR051336; RhoGEF_Guanine_NuclExch_SF.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR055251; SOS1_NGEF_PH.
DR   PANTHER; PTHR22826:SF49; KALIRIN; 1.
DR   PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF07679; I-set; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   Pfam; PF16609; SH3-RhoG_link; 1.
DR   Pfam; PF23587; SH3_KALRN; 1.
DR   Pfam; PF22697; SOS1_NGEF_PH; 1.
DR   PRINTS; PR00014; FNTYPEIII.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00325; RhoGEF; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW   Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          232..407
FT                   /note="DH"
FT                   /evidence="ECO:0000259|PROSITE:PS50010"
FT   DOMAIN          419..529
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          623..688
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          772..865
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          872..966
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   DOMAIN          985..1239
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          36..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          546..619
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          710..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..130
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..168
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..604
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..616
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        744..754
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1014
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1287 AA;  144472 MW;  659DDBE70A22312E CRC64;
     MKAGRRGYPA RSGVGWLLAK CCCCCSCKDA YSVSSNDNGG KSDSVANLQP QPSLNSIQSS
     PGPKRSTNTL KKWLTSPVRR LNSGKTESNI KKQKKVRDGR KSFDLGSPKT GDETTPQGDS
     ADEKSKKGWG EDEPDEESHT PLPPPMKIFD NDPTQDEMSS SLLAARQSSS DVPTAADLVS
     AIEQLVKSKL TLEGGSYRGS LKDATGCLNE GMTPSTPPRN LEEEQKAKAM RGRMFVLNEL
     VQTEKDYVKD LGTVVEGFMK RIEEKGVSED MKGKDKIVFG NIHQIYDWHK DFFLAELEKC
     LQEPDRLAQL FIKHERRLHM YVVYCQNKPR SEYIVAEYEA YFEEVQQEIS QRLTISDFLI
     KPIQRITKYQ LLLKDFLRYS EKAGLECSDI EKAVELMCLV PKRCNDMMNL GRLQGFEGKL
     TAQGKLLQQD TFYVTEQDSG VQSRPKERRV FLFEQIVIFS ELLRKGSLTP GYMFKKSIKM
     NYLIIEENVD NDPCKFALMS RETSERVILQ AANPEIQQAW VQDINQVLDT QRDFLNALQS
     PIEYQRKESS SAVLRPQTGR VPQPNSRPYS SVPVESEKPL KATSRNPSLP PLKISTSNGS
     TGYEHSQPGD KYEQSKTDLG GCNGTSSMVV IKDYYALKED EICVNQGEVV QILAINQQNM
     FLVYQPANDH SPAAEGWIPG NILAPLTKST TDNSDGSIKK SCSWHTLRMR KRAEKESSGK
     NEANGPRKSK DILGNKVSVK ETNSSEESEC DDLDPNTSME IINPNFIQEV APEFLVPLVD
     ITCLLGDTVM LQCKVCGRPK PTITWKGPDQ NILDNDNSTA TYTVSSCDSG ELTLKICNLM
     PQDSGIYTCV ATNEHGTAST SATIKVQGVP AAPNRPIAQE RSCTSVILRW LPPSSTGNCT
     ISGYTVEYRE EGSQVWQQSV ASTLDTYLVI EDLSPGCQYQ FRVSASNPWG ISLPSDPSEF
     VRLPEYDSAA DGATISWKEN FDLAYVELHE IGRGRFSIVK KCIHKATRKD VAVKFISKKM
     KKKEQAAHEA ALLQHLQHPQ YITIHDTYES PTSYILVLEL MDDGRLLDYL MNHDELMEEK
     VAFYIRDTME ALQYLHNCRV AHLDIKPENL LIDLRIPVPR VKIIDLEDAV QITGHYHVHH
     LLGNPEFAAP EVIQGLPVSL STDIWSIGVL TYVMLSGVSP FLDESREETC INVCRVDFSF
     PPEYFSDVSH AARDFINVIL QEDSRRRPTA ATCLQHPWLQ PHNGSYSKIP LDTSRLASFI
     ERRRHQYDVH PVPSVKSFLM SRLAPGT
//
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