ID A0A2U3VBS3_ODORO Unreviewed; 2987 AA.
AC A0A2U3VBS3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=KALRN {ECO:0000313|RefSeq:XP_004391977.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004391977.1};
RN [1] {ECO:0000313|RefSeq:XP_004391977.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001433};
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:0000256|ARBA:ARBA00000775};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
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DR RefSeq; XP_004391977.1; XM_004391920.1.
DR STRING; 9708.A0A2U3VBS3; -.
DR GeneID; 101377538; -.
DR KEGG; oro:101377538; -.
DR CTD; 8997; -.
DR InParanoid; A0A2U3VBS3; -.
DR OrthoDB; 2906033at2759; -.
DR Proteomes; UP000245340; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR CDD; cd13240; PH1_Kalirin_Trio_like; 1.
DR CDD; cd13241; PH2_Kalirin_Trio_p63RhoGEF; 1.
DR CDD; cd00160; RhoGEF; 2.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd11852; SH3_Kalirin_1; 1.
DR CDD; cd11853; SH3_Kalirin_2; 1.
DR CDD; cd00176; SPEC; 4.
DR CDD; cd14115; STKc_Kalirin_C; 1.
DR Gene3D; 1.20.58.60; -; 5.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
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; IPR047054; Kalirin_TRIO_PH_1.
DR InterPro; IPR028570; Kalirin_TRIO_SH3_1.
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; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR22826:SF49; KALIRIN; 1.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00621; RhoGEF; 2.
DR Pfam; PF16609; SH3-RhoG_link; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00435; Spectrin; 4.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00409; IG; 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 domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR SUPFAM; SSF46966; Spectrin repeat; 6.
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; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000245340};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 35..180
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1281..1456
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1468..1580
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1646..1711
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1929..2104
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2116..2226
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2321..2386
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2472..2565
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2572..2666
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2685..2939
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 710..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1594..1642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1730..1857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2243..2317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2411..2455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 919..946
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 721..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1617..1642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1730..1773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1782..1804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1813..1837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2243..2278
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2286..2300
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2411..2435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2714
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2987 AA; 340142 MW; 5CE8E7B4E9BD1BDF 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
QKEMLEDVCA DSVDAVQELI KQFQQQQTAT LDATLNVIKE GEDLIQQLRS APPSLGEPSE
ARDSAVSNNK TPHSSSISHI ESVLQQLDDA QVQMEELFHE RKIKLDIFLQ LRIFEQYTIE
VTAELDAWNE DLLRQMNDFN TEDLTLAEQR LQRHTERKLA MNNMTFEVIQ QGQDLHQYIM
EVQASGIELI CEKDIDLAAQ VQELLEFLHE KQHELELNAE QTHKRLEQCL QLRHLQAEVK
QVLGWIRNGE SMLNASLVNA SSLSEAEQLQ REHEQFQLAI ESLFHATSLQ KTHQSALQVQ
QKAEALLQAG HYDADAIREC AEKVALHWQQ LMLKMEDRLK LVNASVAFYK TSEQVCSVLE
SLEQEYRRDE DWCGGRDKLG PAAEIDHVIP LISKHLEQKE AFLKACTLAR RNAEVFLKYI
HRNNVSMPSA AGHTRGPEQQ VKAILSELLQ RENRVLHFWT LKKRRLDQCQ QYVVFERSAK
QALDWIQETG EYYLSTHTST GETTEETQEL LKEYGEFRVP AKQTKEKVKL LIQLADSFVE
KGHIHATEIR KWVTTVDKHY RDFSLRMGKY RYSLEKALGV NTEDNKDLEL DIIPASLSDR
EVKLRDANHE VNEEKRKSAR KKEFIMAELL QTEKAYVRDL HECLETYLWE MTSGVEEIPP
GILNKEHIIF GNIQEIYDFH NNIFLKELEK YEQLPEDVGH CFVTWADKFQ MYVTYCKNKP
DSNQLILEHA GTFFDEIQQR HGLANSISSY LIKPVQRITK YQLLLKELLT CCEEGKGELK
DGLEVMLSVP KKANDAMHVS MLEGFDENLD VQGELILQDA FQVWDPKSLI RKGRERHLFL
FEISLVFSKE IKDSSGHTKY VYKNKLLTSE LGVTEHVEGD PCKFALWSGR TPSSDNKTVL
KASNIETKQE WIKNIREVIQ ERIIHLKGAL KEPIQLPKTP AKQRNNSKRD GVEDVDSQGD
GSSQPDTISI ASRTSQNTVD SDKLSGGCEL TVVLQDFNAG HSSELTIQVG QTVELLERPS
ERPGWCLVRT TERSPPQEGL VPSSALCISH SRSSVEMDCF FPLVKDAYSH SSSENGGKSE
SVANLQSQPS LNSIHSSPGP KRSTNTLKKW LTSPVRRLNS GKADGNIKKQ KKVRDGRKSF
DLGSPKPGDE TTPQGDSADE KNKKGWGEDE PDEESHTPLP PPMKIFDNDP TQDEMSSSLL
AARQASTEVP SAADLVSAIE QLVKSKLSLE GGSYRGSLKD PVGCLNEGMT PPTPPRNLEE
EQKAKALRGR MFVLNELVQT EKDYVKDLGI VVEGFMKRIE EKGVPEDMRG KDKIVFGNIH
QIYDWHKDFF LAELEKCIQE QDRLAQLFIK HERKLHIYVW YCQNKPRSEY IVAEYDAYFE
EVKQEINQRL TLSDFLIKPI QRITKYQLLL KDFLRYSEKA GLECSDIEKA VELMCLVPKR
CNDMMNLGRL QGFEGTLTAQ GKLLQQDTFY VIELDAGMQS RTKERRVFLF EQIVIFSELL
RKGSLTPGYM FKRSIKMNYL VLEENVDNDP CKFALMNRET SERVILQAAN ADIQQAWVQD
INQVLETQRD FLNALQSPIE YQRKERSTAV MRSQPSRVPQ ASPRPYSSVP TGSEKPPKGS
SYNPPLPPLK ISTSNGSPGF DYHQPGDKFE ASKQGDLGGC NGTSSMAVIK DYYALKENEI
CVSQGEVVQV LAVNQQNMCL VYQPASDRSP AAEGWVPGSV LAPLPKATAA AENSDGSIKK
SCSWHTLRMR KRAEVENTGK NEATGPRKPK DILGNKVSVK ETNSSEESEC DDLDPNTSME
ILNPNFIQEV APEFLVPLVD VTCLLGDTVT LQCKVCGRPK PTITWKGPDQ NVLDMDNSSA
TSTVSSCDSG EITLKICNLM PQDSGIYTCI ATNDHGTAST SATVKVQGVP AAPNRPIAQE
RSCTSVILRW LPPSSTGNCT ISGYTVEYRE EGSQAWQQSV ASTLDTYLVV EDLSPGSPYQ
FRVSASNPWG ISLPSEPSEF VRLPEYDAAA DGATISWKEN FDSAYTELNE IGRGRFSIVK
KCIHKATRKD VAVKFVSKKM KKKEQAAHEA ALLQHLQHPQ YITLHDTYES PTSYILILEL
MDDGRLLDYL MNHDELMEEK VAFYIRDIME ALQYLHNCRV AHLDIKPENL LIDLRIPVPR
VKLIDLEDAV QISGHFHIHH LLGNPEFAAP EVIQGIPVSL GTDIWSIGVL TYVMLSGVSP
FLDESKEETC INVCRVDFSF PHEYFCGVSN AARDFINVIL QEDFRRRPTA ATCLQHPWLQ
PHNGSYSKIP LDTSRLACFI ERRKHQNDVR PVPNVKSYIV NRVNQGT
//
