ID A0A2Y9N1I9_DELLE Unreviewed; 2398 AA.
AC A0A2Y9N1I9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Kalirin isoform X16 {ECO:0000313|RefSeq:XP_022423153.1};
GN Name=KALRN {ECO:0000313|RefSeq:XP_022423153.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022423153.1};
RN [1] {ECO:0000313|RefSeq:XP_022423153.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022423153.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR RefSeq; XP_022423153.1; XM_022567445.1.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
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 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; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
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; IPR047054; Kalirin_TRIO_PH_1.
DR InterPro; IPR028570; Kalirin_TRIO_SH3_1.
DR InterPro; IPR047053; Kalirin_TRIO_SH3_2.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
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; PF00169; PH; 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; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 2.
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; SSF50729; PH domain-like; 2.
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; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS50002; SH3; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 37..182
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1283..1458
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1470..1582
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1648..1713
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 2320..2385
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 712..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1596..1644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1751..1857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1898..1917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2245..2295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 860..887
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 921..948
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 723..740
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1619..1644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1751..1774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1783..1805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1814..1837
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2398 AA; 273316 MW; 466DB93C19FF42B4 CRC64;
MNPPEGAAEE GGAADSDVDA FFRTGSFRND 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
DLQKEMLEDV CADSVDAVQE LIKQFQQQQT ATLDATLNVI KEGEDLIQQL RSAPPSLGEP
SEARDSAVSS NKTPHSSSIS HIESVLQQLD DAQVQMEELF HERKIKLDIF LQLRIFEQYT
IEVTAELDAW NEDLLRQMND FNTEDLTLAE QRLQRHTERK LAMNNMTFEV IQQGQDLHQY
IMEVQASGIE LICEKDIDLA AQVQELLEFL QEKQHELELN AEQTHERLEQ CLQLRHLQAE
VRQVLGWIRN GESMLNASLV NASSLSEAEQ LQREHEQFQL AIESLFHATS LQKTHQSALQ
VQQKAEALLQ AGHYDADAIR ECAEKVALHW QQLMLKMEDR LKLVNASVAF YKTSEQVCSV
LESLEQEYRR DEDWCGGRDK LGPAAEIDHV IPLISKHLEQ KEAFLKACTL ARRNAEVFLK
YIHRNNVSMP SAASHTRGPE QQVKAILSEL LQRENRVLHF WTLKKRRLDQ CQQYVVFERS
AKQALDWIQE TGEYYLSTHT SPGETAEETQ ELLKEYGEFR VPAKQTKEKV KLLIQLADSF
VEKGHIHATE IRKWVTTVDK HYRDFSLRMG KYRYSLEKAL GVNTEDNKDL ELDIIPASLS
DREVKLRDAN HEVNEEKRKS ARKKEFIMAE LLQTEKAYVR DLHECLETYL WEMTSGVEEI
PPGILNKEHI IFGNIQEIYD FHNNIFLKEL EKYEQLPEDV GHCFVTWADK FQMYVTYCKN
KPDSNQLILE HAGTFFDEIQ QRHGLANSIS SYLIKPVQRI TKYQLLLKEL LTCCEEGKGE
LKDGLEVMLS VPKKANDAMH VSMLEGFDEN LDVQGELILQ DAFQVWDPKS LIRKGRERHL
FLFEISLVFS KEIKDSSGHT KYVYKNKLLT SELGVTEHVE GDPCKFALWS GRTPSSDNKT
VLKASNIETK QEWIKNIREV IQERIIHLKG ALKEPIQLPK TPAKQRNNSK RDGVEDVDSQ
GDGSSQPDTI SIASRTSQNT VDSDKLSGGC ELTVVLQDFN AGHSSELSIQ VGQTVELLER
PSERPGWCLV RTTERSPPQE GLVPSSALCI SHSRSSVEMD CFFPLVKDAY SHSSENGGKS
ESVANLQAQP SLNSIHSSPG PKRSTNTLKK WLTSPVRRLN SGKADGNIKK QKKVRDGRKS
FDLGSPKPGD ETTPQGDSAD ESKKGWGEDE PDEESHTPLP PPMKIFDNDP TQDEMSSSLL
AARQASTEVP SAADLVSAIE QLVKSKLSLE GGSYRGSLKD PTGCLNEGMT PPTPPRNLEE
EQKAKALRGR MFVLNELVQT EKDYVKDLGI VVEGFMKRIE EKGVPEDMRG KDKIVFGNIH
QIYDWHKDVF LGELEKCIQE QDRLAQLFIK YERKLHIYVW YCQNKPRSEY IVAEYDAYFE
EVKQEINERL TLSDFLIKPI QRITKYQLLL KDFLRYSEKA GLECSDIEKA VELMCLVPKR
CNDMMNLGRL QGFEGTLTAQ GKLLQQDTFY VIELDAGMQS RTKERRVFLF EQIVIFSELL
RKGSLTPGYM FKRSIKMNYL VLEENVDSDP CKFALMNRET SERVILQAAN ADIQQAWVQD
INQVLETQRD FLNALQSPIE YQRKERNTAV MRSQPARVPQ ASPRPYSSIP VGSEKPPKGS
SCNPPLPPLK ISTSNGSSGF DYHQAGDKFE ASKSDLGGCN GVSSMAVIKD YYALKENEIC
VSQGEVVQVL AINQQNMCLV YQPASDHSPA AEGWVPGNIL APLTKATAAT ENSDGSIK
//
