ID A0A452CPM3_BALAS Unreviewed; 1236 AA.
AC A0A452CPM3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 isoform X18 {ECO:0000313|RefSeq:XP_028024888.1};
GN Name=MAGI1 {ECO:0000313|RefSeq:XP_028024888.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_028024888.1};
RN [1] {ECO:0000313|RefSeq:XP_028024888.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028024888.1};
RG RefSeq;
RL Submitted (JAN-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004170};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
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DR RefSeq; XP_028024888.1; XM_028169087.1.
DR AlphaFoldDB; A0A452CPM3; -.
DR Proteomes; UP000261681; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00992; PDZ_signaling; 5.
DR CDD; cd00201; WW; 2.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 2.30.42.10; -; 6.
DR Gene3D; 3.30.63.10; Guanylate Kinase phosphate binding domain; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR10316; MEMBRANE ASSOCIATED GUANYLATE KINASE-RELATED; 1.
DR PANTHER; PTHR10316:SF12; MEMBRANE-ASSOCIATED GUANYLATE KINASE, WW AND PDZ DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF16663; MAGI_u1; 1.
DR Pfam; PF16666; MAGI_u5; 1.
DR Pfam; PF00595; PDZ; 5.
DR Pfam; PF00397; WW; 2.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 6.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 6.
DR SUPFAM; SSF51045; WW domain; 2.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 6.
DR PROSITE; PS01159; WW_DOMAIN_1; 2.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|RefSeq:XP_028024888.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|RefSeq:XP_028024888.1}.
FT DOMAIN 17..105
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 96..189
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 300..333
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 359..392
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 460..529
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 631..709
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 801..883
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 958..1042
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1100..1182
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 237..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..752
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1236 AA; 134459 MW; 2EBF522EBF901CB6 CRC64;
MSKVIQKKNH WTSRVHECTV KRGPQGELGV TVLGGAENGE FPYVGAVAAA EAAGLPGGGQ
SPRLGEGELL LEVQGIRVSG LPRYDVLGVI DSCKEAVTFR AVRQGGKLNK DLRHFLNQRF
QKGSPDHELQ QTIRDNLYRH AVPCTTRSPR EGEVPGVDYS FLTVKEFLDL ERSGTLLEVG
TYEGNYYGTP KPPSQPLSGK VITTDALQSL HSGSKQSTPK RTKSYNDMQN AGIVHAENEE
EDDAPEMNSS FTADSGDQEE HSLQEATLPP ANSSIIAAPI TDPSQKFPQY LPLSAEDNLG
PLPENWEMAY TENGEVYFID HNTKTTSWLD PRCLNKQQKP LEECEDDEGI HTEELDSELE
LPAGWEKIDD PVYGIYYVDH INRKTQYENP VLEAKRKKQL EQQQPQQQQP EEWTEDHSSL
VPPIIPNHPP SNPEQAREAP LQGKPFFTRN PSELKGKFIH TKLRKSSRGF GFTVVGGDEP
DEFLQIKSLV LDGPAALDGK METGDVIVSV NDTCVLGHTH AQVVKIFQSI PIGASVDLEL
CRGYPLPFDP DDPNTSLVTS VAILDKEPII VNGQETYDSP ASHSSKTGKV NGMKDARPSS
PADVASNGSH GYPNDTVSLA SSIATQPELI TVHIVKGPMG FGFTIADSPG GGGQRVKQIV
DSPRCRGLKE GDLIVEVNKK NVQALTHNQV VDMLIESPKG SEVTLLVQRG GLPVPKKSPK
SQPLERKDSQ NSSQHSAASH RSLHTASPSH GTQVLPEFPP AEAPAPDQTD SSGQKKPDPF
KIWAQSRSMY ENRLPDYQEQ DIFLWRKETG FGFRILGGNE PGEPIYIGHI VPLGAADTDG
RLRSGDELIC VDGTPVIGKS HQLVVQLMQQ AAKQGHVNLT VRRKVVFAAS KTENEVPSPA
SSHHSSNQPA SLTEEKRTPQ GSQNSLNTVS SGSGSTSGIG SGGGGGSGVV STVVQPYDVE
IRRGENEGFG FVIVSSVSRP EAGTTFGRII EGSPADRCGK LKVGDRILAV NGCSITNKSH
SDIVNLIKEA GNTVTLRIIP GDESSNATLL TNAEKIATIT TTHTPSQQGA QETRNTTKPK
PESQFEFKAP QVTQEQDFYT VELERGAKGF GFSLRGGREY NMDLYVLRLA EDGPAERCGK
MRVGDEILEI NGETTKNMKH SRAIELIKNG GRRVRLFLKR GDGSVPEYAM IPPNIAACMR
NEKLGEACFY LMGHNQTTTP AATGTALPPV HKVFRK
//
