ID A0A3B5B3M7_9TELE Unreviewed; 1839 AA.
AC A0A3B5B3M7;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Microtubule-associated protein futsch-like {ECO:0000313|Ensembl:ENSSPAP00000027376.1, ECO:0000313|RefSeq:XP_008280328.1};
GN Name=LOC103357519 {ECO:0000313|RefSeq:XP_008280328.1};
OS Stegastes partitus (bicolor damselfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Stegastes.
OX NCBI_TaxID=144197 {ECO:0000313|Ensembl:ENSSPAP00000027376.1, ECO:0000313|Proteomes:UP000261400};
RN [1] {ECO:0000313|Ensembl:ENSSPAP00000027376.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_008280328.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Alpha-type
CC protein kinase family. ALPK subfamily. {ECO:0000256|ARBA:ARBA00008651}.
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DR RefSeq; XP_008280328.1; XM_008282106.1.
DR Ensembl; ENSSPAT00000027820.1; ENSSPAP00000027376.1; ENSSPAG00000020635.1.
DR GeneID; 103357519; -.
DR CTD; 100321139; -.
DR GeneTree; ENSGT00940000158534; -.
DR OrthoDB; 5321836at2759; -.
DR Proteomes; UP000261400; Unplaced.
DR Proteomes; UP000694891; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd16973; Alpha_kinase_ALPK3; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 3.20.200.10; MHCK/EF2 kinase; 1.
DR InterPro; IPR004166; a-kinase_dom.
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; IPR011009; Kinase-like_dom_sf.
DR PANTHER; PTHR47091; ALPHA-PROTEIN KINASE 2-RELATED; 1.
DR PANTHER; PTHR47091:SF1; ALPHA-PROTEIN KINASE 3; 1.
DR Pfam; PF02816; Alpha_kinase; 1.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00811; Alpha_kinase; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51158; ALPHA_KINASE; 1.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 3: Inferred from homology;
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Reference proteome {ECO:0000313|Proteomes:UP000694891};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 63..159
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1414..1502
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1530..1761
FT /note="Alpha-type protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS51158"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1110..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1246..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1769..1839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 629..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..895
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1119..1151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1769..1812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1813..1839
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1839 AA; 204524 MW; F4A21D2D6E3F4251 CRC64;
MTSRRPMTRS FSGNGRTSSF SEEDSGSSNG RSESRSTYLS NVRPENRSTL CSVMAQLTED
IQPSFDTTLK SKAVSENCNV KFTCVVSGLP PPELKWYKDD MEMDRYCGLP KYEIRKNGKT
HTLHIYNCTL DDAAIYQVSA SNSKGIVSCS GVLEVGTMSE FQIHQRFFAK LKQKAEKKKK
DLEEPTKKED KENIQKEKPQ SSPEPPPRKR SVPPPKEKAA VKDSLAVEQL GAAAEPNGIS
PEVKESLKDE TSPSEEMLAK KRIKMSNGVD VGVNSSSSSR SHVMGNGGEN CYDGGISLAQ
FLAETLQSQT AEEKQNTSRV DNPKEMDTAV VSSVNKEKER DQEKMLKKTE EQEKALQEEF
EKEKRREEEL VVEREKERER QLEVLHTAAH GKHGPEVKHH SKGHKDHDHH NIQTSISSML
HTVKDFFFGK TKKGSHDHFE SEEREFDYSH DSAQPLQPEM PPSFRLQAEH DPEVCNSLTE
EVVSMEIDKP KEPSETVDVG QQSVSVEPHK FKYEDSVVHT NLPPAHKLPP ESVKESTEQS
VTEADDAAEA MEVTVAPEGS DARQEMSLTG LQVLTEAEKK DAEVVSVIKE VPVHQQEPEC
LVASAQPNQQ GARAESSPRE DKFVLPQTQA PSDEESLPTS TLASSEDGWT PPHSVVSTTL
NHKLGEAPIE TLQEEELSVD NVGREGEPKA EEAPSSNKLC EEEKAEVKSN SHPFSDINRS
EITEITRCSM EDRIEPCESK ATDQVLSPLS AVAACSAARD HVNEETKCTS LIQEMNVGFP
PTADPEGLEK GDLKMQHECT PSDRGEITGS VNAMQSSNSG FTSSEERCEL NKILSSALEK
DLESNLCNSL KTQEQAVLEG ESNEGRNESL LPEVATESRT LKKEEKLDES EIVSVKQSKG
RNTAILEEHS NNALQDSSEK QHDWPLKNIP PIQISTFEDI TDIKPPEPDM RPNEPFIIPK
IEIVEPELKE CTLPLTILAL NKPETSNLQD HDVTHESKII IQDQSLADSP GLLPTQEGMQ
NNYHLSPTEK VKEVAQCDDE RDTLEQQQPH EKSSEQLPQM DYASIPVINV SCTDEKEADA
FENSHDSHAQ PAFEIPKVPS FVVPPISVTC HESDPEPRLP TQSESTETET SVCTQQGTKH
DVGNNMTTKP EKSQSRRQDL EEMSEKSIKE NTPTMLYEAL IPKVGDSVPS FNKTTEDENL
KPKSLKMENS MSVEDLQKNR FSVERLSSKP PAYPSLSPAS LRKFMSKAAP DSDNEAGTTG
RVSAVGDKTE EDLSGGSTPT SSLSCESSPR LKRRDSLTLI RSATPEELAS GARRKIFFPK
NKDDVEIAVF GALDTQGKKE NPYMSPSQAR RAALLQASTG QSTPPMERRS PLLSRRKATL
EVPKVVEQTA TEEPAGNKRE EKPAEKKIDP LKAPQVIRKI RGEPFPDASG HLKLWCQFFN
VLSDSTIKWY KDEEEILEMK RSGGDESQVA LAIVLASSQD CGVYGCTIKN DYGTDTTDYL
LSIDILSEIL LKDDLEVGEE IEMTPMLFTR GLADCGTWGD KYFGRIMTET VHMGEGCAHK
ASRVKVIYGL DPIFESGSAC IIKVQNPIAY GTKQESNLAE RNLEITKQEC KVQNMIREYC
KIFAAEARVI ENFGCSLEVI PRYLMYRPAN SVPYASVEAD LTGVFLKYCE MDPKGKLISQ
NVSELEQKCS AFQHWIHQWT HGNLLVTQLE GVESKITNVQ VVTKSKGYQG LTEQASPEVF
EQFLGQHQCN YYCGLLGLRP LKTVDSLQQP TKIKGSRSPL LNRKLTSGSP QLQRKGHSPQ
MPRKANSSPK VTRKVQETED SKSDVKPKPA ETLDVLEMR
//
