ID W5M9S8_LEPOC Unreviewed; 977 AA.
AC W5M9S8;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=PPFIA binding protein 2a {ECO:0000313|Ensembl:ENSLOCP00000005137.1};
GN Name=PPFIBP2 {ECO:0000313|Ensembl:ENSLOCP00000005137.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000005137.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000005137.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the liprin family. Liprin-beta subfamily.
CC {ECO:0000256|ARBA:ARBA00007547}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AHAT01008212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01008213; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5M9S8; -.
DR STRING; 7918.ENSLOCP00000005137; -.
DR Ensembl; ENSLOCT00000005145.1; ENSLOCP00000005137.1; ENSLOCG00000004290.1.
DR eggNOG; KOG1899; Eukaryota.
DR GeneTree; ENSGT01050000244951; -.
DR HOGENOM; CLU_011689_2_1_1; -.
DR InParanoid; W5M9S8; -.
DR OMA; KDHESSM; -.
DR Proteomes; UP000018468; Linkage group LG27.
DR Bgee; ENSLOCG00000004290; Expressed in zone of skin and 13 other cell types or tissues.
DR GO; GO:0048786; C:presynaptic active zone; IBA:GO_Central.
DR GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR CDD; cd09563; SAM_liprin-beta1_2_repeat1; 1.
DR CDD; cd09566; SAM_liprin-beta1_2_repeat2; 1.
DR CDD; cd09569; SAM_liprin-beta1_2_repeat3; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 3.
DR InterPro; IPR029515; Liprin.
DR InterPro; IPR037617; Liprin-beta_SAM_rpt_1.
DR InterPro; IPR037618; Liprin-beta_SAM_rpt_2.
DR InterPro; IPR037619; Liprin-beta_SAM_rpt_3.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR12587; LAR INTERACTING PROTEIN LIP -RELATED PROTEIN; 1.
DR PANTHER; PTHR12587:SF18; LIPRIN-BETA-2; 1.
DR Pfam; PF00536; SAM_1; 2.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00454; SAM; 3.
DR SUPFAM; SSF47769; SAM/Pointed domain; 3.
DR PROSITE; PS50105; SAM_DOMAIN; 3.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 612..676
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 689..747
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 772..803
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 327..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 48..157
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 196..258
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 327..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 977 AA; 110286 MW; A59B9A94B1FCCB61 CRC64;
MASNASHMLE AALEQMDDII AGSKAAAEYN NGMFDMGSPG YLGSLQILQL VEELKIALEI
QANEEEKETI RNQIPAATAQ YLMEWLEKEH MRTKIICLSL NNETYQERLT RLEGDKESLV
LQVSVLTDQV EAQGEKIRDL ETSLDEHHQK LNSTEEMLQQ ELLSRTSLET QKLDLMDEVS
YLKLKLVGME KEQNGCEDKQ HKAEGLLQEL RVLQSKVDEL EGEKCQYEKK LKATKAEIAD
LQQLLAAKDA EIERLQSQLM SRVPVSNDNT ERDQELQRLK IGMDSLLTAN EEKDRRIEEL
TILLNQYRKR KDVMAVTQGS GERILSGSSE EELSGNMKIR NPAHTTHTEK ARSEVRPTPL
SHITISAVWE QRCPLSLPAV TAARMRHALQ QHRVIHINPS CKSLSPGPLL SPSEESFENG
QCSLEELQSG SLQKNRQHLE SNKYQTLPGK LYRSNQNGDK EKYMSSDSQK SSASINNNAD
LTALTFSKSK LSFDFTLNFF TFLHRSRSAS APALGKTEKT EDTALSDLSP LSSGVDSGEQ
SPVSPDSKKN PKGIKKFWGK IRRTQSGTLQ ADDLEPSEFR RGGLWATAGP RLARTKETSS
AFCDLNTPFS KWTTEQVCSW LEDFGLGQYV SLARQWVNNG QTLLAATPQE LEKEMGIKHP
LHRKKCLLAL RSFSTKQTEK SSELDHIWVT RWLDDIGLPQ YKDQFNEARV DGRMLQYLTV
NDLLFLKVTS QLHHHSIKCA IHILHVNNFN ANCLRRRPAD ENKSSPLEVM QWSNHRVMEW
LRSVDLAEYA PNLRGSGVHG GLIILEPRFN SDTLAMLLNI PPQKTLLRRH LATNFNMLIG
SEAQQEKREF MESSSYTPLT TTAKVRPKKL GFSNFGHLRK KKLDDSSDYI CPVDTAQQLP
ASNGGHRGFG RTRGLSPIFD RDMERPEQME VTEGTVQQIG AFSAGINNLT EFLRFSGDIN
DNSTMPCFKL TPTPDTS
//
