ID   W5N2U8_LEPOC            Unreviewed;       685 AA.
AC   W5N2U8;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Fermitin family member 2 {ECO:0000313|Ensembl:ENSLOCP00000014957.1};
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:ENSLOCP00000014957.1, 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:ENSLOCP00000014957.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the kindlin family.
CC       {ECO:0000256|ARBA:ARBA00008052}.
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DR   EMBL; AHAT01019070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01019071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01019072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_006632480.1; XM_006632417.2.
DR   AlphaFoldDB; W5N2U8; -.
DR   Ensembl; ENSLOCT00000014986.1; ENSLOCP00000014957.1; ENSLOCG00000012153.1.
DR   GeneID; 102684333; -.
DR   KEGG; loc:102684333; -.
DR   CTD; 10979; -.
DR   GeneTree; ENSGT00390000013444; -.
DR   HOGENOM; CLU_011611_1_0_1; -.
DR   OrthoDB; 5399911at2759; -.
DR   Proteomes; UP000018468; Linkage group LG7.
DR   Bgee; ENSLOCG00000012153; Expressed in larva and 13 other cell types or tissues.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:InterPro.
DR   CDD; cd17181; FERM_F0_KIND2; 1.
DR   CDD; cd17184; FERM_F1_KIND2; 1.
DR   CDD; cd01237; PH_fermitin; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR037843; Kindlin/fermitin.
DR   InterPro; IPR040790; Kindlin_2_N.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR037837; PH_Kindlin/fermitin.
DR   PANTHER; PTHR16160; FERMITIN 2-RELATED; 1.
DR   PANTHER; PTHR16160:SF11; FERMITIN FAMILY HOMOLOG 2; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF18124; Kindlin_2_N; 1.
DR   Pfam; PF00169; PH; 1.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM00233; PH; 1.
DR   SUPFAM; SSF50729; PH domain-like; 2.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT   DOMAIN          378..474
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          141..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        141..159
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   685 AA;  78605 MW;  F0582780D3155267 CRC64;
     MALDGIRMPD GCYADGTWEL KMHVTDLHRD VSLRVTGEIH IGGVMLKLVE KLDVKKDWSD
     HALWWEKKKT WLLKTHWTLD KYGIQADARL LFTPQHKILR LQLPNMKHMK VKVNFSDRVF
     KAVSDICKTF NIRHPEELSL LRKPRDPKKK KKKLDDAEED TLELEGPLIT PGSGSIYSSP
     GLYSKTMTPT YDSRDGSPLS PTSAWFGDSP LSEGNPSILA VSQPISSPEV LAKLYKPQSL
     LDKAKINQGW LDSSRSLMEQ DVKENEVLLL RFKYHSFFDL NPKYDAIRVN QLYEQAKWAI
     LLEEIECTEE EMMMFAALQY HINKLSIMSS DNHMNNSEKE VDEVDAALSD LEITLEGGKT
     SNTLGDITSI PELADYVKVF KPKKLTLKGY KQYWCTFKDI TISCYKSREE AHGTPAHQMN
     LRGCEVTPDV NISGQKFNIK LLIPVADGMN EIWLRCDNEK QYASWMAACR LASKGKTMAD
     SSYNLEVQNI LSFLKMQHMN PDPQMIAEPI NTDINPECLV SPRYLKKYKN KQPGYIRDLI
     SARILEAHQN VAQMSLIEAK MRFIQAWQSL PEFGITHFLA KFQGGKREEL IGITYNRLIR
     MDASTGDAIK TWRFSNMKQW NVNWEIKMVT VEFADEPSLS FICTEVDCKV VHEFIGGYIF
     LSTRAKDQNE SLDEEMFYKL TSGWV
//