ID G3P807_GASAC Unreviewed; 633 AA.
AC G3P807;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Fermitin family member 2 {ECO:0000313|Ensembl:ENSGACP00000013731.1};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000013731.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000013731.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000013731.1}
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 AlphaFoldDB; G3P807; -.
DR Ensembl; ENSGACT00000013756.1; ENSGACP00000013731.1; ENSGACG00000010383.1.
DR GeneTree; ENSGT00390000013444; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000010383; Expressed in testis and 11 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; cd14473; FERM_B-lobe; 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; 2.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635}.
FT DOMAIN 49..526
FT /note="Band 4.1"
FT /evidence="ECO:0000259|SMART:SM00295"
FT DOMAIN 327..432
FT /note="PH"
FT /evidence="ECO:0000259|SMART:SM00233"
FT REGION 97..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 633 AA; 73011 MW; 197F5B9075E21792 CRC64;
MLKLVEKLDV KKDWSDHALW WEKKKTWLLK THWTLDKYGI QADARLLFTP QHKLLRLQLP
NMKHMKVKVN FSDRVFKAVS DICKTFNIRH PEELSLLRKP RDPKKKKKKL EEAEEDDLEL
QGPLLTPGSG SIYSSPGLYS KTMTPTYDSR DGSPLSPTTA WFGDSPLSEG NPSILAVSQP
ISSPDILVKL YKPQSLLDKA KINQGWLDSS RSLMEQDVKE NEVLLLRFKY HSFFDLNPKY
DAIRVNQLYE QSKWAILLEE IECTEEEMMM FAALQYHINK LSIMSSDNHM NNSEKEVDEV
DAALSDLEIT LEGGKTSNSL GDITSIPELA DYVKVFKPKK LTLKGYKQYW CTFKDITISC
YKSKEEAHGT PAHQMNLRGC EVTPDVNISG QKFNIKLLIP VADGMNEIWL RCDMEKQYAH
WMAACRLASK GKTMADSSYN LEVQNILSFL KMQHMNPDPQ FIEPITTDIN PECLVSPRYL
KKYKNKQISA RILEAHQNVA QMSLIEAKMR FIQAWQSLPE FGITHFLAKF QGGKRDELIG
ITYNRLIRMD ASTGDAIKTW RFSNMKQWNV NWEIKMVKVE FADEPCLSFI CAEVDCKVVH
EFIGGYIFLS TRAKDQNESL DEEMFYKLTS GWI
//
