ID A0A3P8PM67_ASTCA Unreviewed; 687 AA.
AC A0A3P8PM67;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Fermitin family member 2 {ECO:0000313|Ensembl:ENSACLP00000018064.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000018064.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000018064.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000018064.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the kindlin family.
CC {ECO:0000256|ARBA:ARBA00008052}.
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DR AlphaFoldDB; A0A3P8PM67; -.
DR Ensembl; ENSACLT00000018495.1; ENSACLP00000018064.1; ENSACLG00000012283.1.
DR GeneTree; ENSGT00390000013444; -.
DR Proteomes; UP000265100; Chromosome 19.
DR Bgee; ENSACLG00000012283; Expressed in muscle tissue and 7 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; 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; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889}.
FT DOMAIN 389..485
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 141..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 687 AA; 78837 MW; 775524D001BFA809 CRC64;
MALDGIRMPD GCYADGTWEL KIHVTDLYRD VSLRVTGEIH IGGVMLKLVE KLDVKRDWSD
HALWWEKKKT WLLKTHWTLD KYGIQADARL LFTPQHKLLR LQLPNMKHMK VKVNFSDRVF
KAVSDICKTF NIRHPEELSL LRKPRDPKKK KKKLEETEED DLELEGPMLT PGSASEIIYI
GPVKGSIYSS PGLYSKTMTP TYDSRDGSPL SPTSAWFGDS PLSEGNPSIL AVSQPISSPD
ILVKLYKPQS LLDKAKINQG WLDSSRSLME QDVKENEVLL LRFKYHSFFD LNPKYDAIRV
NQLYEQAKWA ILLEEIECTE EEMMMFAALQ YHINKLSIMS SDNHMNNSEK EVDEVDAALS
DLEITLEGGK TSNTLGDITS IPELADYVKV FKPKKLTLKG YKQYWCTFKD ITISCYKSKE
EAHGTPSHQM NLRGCEVTPD VNISGQKFNI KLLIPVADGM NEIWLRCDTE KQYAHWMAAC
RLASKGKTMA DSSYNLEVQN ILSFLKMQHM NPDLPIEPVA TDINPECLVS PRYLKKYKNK
QISARILEAH QNVAQMSLIE AKMRFIQAWQ SLPEFGITHF LAKFQGGKRE ELIGITYNRL
IRMDASTGDA IKTWRFSNMK QWNVNWEIKM VTVEFADEPS LSFICAEVDC KVVHEFIGGY
IFLSTRAKDQ NESLDEEMFY KLTSGWV
//
