ID A7MB21_BOVIN Unreviewed; 680 AA.
AC A7MB21;
DT 02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 128.
DE SubName: Full=FERM domain containing kindlin 2 {ECO:0000313|Ensembl:ENSBTAP00000019278.4};
DE SubName: Full=FERMT2 protein {ECO:0000313|EMBL:AAI51293.1};
GN Name=FERMT2 {ECO:0000313|EMBL:AAI51293.1,
GN ECO:0000313|Ensembl:ENSBTAP00000019278.4,
GN ECO:0000313|VGNC:VGNC:28953};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|EMBL:AAI51293.1};
RN [1] {ECO:0000313|EMBL:AAI51293.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=L1 Hereford {ECO:0000313|EMBL:AAI51293.1};
RC TISSUE=Basal ganglia {ECO:0000313|EMBL:AAI51293.1};
RA Moore S., Alexander L., Brownstein M., Guan L., Lobo S., Meng Y.,
RA Tanaguchi M., Wang Z., Yu J., Prange C., Schreiber K., Shenmen C.,
RA Wagner L., Bala M., Barbazuk S., Barber S., Babakaiff R., Beland J.,
RA Chun E., Del Rio L., Gibson S., Hanson R., Kirkpatrick R., Liu J.,
RA Matsuo C., Mayo M., Santos R.R., Stott J., Tsai M., Wong D., Siddiqui A.,
RA Holt R., Jones S.J., Marra M.A.;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000019278.4, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000019278.4,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSBTAP00000019278.4}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000019278.4};
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; BC151292; AAI51293.1; -; mRNA.
DR RefSeq; NP_001094734.1; NM_001101264.1.
DR STRING; 9913.ENSBTAP00000019278; -.
DR PaxDb; 9913-ENSBTAP00000019278; -.
DR Ensembl; ENSBTAT00000019278.5; ENSBTAP00000019278.4; ENSBTAG00000014501.5.
DR GeneID; 616981; -.
DR KEGG; bta:616981; -.
DR CTD; 10979; -.
DR VEuPathDB; HostDB:ENSBTAG00000014501; -.
DR VGNC; VGNC:28953; FERMT2.
DR eggNOG; KOG3727; Eukaryota.
DR GeneTree; ENSGT00390000013444; -.
DR HOGENOM; CLU_011611_1_0_1; -.
DR OMA; PEHGIHY; -.
DR TreeFam; TF314677; -.
DR Reactome; R-BTA-446353; Cell-extracellular matrix interactions.
DR Reactome; R-BTA-9013149; RAC1 GTPase cycle.
DR Reactome; R-BTA-9013423; RAC3 GTPase cycle.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000014501; Expressed in myometrium and 107 other cell types or tissues.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:InterPro.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13205; FERM_C_fermitin; 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 1: Evidence at protein level;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A7MB21};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136}.
FT DOMAIN 380..476
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 141..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 77874 MW; 38E266089C3D4977 CRC64;
MALDGIRMPD GCYADGTWEL SVHVTDLNRD VTLRVTGEVH IGGVMLKLVE KLDVKKDWSD
HALWWEKKRT WLLKTHWTLD KYGIQADAKL QFTPQHKLLR LQLPNMKYVK VKVNFSDRVF
KAVSDICKTF NIRHPEELSL LKKPRDPTKK KKKKLDDQSE DEALELEGPL ITPGSGSIYS
SPGLYSKTMT PTYDAHDGSP LSPTSAWFGD SALSEGNPGI LAVSQPITSP EILAKMFKPQ
ALLDKAKINQ GWLDSSRSLM EQDVKENEAL LLRFKYYSFF DLNPKYDAIR INQLYEQAKW
AILLEEIECT EEEMMMFAAL QYHINKLSIM TSENHLNNSD KEVDEVDAAL SDLEITLEGG
KTSTILGDIT SIPELADYIK VFKPKKLTLK GYKQYWCTFK DTSISCYKSK EESSGTPAHQ
MNLRGCEVTP DVNISGQKFN IKLLIPVAEG MNEIWLRCDN EKQYAHWMAA CRLASKGKTM
ADSSYNLEVQ NILSFLKMQH LNPDPQLIPE QITTDINPEC LVSPRYLKKY KNKQITARIL
EAHQNVAQMS LIEAKMRFIQ AWQSLPEFGI THFIARFQGG KKEELIGIAY NRLIRMDAST
GDAIKTWRFS NMKQWNVNWE IKMVTVEFAD EVRLSFICTE VDCKVVHEFI GGYIFLSTRA
KDQNESLDEE MFYKLTSGWV
//
