URP2_BOVIN
ID URP2_BOVIN Reviewed; 665 AA.
AC Q32LP0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Fermitin family homolog 3;
DE AltName: Full=Kindlin-3;
DE AltName: Full=Unc-112-related protein 2;
GN Name=FERMT3; Synonyms=KIND3, URP2;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a central role in cell adhesion in hematopoietic cells.
CC Acts by activating the integrin beta-1-3 (ITGB1, ITGB2 and ITGB3).
CC Required for integrin-mediated platelet adhesion and leukocyte adhesion
CC to endothelial cells. Required for activation of integrin beta-2
CC (ITGB2) in polymorphonuclear granulocytes (PMNs).
CC {ECO:0000250|UniProtKB:Q86UX7, ECO:0000250|UniProtKB:Q8K1B8}.
CC -!- SUBUNIT: Interacts with ITGB1, ITGB2 and ITGB3 (via cytoplasmic tails).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell projection, podosome {ECO:0000250}.
CC Note=Present in the F-actin surrounding ring structure of podosomes,
CC which are specialized adhesion structures of hematopoietic cells.
CC {ECO:0000250}.
CC -!- DOMAIN: The FERM domain is not correctly detected by PROSITE or Pfam
CC techniques because it contains the insertion of a PH domain.
CC -!- SIMILARITY: Belongs to the kindlin family. {ECO:0000305}.
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; BC109488; AAI09489.1; -; mRNA.
DR RefSeq; NP_001032695.1; NM_001037606.1.
DR RefSeq; XP_010819463.1; XM_010821161.1.
DR RefSeq; XP_015325547.1; XM_015470061.1.
DR AlphaFoldDB; Q32LP0; -.
DR BMRB; Q32LP0; -.
DR SMR; Q32LP0; -.
DR STRING; 9913.ENSBTAP00000055364; -.
DR PaxDb; Q32LP0; -.
DR PeptideAtlas; Q32LP0; -.
DR PRIDE; Q32LP0; -.
DR Ensembl; ENSBTAT00000062951; ENSBTAP00000055364; ENSBTAG00000045862.
DR GeneID; 525159; -.
DR KEGG; bta:525159; -.
DR CTD; 83706; -.
DR VEuPathDB; HostDB:ENSBTAG00000045862; -.
DR VGNC; VGNC:106741; FERMT3.
DR eggNOG; KOG3727; Eukaryota.
DR GeneTree; ENSGT00390000013444; -.
DR HOGENOM; CLU_065926_0_0_1; -.
DR InParanoid; Q32LP0; -.
DR OMA; AMAGMKT; -.
DR OrthoDB; 248494at2759; -.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000045862; Expressed in monocyte and 101 other tissues.
DR ExpressionAtlas; Q32LP0; baseline and differential.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0030055; C:cell-substrate junction; IBA:GO_Central.
DR GO; GO:0002102; C:podosome; ISS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0033622; P:integrin activation; ISS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0070527; P:platelet aggregation; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0033632; P:regulation of cell-cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd01237; PH_fermitin; 1.
DR Gene3D; 2.30.29.30; -; 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; PTHR16160; 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; SSF47031; SSF47031; 2.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell junction; Cell projection; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..665
FT /note="Fermitin family homolog 3"
FT /id="PRO_0000254653"
FT DOMAIN 229..556
FT /note="FERM"
FT DOMAIN 354..453
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT MOD_RES 11
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q86UX7"
FT MOD_RES 502
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q86UX7"
FT MOD_RES 589
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86UX7"
SQ SEQUENCE 665 AA; 75783 MW; 3E899F65044101CC CRC64;
MAGMKTATGD YIDSSWELRV FIGEEDPEAE SLTLRVTGES HIGGVLLKIV EEIKRKQDWS
DHAIWWEQKR QWLLQTHWTL DKYGILADAR LFFGPQHRPV ILRLPNRRAL RLRASFSQPL
FQAMVAICRL LSIRHPEEMS LLRAPEKEKK KKKEKEPEEE VYDLTKVVLV GGVAPASFRG
MPAHFSDSAQ TEACYHMLSR PQPPPDPLLL QRLPRPSSLL DKTQLHSRWL DSSRCLMQQG
IKAGDTLWLR FKYYSFFDLD PKTDPVRLTQ LYEQARWDLL LEEIDCTEEE MMVFAALQYH
INKLSQSGEV DEPAGTDSGL DDLDLALSNL EVKLEGSAPT DMLDSLTTIP ELKDHLRIFR
PRKLTLKGYR QHWVVFKETT LSYYKSQDEA PGEPIQQLNL KGCEVVPDVN VSGQKFCIKL
LVPSPEGMSE IYLRCQDEQQ YARWMAGCRL ASKGRTMADS SYSSEVQAIL AFLSLQRTGG
GGGGSGNHPQ GPDASAEGLN PYGLVAPRFQ RKFKAKQLTP RILEAHQNVA QLSLSEAQLR
FIQAWQSLPD FGISYVVVRF KGSRKDEILG IANNRLIRID LSVGDVVKTW RFSNMRQWNV
NWDIRQVAIE FDEHINVAFS CVSASCRIVH EYIGGYIFLS TRERARGEEL DEDLFLQLTG
GHEAF
