FERM1_PONAB
ID FERM1_PONAB Reviewed; 677 AA.
AC Q5R8M5;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Fermitin family homolog 1;
DE AltName: Full=Kindlin-1;
DE AltName: Full=Unc-112-related protein 1;
GN Name=FERMT1; Synonyms=KIND1, URP1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in cell adhesion. Contributes to integrin
CC activation. When coexpressed with talin, potentiates activation of
CC ITGA2B. Required for normal keratinocyte proliferation. Required for
CC normal polarization of basal keratinocytes in skin, and for normal cell
CC shape. Required for normal adhesion of keratinocytes to fibronectin and
CC laminin, and for normal keratinocyte migration to wound sites (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the cytoplasmic domain of integrins ITGB1 and
CC ITGB3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell
CC junction, focal adhesion {ECO:0000250}. Cell projection, ruffle
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC Cytoplasmic side {ECO:0000250}. Note=Colocalizes with filamentous
CC actin. Constituent of focal adhesions (By similarity). Localized at the
CC basal aspect of skin keratinocytes, close to the cell membrane (By
CC similarity). Upon TGFB1 treatment, it localizes to membrane ruffles (By
CC similarity). {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. The FERM
CC domain contains the subdomains F1, F2 and F3. It is preceded by a F0
CC domain with a ubiquitin-like fold. The F0 domain is required for
CC integrin activation and for localization at focal adhesions (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the kindlin family. {ECO:0000305}.
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DR EMBL; CR859726; CAH91885.1; -; mRNA.
DR RefSeq; NP_001128976.1; NM_001135504.1.
DR AlphaFoldDB; Q5R8M5; -.
DR SMR; Q5R8M5; -.
DR STRING; 9601.ENSPPYP00000011956; -.
DR GeneID; 100190816; -.
DR KEGG; pon:100190816; -.
DR CTD; 55612; -.
DR eggNOG; KOG3727; Eukaryota.
DR InParanoid; Q5R8M5; -.
DR OrthoDB; 248494at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; ISS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:InterPro.
DR GO; GO:0051546; P:keratinocyte migration; ISS:UniProtKB.
DR GO; GO:0043616; P:keratinocyte proliferation; 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; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell junction; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..677
FT /note="Fermitin family homolog 1"
FT /id="PRO_0000270750"
FT DOMAIN 96..653
FT /note="FERM"
FT DOMAIN 337..433
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQL6"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQL6"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQL6"
SQ SEQUENCE 677 AA; 77419 MW; 5053056E5F47A7C9 CRC64;
MLSSTDFTSA SWELVVRVDH PNEEQQKDVT LRVSGDLHVG GVMLQLVEQI NISQDWSDFA
LWWEQKHCWL LKTHWTLDKY GVQADAKLLF TPQHKMLRLR LPNLKMVRLR VSFSAVVFKA
VSDICKTLNI RRSEELSLLK PCGDYFKKKK KKDKNNKEPI TEDILNLESS PTASVSSVSP
GLYSKTMTPI YDPINGTPAS STMTWFSDSP LTEQNCSILA FSQPPQSSEA LADMYQPRSL
VDKAKLNAGW LDSSRSLMEQ GIQEDGQLLL RFKYYSFFDL NPKYDAVRIN QLYEQARWAI
LLEEIDCTEE EMLIFAALQY HISKLSLSAE TQDFTSESEV DEIEAALSNL EVTLEGGKAD
SLLEDITDIP KLADNLKLFR PKKLLLKAFK QYWFVFKDTS IAYFKNKELE QGEPLEKLNL
RGCEVVPNVN VAERKFGIKL LIPVADGMNE MYLRCDHENQ YAQWMAACML ASKGKTMADS
SYRPEVLNIL SFLRMKNRNS ASQVASSPEN MDMNPECFVS PRCAKKHKSK QLAARILEAH
QNVAQMPLVE AKLRFIQAWQ SLPEFGLTYY LVRFKGSKKD DILGVSYNRL IKIDAATGIP
VTTWRFTNIK QWNVSWETRQ VVIEFDQNVF TAFTCLSADC KIVHEYIGGY IFLSTRSKDQ
NETLDEDLFH KLTGGQD
