ID   URP2_HUMAN              Reviewed;         667 AA.
AC   Q86UX7; Q8IUA1; Q8N207; Q9BT48;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 177.
DE   RecName: Full=Fermitin family homolog 3;
DE   AltName: Full=Kindlin-3;
DE   AltName: Full=MIG2-like protein;
DE   AltName: Full=Unc-112-related protein 2;
GN   Name=FERMT3; Synonyms=KIND3, MIG2B, URP2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RX   PubMed=12697302; DOI=10.1016/s0925-4439(03)00035-8;
RA   Weinstein E.J., Bourner M., Head R., Zakeri H., Bauer C., Mazzarella R.;
RT   "URP1: a member of a novel family of PH and FERM domain-containing
RT   membrane-associated proteins is significantly over-expressed in lung and
RT   colon carcinomas.";
RL   Biochim. Biophys. Acta 1637:207-216(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Thymus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Lung, and Lymph;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 20-35; 424-438 AND 569-577, IDENTIFICATION BY MASS
RP   SPECTROMETRY, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12886250; DOI=10.1038/sj.leu.2402993;
RA   Boyd R.S., Adam P.J., Patel S., Loader J.A., Berry J., Redpath N.T.,
RA   Poyser H.R., Fletcher G.C., Burgess N.A., Stamps A.C., Hudson L., Smith P.,
RA   Griffiths M., Willis T.G., Karran E.L., Oscier D.G., Catovsky D.,
RA   Terrett J.A., Dyer M.J.S.;
RT   "Proteomic analysis of the cell-surface membrane in chronic lymphocytic
RT   leukemia: identification of two novel proteins, BCNP1 and MIG2B.";
RL   Leukemia 17:1605-1612(2003).
RN   [5]
RP   POSSIBLE FUNCTION (ISOFORM 2).
RX   PubMed=18280249; DOI=10.1016/j.bbrc.2008.02.024;
RA   Wang L., Deng W., Shi T., Ma D.;
RT   "URP2SF, a FERM and PH domain containing protein, regulates NF-kappaB and
RT   apoptosis.";
RL   Biochem. Biophys. Res. Commun. 368:899-906(2008).
RN   [6]
RP   INVOLVEMENT IN LAD3.
RX   PubMed=18779414; DOI=10.1182/blood-2008-06-163162;
RA   Mory A., Feigelson S.W., Yarali N., Kilic S.S., Bayhan G.I.,
RA   Gershoni-Baruch R., Etzioni A., Alon R.;
RT   "Kindlin-3: a new gene involved in the pathogenesis of LAD-III.";
RL   Blood 112:2591-2591(2008).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-11, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [8]
RP   INVOLVEMENT IN LAD3.
RX   PubMed=19617577; DOI=10.1182/blood-2009-04-218636;
RA   Manevich-Mendelson E., Feigelson S.W., Pasvolsky R., Aker M., Grabovsky V.,
RA   Shulman Z., Kilic S.S., Rosenthal-Allieri M.A., Ben-Dor S., Mory A.,
RA   Bernard A., Moser M., Etzioni A., Alon R.;
RT   "Loss of Kindlin-3 in LAD-III eliminates LFA-1 but not VLA-4 adhesiveness
RT   developed under shear flow conditions.";
RL   Blood 114:2344-2353(2009).
RN   [9]
RP   INVOLVEMENT IN LAD3.
RX   PubMed=19064721; DOI=10.1182/blood-2008-10-182154;
RA   Kuijpers T.W., van de Vijver E., Weterman M.A.J., de Boer M., Tool A.T.J.,
RA   van den Berg T.K., Moser M., Jakobs M.E., Seeger K., Sanal O., Uenal S.,
RA   Cetin M., Roos D., Verhoeven A.J., Baas F.;
RT   "LAD-1/variant syndrome is caused by mutations in FERMT3.";
RL   Blood 113:4740-4746(2009).
RN   [10]
RP   INVOLVEMENT IN LAD3, AND FUNCTION.
RX   PubMed=19234463; DOI=10.1038/nm.1931;
RA   Svensson L., Howarth K., McDowall A., Patzak I., Evans R., Ussar S.,
RA   Moser M., Metin A., Fried M., Tomlinson I., Hogg N.;
RT   "Leukocyte adhesion deficiency-III is caused by mutations in KINDLIN3
RT   affecting integrin activation.";
RL   Nat. Med. 15:306-312(2009).
RN   [11]
RP   INVOLVEMENT IN LAD3, AND FUNCTION.
RX   PubMed=19234460; DOI=10.1038/nm.1917;
RA   Malinin N.L., Zhang L., Choi J., Ciocea A., Razorenova O., Ma Y.-Q.,
RA   Podrez E.A., Tosi M., Lennon D.P., Caplan A.I., Shurin S.B., Plow E.F.,
RA   Byzova T.V.;
RT   "A point mutation in KINDLIN3 ablates activation of three integrin
RT   subfamilies in humans.";
RL   Nat. Med. 15:313-318(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-11 AND TYR-504, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND THR-591, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [16]
RP   STRUCTURE BY NMR OF 349-478.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the PH domain of kindlin-3 from human.";
RL   Submitted (FEB-2009) to the PDB data bank.
RN   [17]
RP   VARIANT LAD3 SER-599, CHARACTERIZATION OF VARIANT LAD3 SER-599, AND
RP   FUNCTION.
RX   PubMed=26359933; DOI=10.1111/pai.12485;
RA   Suratannon N., Yeetong P., Srichomthong C., Amarinthnukrowh P.,
RA   Chatchatee P., Sosothikul D., van Hagen P.M., van der Burg M., Wentink M.,
RA   Driessen G.J., Suphapeetiporn K., Shotelersuk V.;
RT   "Adaptive immune defects in a patient with leukocyte adhesion deficiency
RT   type III with a novel mutation in FERMT3.";
RL   Pediatr. Allergy Immunol. 27:214-217(2016).
CC   -!- FUNCTION: Plays a central role in cell adhesion in hematopoietic cells
CC       (PubMed:19234463, PubMed:26359933). Acts by activating the integrin
CC       beta-1-3 (ITGB1, ITGB2 and ITGB3) (By similarity). Required for
CC       integrin-mediated platelet adhesion and leukocyte adhesion to
CC       endothelial cells (PubMed:19234460). Required for activation of
CC       integrin beta-2 (ITGB2) in polymorphonuclear granulocytes (PMNs) (By
CC       similarity). {ECO:0000250|UniProtKB:Q8K1B8,
CC       ECO:0000269|PubMed:19234460, ECO:0000269|PubMed:19234463,
CC       ECO:0000269|PubMed:26359933}.
CC   -!- FUNCTION: Isoform 2 may act as a repressor of NF-kappa-B and apoptosis.
CC       {ECO:0000269|PubMed:19064721, ECO:0000269|PubMed:19234460,
CC       ECO:0000269|PubMed:19234463}.
CC   -!- SUBUNIT: Interacts with ITGB1, ITGB2 and ITGB3 (via cytoplasmic tails).
CC       {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q86UX7-2; Q8N6D5: ANKRD29; NbExp=3; IntAct=EBI-12915620, EBI-17439331;
CC       Q86UX7-2; Q99633: PRPF18; NbExp=3; IntAct=EBI-12915620, EBI-2798416;
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Long, URP2LF;
CC         IsoId=Q86UX7-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short, URP2SF;
CC         IsoId=Q86UX7-2; Sequence=VSP_009226;
CC   -!- TISSUE SPECIFICITY: Highly expressed in lymph node. Expressed in
CC       thymus, spleen and leukocytes. Weakly expressed in placenta, small
CC       intestine, stomach, testis and lung. Overexpressed in B-cell
CC       malignancies. {ECO:0000269|PubMed:12697302,
CC       ECO:0000269|PubMed:12886250}.
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   -!- DISEASE: Leukocyte adhesion deficiency 3 (LAD3) [MIM:612840]: A
CC       disorder characterized by recurrent bacterial infections without pus
CC       formation, leukocytosis and major bleeding disorders.
CC       {ECO:0000269|PubMed:18779414, ECO:0000269|PubMed:19064721,
CC       ECO:0000269|PubMed:19234460, ECO:0000269|PubMed:19234463,
CC       ECO:0000269|PubMed:19617577, ECO:0000269|PubMed:26359933}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
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; AY093951; AAM19736.1; -; mRNA.
DR   EMBL; AY093952; AAM19737.1; -; mRNA.
DR   EMBL; AK093719; BAC04220.1; -; mRNA.
DR   EMBL; BC004347; AAH04347.2; -; mRNA.
DR   EMBL; BC013366; AAH13366.1; -; mRNA.
DR   EMBL; BC015584; AAH15584.1; -; mRNA.
DR   CCDS; CCDS8059.1; -. [Q86UX7-2]
DR   CCDS; CCDS8060.1; -. [Q86UX7-1]
DR   RefSeq; NP_113659.3; NM_031471.5. [Q86UX7-2]
DR   RefSeq; NP_848537.1; NM_178443.2. [Q86UX7-1]
DR   RefSeq; XP_011543596.1; XM_011545294.2.
DR   RefSeq; XP_016873887.1; XM_017018398.1.
DR   PDB; 2YS3; NMR; -; A=349-482.
DR   PDB; 6V97; X-ray; 2.38 A; A/B=1-667.
DR   PDB; 6V9G; X-ray; 2.35 A; A/B=1-667.
DR   PDB; 7C3M; X-ray; 3.60 A; A/B/C=1-667.
DR   PDBsum; 2YS3; -.
DR   PDBsum; 6V97; -.
DR   PDBsum; 6V9G; -.
DR   PDBsum; 7C3M; -.
DR   AlphaFoldDB; Q86UX7; -.
DR   SMR; Q86UX7; -.
DR   BioGRID; 123735; 62.
DR   CORUM; Q86UX7; -.
DR   IntAct; Q86UX7; 40.
DR   MINT; Q86UX7; -.
DR   STRING; 9606.ENSP00000279227; -.
DR   iPTMnet; Q86UX7; -.
DR   PhosphoSitePlus; Q86UX7; -.
DR   BioMuta; FERMT3; -.
DR   DMDM; 41018464; -.
DR   EPD; Q86UX7; -.
DR   jPOST; Q86UX7; -.
DR   MassIVE; Q86UX7; -.
DR   MaxQB; Q86UX7; -.
DR   PaxDb; 9606-ENSP00000279227; -.
DR   PeptideAtlas; Q86UX7; -.
DR   PRIDE; Q86UX7; -.
DR   ProteomicsDB; 69932; -. [Q86UX7-1]
DR   ProteomicsDB; 69933; -. [Q86UX7-2]
DR   Pumba; Q86UX7; -.
DR   Antibodypedia; 29146; 311 antibodies from 37 providers.
DR   DNASU; 83706; -.
DR   Ensembl; ENST00000279227.10; ENSP00000279227.5; ENSG00000149781.14. [Q86UX7-1]
DR   Ensembl; ENST00000345728.10; ENSP00000339950.5; ENSG00000149781.14. [Q86UX7-2]
DR   Ensembl; ENST00000544997.6; ENSP00000445778.2; ENSG00000149781.14. [Q86UX7-2]
DR   Ensembl; ENST00000698852.1; ENSP00000513984.1; ENSG00000149781.14. [Q86UX7-2]
DR   Ensembl; ENST00000698860.1; ENSP00000513988.1; ENSG00000149781.14. [Q86UX7-1]
DR   Ensembl; ENST00000698861.1; ENSP00000513989.1; ENSG00000149781.14. [Q86UX7-2]
DR   Ensembl; ENST00000698863.1; ENSP00000513991.1; ENSG00000149781.14. [Q86UX7-2]
DR   Ensembl; ENST00000698870.1; ENSP00000513996.1; ENSG00000149781.14. [Q86UX7-2]
DR   GeneID; 83706; -.
DR   KEGG; hsa:83706; -.
DR   MANE-Select; ENST00000345728.10; ENSP00000339950.5; NM_031471.6; NP_113659.3. [Q86UX7-2]
DR   UCSC; uc001nyl.3; human. [Q86UX7-1]
DR   AGR; HGNC:23151; -.
DR   CTD; 83706; -.
DR   DisGeNET; 83706; -.
DR   GeneCards; FERMT3; -.
DR   HGNC; HGNC:23151; FERMT3.
DR   HPA; ENSG00000149781; Tissue enhanced (bone marrow, lymphoid tissue).
DR   MalaCards; FERMT3; -.
DR   MIM; 607901; gene.
DR   MIM; 612840; phenotype.
DR   neXtProt; NX_Q86UX7; -.
DR   OpenTargets; ENSG00000149781; -.
DR   Orphanet; 99844; Leukocyte adhesion deficiency type III.
DR   PharmGKB; PA162388384; -.
DR   VEuPathDB; HostDB:ENSG00000149781; -.
DR   eggNOG; KOG3727; Eukaryota.
DR   GeneTree; ENSGT00390000013444; -.
DR   HOGENOM; CLU_011611_0_0_1; -.
DR   InParanoid; Q86UX7; -.
DR   OMA; RWLLQTH; -.
DR   OrthoDB; 5399911at2759; -.
DR   PhylomeDB; Q86UX7; -.
DR   TreeFam; TF314677; -.
DR   PathwayCommons; Q86UX7; -.
DR   Reactome; R-HSA-114608; Platelet degranulation.
DR   SignaLink; Q86UX7; -.
DR   SIGNOR; Q86UX7; -.
DR   BioGRID-ORCS; 83706; 32 hits in 1152 CRISPR screens.
DR   ChiTaRS; FERMT3; human.
DR   EvolutionaryTrace; Q86UX7; -.
DR   GeneWiki; FERMT3; -.
DR   GenomeRNAi; 83706; -.
DR   Pharos; Q86UX7; Tbio.
DR   PRO; PR:Q86UX7; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q86UX7; Protein.
DR   Bgee; ENSG00000149781; Expressed in granulocyte and 121 other cell types or tissues.
DR   ExpressionAtlas; Q86UX7; 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:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR   GO; GO:0002102; C:podosome; ISS:UniProtKB.
DR   GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR   GO; GO:0008289; F:lipid binding; EXP:DisProt.
DR   GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR   GO; GO:0033622; P:integrin activation; IDA:UniProtKB.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
DR   GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:UniProtKB.
DR   GO; GO:0070527; P:platelet aggregation; HMP:UniProtKB.
DR   GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR   GO; GO:0033632; P:regulation of cell-cell adhesion mediated by integrin; IDA:UniProtKB.
DR   GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13205; FERM_C_fermitin; 1.
DR   CDD; cd17182; FERM_F0_KIND3; 1.
DR   CDD; cd17185; FERM_F1_KIND3; 1.
DR   CDD; cd01237; PH_fermitin; 1.
DR   DisProt; DP01784; -.
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:SF1; FERMITIN FAMILY HOMOLOG 3; 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; PS00661; FERM_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   Genevisible; Q86UX7; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell adhesion; Cell junction;
KW   Cell projection; Direct protein sequencing; Disease variant;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..667
FT                   /note="Fermitin family homolog 3"
FT                   /id="PRO_0000219454"
FT   DOMAIN          229..558
FT                   /note="FERM"
FT   DOMAIN          354..457
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         11
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:18088087,
FT                   ECO:0007744|PubMed:19690332"
FT   MOD_RES         504
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         591
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         360..363
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12697302,
FT                   ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT                   /id="VSP_009226"
FT   VARIANT         599
FT                   /note="Q -> S (in LAD3; uncertain significance; decreases
FT                   cell adhesion in hematopoietic cells; requires 2 nucleotide
FT                   substitutions)"
FT                   /evidence="ECO:0000269|PubMed:26359933"
FT                   /id="VAR_074597"
FT   CONFLICT        472
FT                   /note="A -> P (in Ref. 2; BAC04220)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        480
FT                   /note="Q -> R (in Ref. 2; BAC04220)"
FT                   /evidence="ECO:0000305"
FT   STRAND          16..21
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   STRAND          24..26
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   STRAND          29..36
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   HELIX           42..51
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   STRAND          62..66
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   TURN            67..70
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   HELIX           80..83
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   STRAND          91..103
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   STRAND          109..118
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   HELIX           120..130
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   HELIX           136..138
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   STRAND          139..142
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   HELIX           195..199
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   HELIX           207..212
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   HELIX           220..228
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   HELIX           237..239
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   STRAND          246..251
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   TURN            261..263
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   HELIX           265..280
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   HELIX           288..306
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   STRAND          370..373
FT                   /evidence="ECO:0007829|PDB:2YS3"
FT   STRAND          377..380
FT                   /evidence="ECO:0007829|PDB:2YS3"
FT   STRAND          385..390
FT                   /evidence="ECO:0007829|PDB:2YS3"
FT   TURN            391..395
FT                   /evidence="ECO:0007829|PDB:2YS3"
FT   TURN            404..406
FT                   /evidence="ECO:0007829|PDB:2YS3"
FT   STRAND          408..411
FT                   /evidence="ECO:0007829|PDB:2YS3"
FT   HELIX           415..417
FT                   /evidence="ECO:0007829|PDB:2YS3"
FT   STRAND          419..427
FT                   /evidence="ECO:0007829|PDB:2YS3"
FT   STRAND          429..441
FT                   /evidence="ECO:0007829|PDB:2YS3"
FT   HELIX           442..456
FT                   /evidence="ECO:0007829|PDB:2YS3"
FT   HELIX           465..480
FT                   /evidence="ECO:0007829|PDB:2YS3"
FT   HELIX           503..505
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   HELIX           509..514
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   HELIX           517..529
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   TURN            530..533
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   HELIX           536..548
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   TURN            551..554
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   STRAND          556..562
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   STRAND          569..573
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   STRAND          575..581
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   TURN            583..585
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   STRAND          587..593
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   HELIX           594..596
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   STRAND          597..603
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   TURN            604..607
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   STRAND          608..613
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   TURN            614..616
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   STRAND          617..626
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   HELIX           628..641
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   TURN            642..645
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   TURN            647..649
FT                   /evidence="ECO:0007829|PDB:6V9G"
FT   HELIX           654..660
FT                   /evidence="ECO:0007829|PDB:6V9G"
SQ   SEQUENCE   667 AA;  75953 MW;  5ACE15EB689B91B5 CRC64;
     MAGMKTASGD YIDSSWELRV FVGEEDPEAE SVTLRVTGES HIGGVLLKIV EQINRKQDWS
     DHAIWWEQKR QWLLQTHWTL DKYGILADAR LFFGPQHRPV ILRLPNRRAL RLRASFSQPL
     FQAVAAICRL LSIRHPEELS LLRAPEKKEK KKKEKEPEEE LYDLSKVVLA GGVAPALFRG
     MPAHFSDSAQ TEACYHMLSR PQPPPDPLLL QRLPRPSSLS DKTQLHSRWL DSSRCLMQQG
     IKAGDALWLR FKYYSFFDLD PKTDPVRLTQ LYEQARWDLL LEEIDCTEEE MMVFAALQYH
     INKLSQSGEV GEPAGTDPGL DDLDVALSNL EVKLEGSAPT DVLDSLTTIP ELKDHLRIFR
     IPRRPRKLTL KGYRQHWVVF KETTLSYYKS QDEAPGDPIQ QLNLKGCEVV PDVNVSGQKF
     CIKLLVPSPE GMSEIYLRCQ DEQQYARWMA GCRLASKGRT MADSSYTSEV QAILAFLSLQ
     RTGSGGPGNH PHGPDASAEG LNPYGLVAPR FQRKFKAKQL TPRILEAHQN VAQLSLAEAQ
     LRFIQAWQSL PDFGISYVMV RFKGSRKDEI LGIANNRLIR IDLAVGDVVK TWRFSNMRQW
     NVNWDIRQVA IEFDEHINVA FSCVSASCRI VHEYIGGYIF LSTRERARGE ELDEDLFLQL
     TGGHEAF
//