ID D7PS99_DANRE Unreviewed; 1041 AA. AC D7PS99; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 12-OCT-2022, entry version 65. DE SubName: Full=Integrin alpha 3 protein {ECO:0000313|EMBL:ADI46646.1}; DE SubName: Full=integrin alpha-3 precursor {ECO:0000313|RefSeq:NP_001177238.1}; GN Name=im:7155971 {ECO:0000313|RefSeq:NP_001177238.1}; GN Synonyms=im:7145180 {ECO:0000313|RefSeq:NP_001177238.1}; GN OrderedLocusNames=itga3b {ECO:0000313|RefSeq:NP_001177238.1, GN ECO:0000313|ZFIN:ZDB-GENE-050411-55}; GN ORFNames=SO:0001217 {ECO:0000313|ZFIN:ZDB-GENE-050411-55}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:ADI46646.1}; RN [1] {ECO:0000313|RefSeq:NP_001177238.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=9007245; RA van Eeden F.J., Granato M., Schach U., Brand M., Furutani-Seiki M., RA Haffter P., Hammerschmidt M., Heisenberg C.P., Jiang Y.J., Kane D.A., RA Kelsh R.N., Mullins M.C., Odenthal J., Warga R.M., Nusslein-Volhard C.; RT "Genetic analysis of fin formation in the zebrafish, Danio rerio."; RL Development 123:255-262(1996). RN [2] {ECO:0000313|EMBL:ADI46646.1, ECO:0000313|RefSeq:NP_001177238.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=20419147; DOI=10.1371/journal.pgen.1000907; RA Carney T.J., Feitosa N.M., Sonntag C., Slanchev K., Kluger J., Kiyozumi D., RA Gebauer J.M., Coffin Talbot J., Kimmel C.B., Sekiguchi K., Wagener R., RA Schwarz H., Ingham P.W., Hammerschmidt M.; RT "Genetic analysis of fin development in zebrafish identifies furin and RT hemicentin1 as potential novel fraser syndrome disease genes."; RL PLoS Genet. 6:e1000907-e1000907(2010). RN [3] {ECO:0000313|RefSeq:NP_001177238.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=21871448; RA O'Brien L.L., Grimaldi M., Kostun Z., Wingert R.A., Selleck R., RA Davidson A.J.; RT "Wt1a, Foxc1a, and the Notch mediator Rbpj physically interact and regulate RT the formation of podocytes in zebrafish."; RL Dev. Biol. 358:318-330(2011). RN [4] {ECO:0000313|RefSeq:NP_001177238.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=24023910; RA Zhang H., Fei C., Wu H., Yang M., Liu Q., Wang Q., Zhang Y.; RT "Transcriptome profiling reveals Th17-like immune responses induced in RT zebrafish bath-vaccinated with a live attenuated Vibrio anguillarum."; RL PLoS ONE 8:e73871-e73871(2013). RN [5] {ECO:0000313|RefSeq:NP_001177238.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26469318; RA Elkon R., Milon B., Morrison L., Shah M., Vijayakumar S., Racherla M., RA Leitch C.C., Silipino L., Hadi S., Weiss-Gayet M., Barras E., Schmid C.D., RA Ait-Lounis A., Barnes A., Song Y., Eisenman D.J., Eliyahu E., RA Frolenkov G.I., Strome S.E., Durand B., Zaghloul N.A., Jones S.M., RA Reith W., Hertzano R.; RT "RFX transcription factors are essential for hearing in mice."; RL Nat. Commun. 6:8549-8549(2015). RN [6] {ECO:0000313|RefSeq:NP_001177238.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=27189481; RA Pasquier J., Cabau C., Nguyen T., Jouanno E., Severac D., Braasch I., RA Journot L., Pontarotti P., Klopp C., Postlethwait J.H., Guiguen Y., RA Bobe J.; RT "Gene evolution and gene expression after whole genome duplication in fish: RT the PhyloFish database."; RL BMC Genomics 17:368-368(2016). RN [7] {ECO:0000313|RefSeq:NP_001177238.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=26876635; RA Gistelinck C., Gioia R., Gagliardi A., Tonelli F., Marchese L., Bianchi L., RA Landi C., Bini L., Huysseune A., Witten P.E., Staes A., Gevaert K., RA De Rocker N., Menten B., Malfait F., Leikin S., Carra S., Tenni R., RA Rossi A., De Paepe A., Coucke P., Willaert A., Forlino A.; RT "Zebrafish Collagen Type I: Molecular and Biochemical Characterization of RT the Major Structural Protein in Bone and Skin."; RL Sci. Rep. 6:21540-21540(2016). RN [8] {ECO:0000313|RefSeq:NP_001177238.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=29615614; RA Williams M.L.K., Sawada A., Budine T., Yin C., Gontarz P., RA Solnica-Krezel L.; RT "Gon4l regulates notochord boundary formation and cell polarity underlying RT axis extension by repressing adhesion genes."; RL Nat. Commun. 9:1319-1319(2018). RN [9] {ECO:0000313|RefSeq:NP_001177238.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=30327840; RA Tian J., Shao J., Liu C., Hou H.Y., Chou C.W., Shboul M., Li G.Q., RA El-Khateeb M., Samarah O.Q., Kou Y., Chen Y.H., Chen M.J., Lyu Z., RA Chen W.L., Chen Y.F., Sun Y.H., Liu Y.W.; RT "Deficiency of lrp4 in zebrafish and human LRP4 mutation induce aberrant RT activation of Jagged-Notch signaling in fin and limb development."; RL Cell. Mol. Life Sci. 76:163-178(2019). RN [10] {ECO:0000313|RefSeq:NP_001177238.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=30635353; RA Gunawan F., Gentile A., Fukuda R., Tsedeke A.T., Jimenez-Amilburu V., RA Ramadass R., Iida A., Sehara-Fujisawa A., Stainier D.Y.R.; RT "Focal adhesions are essential to drive zebrafish heart valve RT morphogenesis."; RL J. Cell Biol. 218:1039-1054(2019). RN [11] {ECO:0000313|RefSeq:NP_001177238.1} RP IDENTIFICATION. RG RefSeq; RL Submitted (APR-2022) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479, CC ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein CC {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}. CC -!- SIMILARITY: Belongs to the integrin alpha chain family. CC {ECO:0000256|ARBA:ARBA00008054, ECO:0000256|RuleBase:RU003762}. 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; GU936669; ADI46646.1; -; mRNA. DR RefSeq; NP_001177238.1; NM_001190309.1. DR SMR; D7PS99; -. DR GeneID; 100331874; -. DR KEGG; dre:100331874; -. DR CTD; 100331874; -. DR ZFIN; ZDB-GENE-050411-55; itga3b. DR ZFIN; ZDB-GENE-050411-55; SO:0001217. DR OrthoDB; 743479at2759; -. DR PhylomeDB; D7PS99; -. DR ChiTaRS; itga3b; zebrafish. DR Proteomes; UP000000437; Chromosome 12. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0008305; C:integrin complex; IBA:GO_Central. DR GO; GO:0005178; F:integrin binding; IBA:GO_Central. DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central. DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central. DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central. DR GO; GO:0033333; P:fin development; IMP:ZFIN. DR GO; GO:0033334; P:fin morphogenesis; IMP:ZFIN. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0050900; P:leukocyte migration; IBA:GO_Central. DR Gene3D; 2.130.10.130; -; 1. DR InterPro; IPR013517; FG-GAP. DR InterPro; IPR013519; Int_alpha_beta-p. DR InterPro; IPR000413; Integrin_alpha. DR InterPro; IPR013649; Integrin_alpha-2. DR InterPro; IPR018184; Integrin_alpha_C_CS. DR InterPro; IPR028994; Integrin_alpha_N. DR InterPro; IPR032695; Integrin_dom_sf. DR Pfam; PF01839; FG-GAP; 2. DR Pfam; PF08441; Integrin_alpha2; 1. DR PRINTS; PR01185; INTEGRINA. DR SMART; SM00191; Int_alpha; 5. DR SUPFAM; SSF69179; SSF69179; 3. DR SUPFAM; SSF69318; SSF69318; 1. DR PROSITE; PS51470; FG_GAP; 3. DR PROSITE; PS00242; INTEGRIN_ALPHA; 1. PE 2: Evidence at transcript level; KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889, KW ECO:0000256|RuleBase:RU003762}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU003762}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003762}; KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|RuleBase:RU003762}; KW Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU003762}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU003762}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU003762}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|RuleBase:RU003762, FT ECO:0000313|RefSeq:NP_001177238.1" FT CHAIN 22..1041 FT /evidence="ECO:0000256|RuleBase:RU003762, FT ECO:0000313|RefSeq:NP_001177238.1" FT /id="PRO_5001424205" FT TRANSMEM 982..1004 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU003762" FT REPEAT 288..349 FT /note="FG-GAP" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803" FT REPEAT 350..405 FT /note="FG-GAP" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803" FT REPEAT 409..471 FT /note="FG-GAP" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00803" FT DOMAIN 456..906 FT /note="Integrin_alpha2" FT /evidence="ECO:0000259|Pfam:PF08441" SQ SEQUENCE 1041 AA; 114923 MW; F5870D8743AA40C6 CRC64; MAGKSLHLCV FVICAIQTNT GFNIDVQFPV IKEGKTKGSL FGFSVALHKQ TEKAKKNLLL VGAPQEKAQP QLSKFKINET GAVYYCPITV NLDDCGSMDL ISPPKSTDML EGMWLGVTVA SQRNGGRVLA CGHRYVKKLL GAEEQQRMVG KCYVRGNDLS YDPSDYWQSE TYELCDFNHD QDLEGMCNMG ISGGMTEKDV YFGTPGSFTW QGTVHMKCRD TDSDYAGDAN DRSFGKLGED KFNIYIGYSV LEDIKLLDRS VFTVVMGAPR DEFKGSVILA DKQDLILKQL MNITGEQIGS YFGSCLAVTD LNNDDWNDLI VGAPFYFDRY KEEGGAVYIF MNENGSFQKK ASLVLKGKKG SGFGFAIAAV GDVNQDGFQD IAVGAPFQDS GKVYIWMGSK SGITKEPSQV IEGKSLGPSG FQTFGYSLSG GMDMDGNDYP DILVGSLDDR IALLRSRPVI HLSKNFTVEP KIVIPSQCGN SCIKVKVCFS YTLSNGNSNF RKEITVKFTI DADQNRRGAR VRFIDNKQST FTGLLSFSAS SCQELELSVN NPVTDKLQPI VFSLNVSLNQ QKAEAQQTLQ SLDSFPVLSG QQILTDKAEI NFHKECGDDN RCSSNLQLKA RFADENYNPF PSQTLEFSSN VKKLVLMVEV SNTADENKPA EDAHQATLNI SIPYSLKYSG VRPPAGFDME CSADEAVICD LGNPFKSNQK VSFIIIFETS GITLYTEQIQ SQLQLSTISE QADLFPVLVT LNVKNTILTT FSLEKLIIDT SFSGNVIGES AMSSTSDVGS PLEFVFRVQV LGEPLGDLGT LVIDFDWPYA VANGKWLLYL TEIVIKGSSE SHCVPPGNIV NYLNLTLSKE GTKRNKREVD SGFPHAEASV TVLATRKVAH FLDCSKKTAL CQTFSCPLLN MSTQAEVRVR ARVWNGTLLE DYAKALRVEV KGQATLRLLT DKPAIKMDNQ TREFSVNIDP VLGEETPYEV PLWIIIVAAV AGILLLGIIS LILWKCGFFR RASRREMYEA KSQKAEIKIQ PSETERLTEE F //