ID A0A3P9CMF5_9CICH Unreviewed; 803 AA.
AC A0A3P9CMF5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
OS Maylandia zebra (zebra mbuna).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005023001.1, ECO:0000313|Proteomes:UP000265160};
RN [1] {ECO:0000313|Ensembl:ENSMZEP00005023001.1, ECO:0000313|Proteomes:UP000265160}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25186727; DOI=10.1038/nature13726;
RA Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA Di Palma F.;
RT "The genomic substrate for adaptive radiation in African cichlid fish.";
RL Nature 513:375-381(2014).
RN [2] {ECO:0000313|Ensembl:ENSMZEP00005023001.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251,
CC ECO:0000256|RuleBase:RU000633}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}. Cell
CC projection, invadopodium membrane {ECO:0000256|ARBA:ARBA00004297};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004297}.
CC Cell projection, lamellipodium {ECO:0000256|ARBA:ARBA00004510}. Cell
CC projection, ruffle membrane {ECO:0000256|ARBA:ARBA00004199}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004199}.
CC Melanosome {ECO:0000256|ARBA:ARBA00004223}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family.
CC {ECO:0000256|ARBA:ARBA00007449, ECO:0000256|RuleBase:RU000633}.
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DR RefSeq; XP_004568570.1; XM_004568513.3.
DR AlphaFoldDB; A0A3P9CMF5; -.
DR Ensembl; ENSMZET00005023757.1; ENSMZEP00005023001.1; ENSMZEG00005017220.1.
DR GeneID; 101477057; -.
DR CTD; 556734; -.
DR GeneTree; ENSGT01090000259987; -.
DR OrthoDB; 5475862at2759; -.
DR Proteomes; UP000265160; LG9.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR Gene3D; 4.10.1240.30; -; 1.
DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR040622; I-EGF_1.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR InterPro; IPR012896; Integrin_bsu_tail.
DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR PANTHER; PTHR10082:SF28; INTEGRIN BETA-1; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF18372; I-EGF_1; 1.
DR Pfam; PF08725; Integrin_b_cyt; 1.
DR Pfam; PF07965; Integrin_B_tail; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR PIRSF; PIRSF002512; Integrin_B; 1.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00187; INB; 1.
DR SMART; SM01241; Integrin_b_cyt; 1.
DR SMART; SM01242; Integrin_B_tail; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF69687; Integrin beta tail domain; 1.
DR SUPFAM; SSF69179; Integrin domains; 1.
DR SUPFAM; SSF103575; Plexin repeat; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS00243; INTEGRIN_BETA; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU000633};
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR002512-1};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU000633};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Myogenesis {ECO:0000256|ARBA:ARBA00022541};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000265160};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000633};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..803
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018093497"
FT TRANSMEM 733..755
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 34..468
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 644..732
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 756..802
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT DISULFID 27..468
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 35..45
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 38..75
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 48..64
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 210..216
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 264..304
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 438..696
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 466..470
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 490..529
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 495..504
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 506..520
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 535..540
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 537..572
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 542..557
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 559..564
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 578..583
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 580..611
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 585..594
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 596..603
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 617..622
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 619..665
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 624..634
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 637..640
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 644..653
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 650..727
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 669..704
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 803 AA; 89405 MW; 921B70E78D719F03 CRC64;
MDLKVILISL LLGVFCYCNP QKEGNECISA NAKHCGECIQ AGAKCGWCEQ ENFLKQGEAL
STRCDEVESL KDRGCNDSQI QNPTGKKWII TNKRVTNRKK VTGVETNKPK PEEITQIQPQ
KLRLNLRSGQ PQSFDLKFKR AEDYPIDLYY LMDLSYSMKD DLENVKNLGT SLMLEMKKIT
SDFHIGFGSF VEKTVMPYIS TTPSKLLNPC TGDQNCTSPF SYKNVLSLTS DGNMFNSLVG
KQQISGNLDS PEGGFDAIMQ VAVCGKEIGW RNVTRLLVFS TDAGFHFAGD GKLGGIVLPN
DGKCHLEDNV YTMSHYYDYP SIAHLVQKLS DNNIQTIFAV TEEFQPVYQE LKNLIPKSAV
GTLSANSSNV INLIIDAYNS LSSEVILDNS KLPEGVEIEY KSQCKNGVVN DKDDGRKCSN
ISIGDEVNFN ITVTSKGCPN EGKSETIKIK PLGFTEEVEI ILNFICDCQC QNNDVVKKSE
KCSLNGTFEC GACRCFEGRV GRNCECSSND MATDDMDQTC RKDNSTDICS NNGECVCGTC
ECKKRPNPEE RYSGQFCECD NFNCDRSENK LCGGNGRCVC RECICDPMWS GRACDCSLDN
STCLATNKQI CNGRGRCECG VCKCTDPKFQ GPTCETCPTC PGVCAEHKLC VQCRAFGTGE
KMKTCKEECS YFNLITVKDR NKLPQPNDYP YPVMHCKERD ANDCWFYYTY AVNDTEREVH
VVDKLDCPSG PDIIPIVAGV VAGIVLIGLA LLLIWKLLMI IHDRREFAKF EKEKMNAKWD
TGENPIYKSA VTTVVNPKYE GKC
//
