ID F6QJM4_CIOIN Unreviewed; 751 AA.
AC F6QJM4;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=LOC100179396 {ECO:0000313|Ensembl:ENSCINP00000006408.3};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000006408.3, ECO:0000313|Proteomes:UP000008144};
RN [1] {ECO:0000313|Proteomes:UP000008144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12481130; DOI=10.1126/science.1080049;
RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA Satoh N., Rokhsar D.S.;
RT "The draft genome of Ciona intestinalis: insights into chordate and
RT vertebrate origins.";
RL Science 298:2157-2167(2002).
RN [2] {ECO:0000313|Ensembl:ENSCINP00000006408.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {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 AlphaFoldDB; F6QJM4; -.
DR STRING; 7719.ENSCINP00000006408; -.
DR Ensembl; ENSCINT00000006408.3; ENSCINP00000006408.3; ENSCING00000003141.3.
DR GeneTree; ENSGT01100000263555; -.
DR HOGENOM; CLU_011772_4_0_1; -.
DR InParanoid; F6QJM4; -.
DR OMA; TERCEFR; -.
DR TreeFam; TF105392; -.
DR Proteomes; UP000008144; Unplaced.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; 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:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
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; 2.
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; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR012896; Integrin_bsu_tail.
DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR PANTHER; PTHR10082:SF42; INTEGRIN BETA-4; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF18372; I-EGF_1; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF17205; PSI_integrin; 1.
DR PIRSF; PIRSF002512; Integrin_B; 1.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00187; INB; 1.
DR SMART; SM01242; Integrin_B_tail; 1.
DR SUPFAM; SSF69687; Integrin beta tail domain; 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|RuleBase:RU000633};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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 Reference proteome {ECO:0000313|Proteomes:UP000008144};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000633};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 716..742
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..471
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 632..711
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DISULFID 22..53
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 32..42
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 239..282
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 479..512
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 484..493
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 518..523
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 525..541
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 543..546
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 566..570
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 568..598
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 572..581
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 583..590
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 604..609
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 606..653
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 611..622
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 625..629
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 632..641
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 638..708
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 657..685
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 751 AA; 80623 MW; E252DBCB84D96E00 CRC64;
SSSSSSSTSS SVCVQAKVPE DCIKVNPNCQ WCAQEDFSGQ RCNIQPILEE QGCSDLQIIE
SSVAMDAANE ANRFDHQSAS VSVTSLCRDV VINIRQARIR VGGNVNINFR IREPMVYPVD
FYYLMDVSYS MLDDLKSVQT LAQQLVATLQ ELTQGGTGSV KLGFGKFVDK VQSPMTQMTP
YKLQHPYGSS TDAPFLFRNV IDLTSDVDKF EQVLSKQNVS GNLDPPEGAL DAMLQVVKCK
ELIGWRGDAL RLLMVATESA FHFAGDGSGY LAGISRANDG RCHTGGDGIY VGAEEQDYPT
VNQVVRAVEE NSITPIFAIG KTYADMYKVG VLYHPEDVFR GSTWGILKKD SSNVVDLVRR
AYLDITGKQE IVTSNPDDSV LCPWYHVTRP GGAMEQLSVD GTLVGGLESG SKVYYNMSLY
ANRGACAGAT SCPVGDVIVK TRQYDDKLTI ATSVVSAFGC AATVIVNSPS CSGNGNFSCG
ICRCLPAWGG SSCSIPVEGK IGCLPLDGGA KCSGRGKCLN NRCQCDPGYR HGKSKIFGDF
CECDECPVRA GLVCSGNGRA VTGTGCSCDC VCDAGWEGSD CACASNTTTC MGLGGEICSG
FGQCVCGACV CDVTSGYSGP TCSDCVQNCP SCAAFKDCIQ CTMHQSGALA DSCVTSCNDE
VIEVEDIDEA SGEVLCAALD KIDNCKFYYS YKPSGSGMVF KAEVEKRCKP EYSLLIILWC
ILLFLLIGLI LLCCWRCCVY VIDKEESKNY K
//
