ID A0AAD6BRV9_9TELE Unreviewed; 2237 AA.
AC A0AAD6BRV9;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 08-OCT-2025, entry version 8.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN ORFNames=JOQ06_009949 {ECO:0000313|EMBL:KAJ4947920.1};
OS Pogonophryne albipinna.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Notothenioidei; Pogonophryne.
OX NCBI_TaxID=1090488 {ECO:0000313|EMBL:KAJ4947920.1, ECO:0000313|Proteomes:UP001219934};
RN [1] {ECO:0000313|EMBL:KAJ4947920.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SGF0006 {ECO:0000313|EMBL:KAJ4947920.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAJ4947920.1};
RA Jo E.;
RT "Chromosome-level genome of Pogonophryne albipinna.";
RL Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Interacts with
CC FLNB. Interacts with HAX1. ITGAV:ITGB6 interacts with FBN1. ITGAV:ITGB6
CC interacts with TGFB1. {ECO:0000256|ARBA:ARBA00046864}.
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251,
CC ECO:0000256|RuleBase:RU000633}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family.
CC {ECO:0000256|ARBA:ARBA00007449, ECO:0000256|RuleBase:RU000633}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAJ4947920.1}.
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DR EMBL; JAPTMU010000002; KAJ4947920.1; -; Genomic_DNA.
DR Proteomes; UP001219934; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:TreeGrafter.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0034685; C:integrin alphav-beta6 complex; IEA:TreeGrafter.
DR GO; GO:0005178; F:integrin binding; IEA:TreeGrafter.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:TreeGrafter.
DR GO; GO:0016477; P:cell migration; IEA:TreeGrafter.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:TreeGrafter.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:TreeGrafter.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd00037; CLECT; 7.
DR CDD; cd00062; FN2; 1.
DR FunFam; 2.10.10.10:FF:000001; Fibronectin 1a isoform 1; 1.
DR FunFam; 1.20.5.100:FF:000004; Integrin beta; 1.
DR FunFam; 2.10.25.10:FF:000043; Integrin beta; 1.
DR FunFam; 2.10.25.10:FF:000075; Integrin beta; 1.
DR FunFam; 2.10.25.10:FF:000076; Integrin beta; 1.
DR FunFam; 3.30.1680.10:FF:000002; Integrin beta; 1.
DR FunFam; 3.40.50.410:FF:000002; Integrin beta; 1.
DR FunFam; 2.80.10.50:FF:000039; Secretory phospholipase A2 receptor; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR Gene3D; 2.10.10.10; Fibronectin, type II, collagen-binding; 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; 3.10.100.10; Mannose-Binding Protein A, subunit A; 8.
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; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR040622; EGF_integrin_1.
DR InterPro; IPR057073; EGF_integrin_2.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR033760; Integrin_beta_N.
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; IPR057243; Integrin_I-EGF_CS.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR PANTHER; PTHR10082:SF11; INTEGRIN BETA-6; 1.
DR Pfam; PF24562; CysR_MRC2_N; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF23105; EGF_integrin; 1.
DR Pfam; PF00040; fn2; 1.
DR Pfam; PF18372; I-EGF_1; 1.
DR Pfam; PF08725; Integrin_b_cyt; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF00059; Lectin_C; 8.
DR Pfam; PF17205; PSI_integrin; 1.
DR PRINTS; PR00013; FNTYPEII.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00034; CLECT; 8.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00187; INB; 1.
DR SMART; SM01241; Integrin_b_cyt; 1.
DR SMART; SM01242; Integrin_B_tail; 1.
DR SMART; SM00423; PSI; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 8.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF69687; Integrin beta tail domain; 1.
DR SUPFAM; SSF69179; Integrin domains; 1.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF103575; Plexin repeat; 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 8.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 1.
DR PROSITE; PS00243; I_EGF_1; 1.
DR PROSITE; PS52047; I_EGF_2; 3.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
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 Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00479}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU000633};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP001219934};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 2171..2194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 934..982
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 1000..1114
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1143..1264
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1288..1400
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1444..1566
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1589..1707
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1733..1858
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1889..1995
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 2027..2150
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DISULFID 939..965
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 953..980
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
SQ SEQUENCE 2237 AA; 250760 MW; B5017399C01A53EC CRC64;
MKAEDAPEGS CSAGSAAVTC DECLQLSSHC AWCTQENFTD WFSVSERCDT LDNLLEKGCA
RDQLEFPVSV GQILQDHPLG KKTINDNTTQ ISPQKMALKL RPGTQVTFQV KIQHTEDYPV
DVYYLMDLSA SMIDDLVMIK DLGTSLSKEM AKLTSKFRMG FGSFVEKPVL PFIKITEEEL
ANPCRGVGFH CLPTFGYKHV LSLTSSTDKF NEIIAMQRVS ANIDVPECGF DAVMQAAVCG
DKIGWRNDSM RLLVFVSDAD SHFGMDSKMA GIVIPNDGQC HLDVNNEYSM STVLEYPTLG
QLIDKVVENN ILLIFAVTEG EQNNYKNYAH LIPGATVGVV AKDSRNILEL IVTAYKELRS
EIELEVLGDT EELHMSFTAI CPNGTVFHDQ KNCSNIKPGE TVVFNVTVEL PECLSGVRHF
SLKPVGLQDS LEVELESLCS CDCRHTPEAN SSQCTEGQGA FQCGVCVCHP GFLGAECECN
EESALLSNCL ANNESEICSG QGQCYCGECV CHASTFGRIY GPYCECNNYS CVRFRGELCG
GHGVCDCGEC HCESGWTGEY CNCSSSTDAC MSEDGALCSG QGRCECGHCV CSVPGASGDK
CEKCPTCGDA CTSARDCVEC HLQDDDDAEL CDQKCSVPKI SINTTADYDK SPSMKCKLMM
EDECWVSFKV VGGETGITAY DLLKFGCPEP PNIPMIILGV SLSIVCIGLI LLAVWKVLVS
VHDRKEVAKF EAERAKAKWQ TGTNPLFKSS TSTFKNVTYK KTEREKIITL AVLLARGCMC
VNEEDDEVLE KKQLMEFYKK GMFILESEPL KRCIKVDRSN LVLEDCERPT RHMLWKWVSR
HRLFNLGTST CLGLNISDTT QPLGTFECDM ALPVLWWRCS GNMLYGASQW KVAVAGRLVV
VKKNTYHEWK RYNTPKGGPC SYPYEDIHTL LGNAHGMPCA LPFKYNNKWY SECTTEGRED
HLPWCATTTR YDEAEKWGFC PVQDTSCERF WESNQELRAC YQFNLYTILT WSQALSTCQA
QGGNLLSITS LAEHRYITDR MASVGAMVWI GLNHLKDRRG WQWSDGAPLS LVNFTKTLPA
SPLKDDRQCG VYNSATEGHW QSLSCESALP YICKKTPNDT RIAEPLENWQ YIQTECANGW
WPHNGFCYRL LSETEAGSWE ESSRACVSQG ANLTSLHSLS EVEMLLSLLT NSSGDSEEAW
IGLWKQEFSP TVEWSDGSPV TLTFWHQYHP PPNLTDASLC VKADRKEGNW LIGSCDERLP
AVCRKESQNP NHQPGTWDEG CPEGWKRHGH SCFTVTSHEQ NYEDAVMGYY CRAPLLTVEN
RFEQAFVNSL LSESETNSSK YYWIGLSDQE KGGEYSWLPL NGSSLPLTFT NWNKHQPVST
GGCVAMSGGP ALGHWEVHDC KSHKALSVCK QSISSYHDVQ LPEHHIDAYA PCPPGWESHA
GMLHCFKVLH DEKVLMKRSW VEADFFCQAL GAQLASFLHY EEQVFVKLLL STMFQGTEGR
WFWVGFNKRD PEHPGAWEWS DGSPVETSFI EDKNDEDDRR DCAVYSDLTN ALMPQPCEAK
HEWICKMSRG DKLMKPYWYN EQSEPWVFYH GAEYLLAKQP FDWDSVSLAC QMMGAYLLSV
HSREELHFVK ERLHRLSLGP TEWWIGLSTG QPGEGARWSD KTEVDFENWA DRGAGGGASN
RMCVTMSSST GKWSESKCGD INGYVCKRKT VSVVETPREP HYIGGCPEKW LYFGHKCLLL
HIIDSPKEGK SWKDARSICS SFDGSLVAIE DEIEQAYITM LLQGSSVGVW IGLRDEDTMK
WTNGKTVSYT NWSPIEPKSY LTENEWLSGF TDEPLCTVLS NNHNFHLTGK WYDEKCSESG
YGFICQKSQD TSKPPTHSYL HPLPANIEYS SRSYKVVSGN MSWYDAMHMC IEKDSDLVSV
TDAYHQAFLT VLVNRLAVPH WIGLYSQDSG INYQWSDGSD TVYTHWDADE DDDDFVTGEC
VYMDVTGGWR RADCETPLPG ALCHVPPPSS KPFISYELEC PSTWVKFGHG CYSFEPVVQK
LTFEESREHC RQKVNTSDVL TIESETENRF VLEQLWTSGF LHHTVWLGMY FNIDTDSMAW
VDGSPIDYTN WLNQAPDPKL LTADACVTTR VVDGVWHLSQ CNERLGFVCK TTSDIITEVE
VEPLNGLHHG VVPAAVLVAV LIFALLAGAM WFVYKRSASR FRRLPTLGSA YYRQTSSQAT
ESDGNVLITD LEAPSGE
//
