ID A0A384ARG3_BALAS Unreviewed; 801 AA.
AC A0A384ARG3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=ITGB1 {ECO:0000313|RefSeq:XP_007189912.1,
GN ECO:0000313|RefSeq:XP_007189913.1, ECO:0000313|RefSeq:XP_007189914.1,
GN ECO:0000313|RefSeq:XP_007189915.1};
OS Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS (Balaenoptera davidsoni).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC Balaenopteridae; Balaenoptera.
OX NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_007189913.1};
RN [1] {ECO:0000313|RefSeq:XP_007189912.1, ECO:0000313|RefSeq:XP_007189913.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_007189912.1,
RC ECO:0000313|RefSeq:XP_007189913.1};
RG RefSeq;
RL Submitted (JAN-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, ruffle {ECO:0000256|ARBA:ARBA00004466}. Endosome
CC {ECO:0000256|ARBA:ARBA00004177}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Recycling endosome
CC {ECO:0000256|ARBA:ARBA00004172}.
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_007189912.1; XM_007189850.1.
DR RefSeq; XP_007189913.1; XM_007189851.1.
DR RefSeq; XP_007189914.1; XM_007189852.1.
DR RefSeq; XP_007189915.1; XM_007189853.1.
DR AlphaFoldDB; A0A384ARG3; -.
DR STRING; 310752.A0A384ARG3; -.
DR GeneID; 103008019; -.
DR KEGG; bacu:103008019; -.
DR CTD; 3688; -.
DR InParanoid; A0A384ARG3; -.
DR OrthoDB; 5475862at2759; -.
DR Proteomes; UP000261681; Unplaced.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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; IPR016201; PSI.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR PANTHER; PTHR10082:SF61; 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 Pfam; PF17205; PSI_integrin; 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 SMART; SM00423; PSI; 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 Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU000633};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR002512-1};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU000633};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000261681};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, 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}; Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..801
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036545015"
FT TRANSMEM 729..751
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..76
FT /note="PSI"
FT /evidence="ECO:0000259|SMART:SM00423"
FT DOMAIN 34..464
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 640..728
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 752..798
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT REGION 75..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 207..213
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 261..301
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 435..691
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 462..466
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 477..489
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 486..525
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 491..500
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 502..516
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 531..536
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 533..568
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 538..553
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 555..560
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 574..579
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 576..607
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 581..590
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 592..599
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 613..618
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 615..661
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 620..630
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 633..636
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 640..649
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 646..723
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 665..699
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 801 AA; 88628 MW; 84828B0A0E7C5DE2 CRC64;
MNLQLIFWIG LISSVCYVFG QTDENRCLKA NAKSCGECIQ AGPNCGWCTN STFLQEGMPT
SARCDDLEAL KKKGCHPDDI ENPRGSKDIK KNKNVTNRSK GTAEKLQPED ITQIQPQQLV
LQLRSGEPQT FTLKFKRAED YPIDLYYLMD LSYSMKDDLE NVKSLGTDLM NEMRRITSDF
RIGFGSFVEK TVMPYISTTP AKLRNPCTSE QNCTSPFSYK NVLSLTDKGE VFNELVGKQR
ISGNLDSPEG GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ
CHLENDVYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN LIPKSAVGTL
SANSSNVIQL IIDAYNSLSS EVILENSKLP EGVTINYKSY CKNGVNGTGE NGRKCSNISI
GDEVQFEISV TSNKCPNKNS ETIKIKPLGF TEEVEIILQF ICECECQSEG IPGSPKCHDG
NGTFECGACR CNEGRVGRHC ECSTDEVNSE DMDAYCRKEN SSEICSNNGE CVCGQCVCRK
RDNTNEIYSG KFCECDNFNC DRSNGLICGG NGVCKCRVCE CNPNYTGSAC DCSLDTTSCT
AVNGQICNGR GVCECGACKC TDPKFQGPTC EMCQTCLGVC AEHKECVQCR AFNKGEKKDT
CAQECSHFNI TKVENRDKLP QPGQVDPLSH CKEKDVDDCW FYFTYSVNGN NEATVHVVET
PECPTGPDII PIVAGVVAGI VLIGLALLLI WKLLMIIHDR REFAKFEKEK MNAKWDTQEN
PIYKSPINNF KNPNYGRKAG L
//
