ID M3XH97_LATCH Unreviewed; 818 AA.
AC M3XH97;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=ITGB1 {ECO:0000313|Ensembl:ENSLACP00000022103.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000022103.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000022103.1}
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}. 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 EMBL; AFYH01247537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01247538; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01247539; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01247540; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01247541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01247542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01247543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; M3XH97; -.
DR Ensembl; ENSLACT00000025552.1; ENSLACP00000022103.1; ENSLACG00000001067.2.
DR GeneTree; ENSGT01090000259987; -.
DR HOGENOM; CLU_011772_2_1_1; -.
DR Proteomes; UP000008672; Unassembled WGS sequence.
DR Bgee; ENSLACG00000001067; Expressed in post-anal tail muscle and 6 other cell types or tissues.
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; 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: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 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 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:UP000008672};
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}.
FT SIGNAL 1..39
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 40..818
FT /note="Integrin beta"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004043617"
FT TRANSMEM 749..771
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 45..95
FT /note="PSI"
FT /evidence="ECO:0000259|SMART:SM00423"
FT DOMAIN 53..483
FT /note="Integrin beta subunit VWA"
FT /evidence="ECO:0000259|SMART:SM00187"
FT DOMAIN 658..748
FT /note="Integrin beta subunit tail"
FT /evidence="ECO:0000259|SMART:SM01242"
FT DOMAIN 772..818
FT /note="Integrin beta subunit cytoplasmic"
FT /evidence="ECO:0000259|SMART:SM01241"
FT REGION 95..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 46..483
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 54..64
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 57..94
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 67..83
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 225..231
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 279..319
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 453..710
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 481..485
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 496..508
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 505..544
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 510..519
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 521..535
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 550..555
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 552..587
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 557..572
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 574..579
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 593..598
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 595..626
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 600..609
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 611..618
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 632..637
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 634..679
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 639..648
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 651..654
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 658..667
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 664..743
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 683..718
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 818 AA; 90998 MW; 7484828F6F5798A9 CRC64;
MFLTFFVMFC LRIYSSFKLQ MDCRLHFLIA FCLMCHVFAQ QDGSECLKAN AKSCGECIQA
GPSCGWCTKL DFLQQGEPTS ARCDDLAALK TKGCPESQIE NPRGSKNITN NKEVTNRVGN
TQKPKPEDIT QIQPQRLELH LRSGEPQTFE LKFKRAEDYP IDLYYLMDLS YSMKDDLENV
KSLGTALMVE MRKITSDFRI GFGSFVEKTV MPYISTTPAK LLNPCTSDQN CTSPFSYKNV
LNLTSNGNLF NELVGKQRIS GNLDSPEGGF DAIMQVAVCG EQIGWRNVTR LLVFSTDAGF
HFAGDGKLGG IVLPNDGKCH LENNMYTMSH YYDYPSIAHL VQKLSDNNIQ TIFAVTQEFE
PVYKELQNLI PKSAVGTLSS NSSNVIQLII DAYNSLSSEV ILENSKLPEG VTISYKSYCK
NGINGTGENG RKCSNISIGD EVKFDVSITA QKCPKNGHEE VIKLKPLGFT EEVEIVLKFI
CECDCHNEGI PNSDECNYGN GTFECGACRC NEGRIGRLCE CSTDEVNSED MDASCRKDNS
SEICSNNGDC ICGECVCKKR ENPNEVYSGK YCECDNFNCD RSNGLICGGN GVCKCRKCEC
YENFTGSACD CSMDTKPCES MYRQICNGRG ECICGRCKCS DKFQGPTCEM CPTCPGVCAE
HKECVQCRAF NKGEKKDVCN EACGKAFKLV IVEDRLQLPQ PGQLEALTHC KEKDVDDCWF
YFTYAVNNTN NDYVVHVVKK PDCPAGPEII PIVAGVVAGI VLIGLALLLI WKLLMIIHDR
REFAKFEKEK MNAKWDTGEN PIYKSAVTTV VNPKYEGK
//
