ITBP2_PIG
ID ITBP2_PIG Reviewed; 346 AA.
AC Q462R2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Integrin beta-1-binding protein 2;
DE AltName: Full=Melusin;
GN Name=ITGB1BP2;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Pan G., Xiong Z.Y.;
RT "Identification of Sus scrofa gene encoded for integrin beta 1 binding
RT protein (melusin) 2.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role during maturation and/or organization of
CC muscles cells. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with beta-1 integrin subunit. This interaction is
CC regulated by divalent cations, and it occurs only in absence of calcium
CC (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The tail domain binds to the cytoplasmic domain of both
CC integrin beta-1a and beta-1d isoforms. The presence of Ca(2+) ions does
CC not prevent binding of a fragment consisting of the second cysteine
CC rich repeat and the tail domain but prevents the binding of the full-
CC length protein (By similarity). {ECO:0000250}.
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DR EMBL; DQ002920; AAY57557.1; -; mRNA.
DR RefSeq; NP_001028181.1; NM_001033009.3.
DR AlphaFoldDB; Q462R2; -.
DR SMR; Q462R2; -.
DR STRING; 9823.ENSSSCP00000023164; -.
DR PaxDb; Q462R2; -.
DR PeptideAtlas; Q462R2; -.
DR PRIDE; Q462R2; -.
DR GeneID; 613129; -.
DR KEGG; ssc:613129; -.
DR CTD; 26548; -.
DR eggNOG; KOG1667; Eukaryota.
DR InParanoid; Q462R2; -.
DR OrthoDB; 1163528at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007051; CHORD_dom.
DR InterPro; IPR039790; CHORD_protein.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR PANTHER; PTHR12621; PTHR12621; 1.
DR Pfam; PF04968; CHORD; 2.
DR Pfam; PF04969; CS; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51401; CHORD; 2.
DR PROSITE; PS51203; CS; 1.
PE 2: Evidence at transcript level;
KW Metal-binding; Reference proteome; Repeat; SH3-binding; Zinc.
FT CHAIN 1..346
FT /note="Integrin beta-1-binding protein 2"
FT /id="PRO_0000084269"
FT DOMAIN 5..64
FT /note="CHORD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT DOMAIN 150..209
FT /note="CHORD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT DOMAIN 216..305
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT REGION 70..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 28..31
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 70..78
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 159..162
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT MOTIF 173..176
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 235..238
FT /note="SH2-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 76..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..346
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 5
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 10
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 187
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00734"
SQ SEQUENCE 346 AA; 38037 MW; 7D01AA19B7D35F47 CRC64;
MSLLCHNKGC GQHFDPQTNL PDSCCHHPGV PVFHDALKGW SCCRKRTVDF SEFLNIKGCT
VGPHCAEKLP EAPQPEGPAT SSSLLEQKPP NTIPKSAETL RRERPKSDLP PKLLPLNISQ
ALEMALEQKE LDQEPGAGLD SSLIQTGASC QNPGCDAVYQ GSESDATPCT YHPGAPRFHE
GMKSWSCCGI QTLDFGVFLA QPGCRVGRHD WGKKLLASCR HDWHQTDSLV VVTVYGQIPL
PAFNWVEASQ TELHIHIVFD GNRVFQAQVK LWGVVNVEQS SVSLMPSRVE ISLVKADPGF
WAQLEHPDAL AEKSKSGVGL EMDEEESEDS DDDLSWTEEE EEAMGE
