GenomeNet

Database: UniProt
Entry: P49134
LinkDB: P49134
Original site: P49134 
ID   ITB1_RAT                Reviewed;         799 AA.
AC   P49134; A2RRT8;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   13-FEB-2019, entry version 176.
DE   RecName: Full=Integrin beta-1;
DE   AltName: Full=Beta oligodendroglia;
DE            Short=Beta OL;
DE   AltName: Full=Fibronectin receptor subunit beta;
DE   AltName: Full=VLA-4 subunit beta;
DE   AltName: CD_antigen=CD29;
DE   Flags: Precursor;
GN   Name=Itgb1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Oligodendrocyte;
RX   PubMed=7541764; DOI=10.1016/0378-1119(94)00911-B;
RA   Malek-Hedayat S., Rome L.H.;
RT   "Cloning and sequence of the cDNA encoding the rat oligodendrocyte
RT   integrin beta 1 subunit.";
RL   Gene 158:287-290(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-
CC       1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-
CC       1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated
CC       sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-
CC       3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-
CC       10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for
CC       fibronectin. Alpha-4/beta-1 recognizes one or more domains within
CC       the alternatively spliced CS-1 and CS-5 regions of fibronectin.
CC       Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin
CC       alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1
CC       are receptors for lamimin. Integrin alpha-6/beta-1 (ITGA6:ITGB1)
CC       is present in oocytes and is involved in sperm-egg fusion.
CC       Integrin alpha-4/beta-1 is a receptor for VCAM1 and recognizes the
CC       sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a receptor
CC       for VCAM1, cytotactin and osteopontin. It recognizes the sequence
CC       A-E-I-D-G-I-E-L in cytotactin. Integrin alpha-3/beta-1 is a
CC       receptor for epiligrin, thrombospondin and CSPG4. Integrin alpha-
CC       3/beta-1 provides a docking site for FAP (seprase) at invadopodia
CC       plasma membranes in a collagen-dependent manner and hence may
CC       participate in the adhesion, formation of invadopodia and matrix
CC       degradation processes, promoting cell invasion. Alpha-3/beta-1 may
CC       mediate with LGALS3 the stimulation by CSPG4 of endothelial cells
CC       migration. Integrin alpha-V/beta-1 is a receptor for vitronectin.
CC       Beta-1 integrins recognize the sequence R-G-D in a wide array of
CC       ligands. When associated with alpha-7/beta-1 integrin, regulates
CC       cell adhesion and laminin matrix deposition. Involved in promoting
CC       endothelial cell motility and angiogenesis. Involved in osteoblast
CC       compaction through the fibronectin fibrillogenesis cell-mediated
CC       matrix assembly process and the formation of mineralized bone
CC       nodules. May be involved in up-regulation of the activity of
CC       kinases such as PKC via binding to KRT1. Together with KRT1 and
CC       RACK1, serves as a platform for SRC activation or inactivation.
CC       Plays a mechanistic adhesive role during telophase, required for
CC       the successful completion of cytokinesis (By similarity).
CC       ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its
CC       coreceptor in CX3CR1-dependent fractalkine signaling. ITGA4:ITGB1
CC       and ITGA5:ITGB1 bind to PLA2G2A via a site (site 2) which is
CC       distinct from the classical ligand-binding site (site 1) and this
CC       induces integrin conformational changes and enhanced ligand
CC       binding to site 1. ITGA5:ITGB1 acts as a receptor for fibrillin-1
CC       (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1.
CC       ITGA5:ITGB1 is a receptor for IL1B and binding is essential for
CC       IL1B signaling (By similarity). {ECO:0000250|UniProtKB:P05556,
CC       ECO:0000250|UniProtKB:P09055}.
CC   -!- SUBUNIT: Interacts with seprase FAP (seprase); the interaction
CC       occurs at the cell surface of invadopodia membrane in a collagen-
CC       dependent manner (By similarity). Heterodimer of an alpha and a
CC       beta subunit. Beta-1 associates with either alpha-1, alpha-2,
CC       alpha-3, alpha-4, alpha-5, alpha-6, alpha-7, alpha-8, alpha-9,
CC       alpha-10, alpha-11 or alpha-V (By similarity). ITGA6:ITGB1 is
CC       found in a complex with CD9; interaction takes place in oocytes
CC       and is involved in sperm-egg fusion (By similarity). Binds
CC       LGALS3BP and NMRK2, when associated with alpha-7, but not with
CC       alpha-5. Interacts with FLNA, FLNB, FLNC and RANBP9. Interacts
CC       with KRT1 in the presence of RACK1 and SRC. Interacts with JAML;
CC       integrin alpha-4/beta-1 may regulate leukocyte to endothelial
CC       cells adhesion by controlling JAML homodimerization. Interacts
CC       with RAB21. Interacts (via the cytoplasmic region) with RAB25 (via
CC       the hypervariable C-terminal region). Interacts with MYO10.
CC       Interacts with ITGB1BP1 (via C-terminal region); the interaction
CC       is a prerequisite for focal adhesion disassembly. Interacts with
CC       TLN1; the interaction is prevented by competitive binding of
CC       ITGB1BP1. Interacts with ACAP1; required for ITGB1 recycling.
CC       Interacts with ASAP3. Interacts with FERMT2; the interaction is
CC       inhibited in presence of ITGB1BP1. Interacts with DAB2. Interacts
CC       with FGR and HCK. Isoform 2 interacts with alpha-7A and alpha-7B
CC       in adult skeletal muscle. Isoform 2 interacts with alpha-7B in
CC       cardiomyocytes of adult heart. Interacts with EMP2; the
CC       interaction may be direct or indirect and ITGB1 has an heterodimer
CC       form (By similarity). ITGA5:ITGB1 interacts with CCN3 (By
CC       similarity). ITGA4:ITGB1 is found in a ternary complex with CX3CR1
CC       and CX3CL1 (By similarity). ITGA5:ITGB1 interacts with FBN1 (By
CC       similarity). ITGA5:ITGB1 interacts with IL1B (By similarity).
CC       {ECO:0000250|UniProtKB:P05556, ECO:0000250|UniProtKB:P09055}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane
CC       protein {ECO:0000255}. Cell projection, invadopodium membrane
CC       {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane
CC       protein {ECO:0000255}. Cell projection, ruffle membrane
CC       {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane
CC       protein {ECO:0000255}. Recycling endosome
CC       {ECO:0000250|UniProtKB:P05556}. Melanosome
CC       {ECO:0000250|UniProtKB:P05556}. Cell projection, lamellipodium
CC       {ECO:0000250|UniProtKB:P05556}. Cell projection, ruffle
CC       {ECO:0000250|UniProtKB:P05556}. Cell junction, focal adhesion
CC       {ECO:0000250|UniProtKB:P05556}. Cell surface
CC       {ECO:0000250|UniProtKB:P05556}. Note=Enriched preferentially at
CC       invadopodia, cell membrane protrusions that correspond to sites of
CC       cell invasion, in a collagen-dependent manner. Localized at plasma
CC       and ruffle membranes in a collagen-independent manner. Colocalizes
CC       with ITGB1BP1 and metastatic suppressor protein NME2 at the edge
CC       or peripheral ruffles and lamellipodia during the early stages of
CC       cell spreading on fibronectin or collagen. Translocates from
CC       peripheral focal adhesions to fibrillar adhesions in an ITGB1BP1-
CC       dependent manner. {ECO:0000250|UniProtKB:P05556}.
CC   -!- PTM: The cysteine residues are involved in intrachain disulfide
CC       bonds. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI31846.1; Type=Frameshift; Positions=442, 443, 447; Evidence={ECO:0000305};
DR   EMBL; U12309; AAA86669.1; -; mRNA.
DR   EMBL; BC131845; AAI31846.1; ALT_FRAME; mRNA.
DR   PIR; JC4126; JC4126.
DR   RefSeq; NP_058718.2; NM_017022.2.
DR   UniGene; Rn.25733; -.
DR   ProteinModelPortal; P49134; -.
DR   SMR; P49134; -.
DR   BioGrid; 246668; 7.
DR   CORUM; P49134; -.
DR   IntAct; P49134; 4.
DR   MINT; P49134; -.
DR   STRING; 10116.ENSRNOP00000014785; -.
DR   iPTMnet; P49134; -.
DR   PhosphoSitePlus; P49134; -.
DR   jPOST; P49134; -.
DR   PaxDb; P49134; -.
DR   PRIDE; P49134; -.
DR   GeneID; 24511; -.
DR   KEGG; rno:24511; -.
DR   UCSC; RGD:2927; rat.
DR   CTD; 3688; -.
DR   RGD; 2927; Itgb1.
DR   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   HOGENOM; HOG000252936; -.
DR   HOVERGEN; HBG006190; -.
DR   InParanoid; P49134; -.
DR   KO; K05719; -.
DR   OrthoDB; 473040at2759; -.
DR   PhylomeDB; P49134; -.
DR   TreeFam; TF105392; -.
DR   PRO; PR:P49134; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:RGD.
DR   GO; GO:0005912; C:adherens junction; IDA:RGD.
DR   GO; GO:0005604; C:basement membrane; IDA:RGD.
DR   GO; GO:0009986; C:cell surface; IDA:RGD.
DR   GO; GO:0005911; C:cell-cell junction; IDA:RGD.
DR   GO; GO:0043197; C:dendritic spine; IDA:SynGO.
DR   GO; GO:0005925; C:focal adhesion; IDA:RGD.
DR   GO; GO:0097386; C:glial cell projection; IDA:ARUK-UCL.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0030056; C:hemidesmosome; IDA:RGD.
DR   GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR   GO; GO:0034667; C:integrin alpha3-beta1 complex; IDA:RGD.
DR   GO; GO:0034679; C:integrin alpha9-beta1 complex; IDA:RGD.
DR   GO; GO:0008305; C:integrin complex; IDA:RGD.
DR   GO; GO:0071438; C:invadopodium membrane; ISS:UniProtKB.
DR   GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IDA:RGD.
DR   GO; GO:0045121; C:membrane raft; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
DR   GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IDA:RGD.
DR   GO; GO:0051393; F:alpha-actinin binding; IDA:RGD.
DR   GO; GO:0005518; F:collagen binding; IDA:RGD.
DR   GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; IBA:GO_Central.
DR   GO; GO:0001968; F:fibronectin binding; IDA:RGD.
DR   GO; GO:0005178; F:integrin binding; IMP:RGD.
DR   GO; GO:0019900; F:kinase binding; IPI:RGD.
DR   GO; GO:0043236; F:laminin binding; IDA:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0002020; F:protease binding; IPI:RGD.
DR   GO; GO:0019904; F:protein domain specific binding; IDA:RGD.
DR   GO; GO:0046982; F:protein heterodimerization activity; IMP:RGD.
DR   GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR   GO; GO:0005102; F:signaling receptor binding; IPI:RGD.
DR   GO; GO:0070830; P:bicellular tight junction assembly; IMP:RGD.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; IGI:ARUK-UCL.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0030030; P:cell projection organization; IMP:ARUK-UCL.
DR   GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR   GO; GO:0071479; P:cellular response to ionizing radiation; IEP:RGD.
DR   GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
DR   GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR   GO; GO:0071305; P:cellular response to vitamin D; IEP:RGD.
DR   GO; GO:0097368; P:establishment of Sertoli cell barrier; IEP:RGD.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0030032; P:lamellipodium assembly; IMP:ARUK-UCL.
DR   GO; GO:0060135; P:maternal process involved in female pregnancy; IEP:RGD.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR   GO; GO:0031345; P:negative regulation of cell projection organization; IMP:RGD.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:RGD.
DR   GO; GO:0006909; P:phagocytosis; IMP:ARUK-UCL.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
DR   GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IMP:RGD.
DR   GO; GO:0045807; P:positive regulation of endocytosis; IMP:RGD.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:RGD.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:RGD.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:UniProtKB.
DR   GO; GO:0032594; P:protein transport within lipid bilayer; IMP:RGD.
DR   GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR   GO; GO:0010710; P:regulation of collagen catabolic process; ISS:UniProtKB.
DR   GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IMP:RGD.
DR   GO; GO:0014823; P:response to activity; IEP:RGD.
DR   GO; GO:0042493; P:response to drug; IEP:RGD.
DR   GO; GO:0034698; P:response to gonadotropin; IEP:RGD.
DR   GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR   GO; GO:0071559; P:response to transforming growth factor beta; IEP:RGD.
DR   GO; GO:0001894; P:tissue homeostasis; IMP:RGD.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR040622; I-EGF_1.
DR   InterPro; IPR027071; Integrin_beta-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; PTHR10082; 1.
DR   PANTHER; PTHR10082:SF28; PTHR10082:SF28; 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; SSF53300; SSF53300; 1.
DR   SUPFAM; SSF69179; SSF69179; 1.
DR   SUPFAM; SSF69687; SSF69687; 1.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS00243; INTEGRIN_BETA; 3.
PE   2: Evidence at transcript level;
KW   Acetylation; Cell adhesion; Cell junction; Cell membrane;
KW   Cell projection; Complete proteome; Disulfide bond; Endosome;
KW   Glycoprotein; Integrin; Isopeptide bond; Magnesium; Membrane;
KW   Metal-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix; Ubl conjugation.
FT   SIGNAL        1     20       {ECO:0000250}.
FT   CHAIN        21    798       Integrin beta-1.
FT                                /FTId=PRO_0000016336.
FT   TOPO_DOM     21    729       Extracellular. {ECO:0000255}.
FT   TRANSMEM    730    752       Helical. {ECO:0000255}.
FT   TOPO_DOM    753    799       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      140    378       VWFA.
FT   REPEAT      467    516       I.
FT   REPEAT      517    560       II.
FT   REPEAT      561    599       III.
FT   REPEAT      600    636       IV.
FT   REGION      207    213       CX3CL1-binding.
FT                                {ECO:0000250|UniProtKB:P05556}.
FT   REGION      295    314       CX3CL1-binding.
FT                                {ECO:0000250|UniProtKB:P05556}.
FT   REGION      467    636       Cysteine-rich tandem repeats.
FT   REGION      763    768       Signal for sorting from recycling
FT                                endosomes; interaction with ACAP1.
FT                                {ECO:0000250}.
FT   REGION      786    793       Interaction with ITGB1BP1. {ECO:0000250}.
FT   METAL       152    152       Magnesium. {ECO:0000250}.
FT   METAL       154    154       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       156    156       Calcium 1. {ECO:0000250}.
FT   METAL       157    157       Calcium 1. {ECO:0000250}.
FT   METAL       189    189       Calcium 2. {ECO:0000250}.
FT   METAL       244    244       Calcium 2. {ECO:0000250}.
FT   METAL       246    246       Calcium 2. {ECO:0000250}.
FT   METAL       248    248       Calcium 2; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       249    249       Calcium 2. {ECO:0000250}.
FT   METAL       249    249       Magnesium. {ECO:0000250}.
FT   MOD_RES     778    778       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P05556}.
FT   MOD_RES     784    784       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P05556}.
FT   MOD_RES     786    786       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P05556}.
FT   MOD_RES     790    790       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P05556}.
FT   MOD_RES     795    795       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P05556}.
FT   CARBOHYD     50     50       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     94     94       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     97     97       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    212    212       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    269    269       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    363    363       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    406    406       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    417    417       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    482    482       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    521    521       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    585    585       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    670    670       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     27     45       {ECO:0000250}.
FT   DISULFID     35    465       {ECO:0000250}.
FT   DISULFID     38     75       {ECO:0000250}.
FT   DISULFID     48     64       {ECO:0000250}.
FT   DISULFID    207    213       {ECO:0000250}.
FT   DISULFID    261    301       {ECO:0000250}.
FT   DISULFID    401    415       {ECO:0000250}.
FT   DISULFID    435    463       {ECO:0000250}.
FT   DISULFID    467    692       {ECO:0000250}.
FT   DISULFID    478    490       {ECO:0000250}.
FT   DISULFID    487    526       {ECO:0000250}.
FT   DISULFID    492    501       {ECO:0000250}.
FT   DISULFID    503    517       {ECO:0000250}.
FT   DISULFID    532    537       {ECO:0000250}.
FT   DISULFID    534    569       {ECO:0000250}.
FT   DISULFID    539    554       {ECO:0000250}.
FT   DISULFID    556    561       {ECO:0000250}.
FT   DISULFID    575    580       {ECO:0000250}.
FT   DISULFID    577    608       {ECO:0000250}.
FT   DISULFID    582    591       {ECO:0000250}.
FT   DISULFID    593    600       {ECO:0000250}.
FT   DISULFID    614    619       {ECO:0000250}.
FT   DISULFID    616    662       {ECO:0000250}.
FT   DISULFID    621    631       {ECO:0000250}.
FT   DISULFID    634    637       {ECO:0000250}.
FT   DISULFID    641    650       {ECO:0000250}.
FT   DISULFID    647    724       {ECO:0000250}.
FT   DISULFID    666    700       {ECO:0000250}.
FT   CROSSLNK    795    795       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO1);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:P05556}.
FT   CONFLICT     76     76       H -> Q (in Ref. 2; AAI31846).
FT                                {ECO:0000305}.
FT   CONFLICT    711    711       K -> N (in Ref. 2; AAI31846).
FT                                {ECO:0000305}.
SQ   SEQUENCE   799 AA;  88495 MW;  F4475202EB8A3EA6 CRC64;
     MNLQLVFWIG LISLICSVFG QTDKNRCLKA NAKSCGECIQ AGPNCGWCTN TTFLQEGMPT
     SARCDDLEAL KKKGCHPSDI ENPRGSQTIK KNKNVTNRSK GMAEKLRPED ITQIQPQQLL
     LKLRSGEPQK FTLKFKRAED YPIDLYYLMD LSYSMKDDLE NVKSLGTDLM NEMRRITSDF
     RIGFGSFVEK TVMPYISTTP AKLRNPCTSE QNCTSPFSYK NVLSLTDRGE FFNELVGQQR
     ISGNLDSPEG GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ
     CHLENNVYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN LIPKSAVGTL
     SGNSSNVIQL IIDAYNSLSS EVILENSKLP DGVTINYKSY CKNGVNGTGE NGRKCSNISI
     GDEVQFEISI TANKCPNKES ENQLKLNPLG FTEEVEVVLQ FICKCNCQSH GIPASPKCHE
     GNGTFECGAC RCNEGRVGRH CECSTDEVNS EDMDAYCRKE NSSEICSNNG ECVCGQCVCR
     KRENTNEIYS GKFCECDNFN CDRSNGLICG GNGVCRCRVC ECYPNYTGSA CDCSLDTVPC
     VATNGQICNG RGICECGACK CTDPKFQGPT CETCQTCLGV CAEHKECVQC RAFNKGEKKD
     TCAQECSHFN LTKVESREKL PQPVQVDPVT HCKEKDIDDC WFYFTYSVNS KGEAHVHVVE
     TPDCPTGPDI IPIVAGVVAG IVLIGLALLL IWKLLMIIHD RREFAKFEKE KMNAKWDTGE
     NPIYKSAVTT VVNPKYEGK
//
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