GenomeNet

Database: UniProt
Entry: P53712
LinkDB: P53712
Original site: P53712 
ID   ITB1_BOVIN              Reviewed;         798 AA.
AC   P53712; Q0PDN7; Q29RM8; Q8SQC0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 3.
DT   10-APR-2019, entry version 165.
DE   RecName: Full=Integrin beta-1;
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHARACTERIZATION AS A FMDV
RP   RECEPTOR.
RC   TISSUE=Tongue keratinocyte;
RX   PubMed=12551988; DOI=10.1128/JVI.77.4.2500-2511.2003;
RA   Duque H., Baxt B.;
RT   "Foot-and-mouth disease virus receptors: comparison of bovine alpha(V)
RT   integrin utilization by type A and O viruses.";
RL   J. Virol. 77:2500-2511(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Du J., Chang H., Cong G., Shao J., Lin T., Liu Z., Liu X., Cai X.,
RA   Xie Q.;
RT   "Molecular cloning and characteristics of bovine integrin beta 1
RT   cDNA.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 24-796 (ISOFORM 1), SUBCELLULAR
RP   LOCATION, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=7545439; DOI=10.1095/biolreprod53.1.153;
RA   Maclaren L.A., Wildeman A.G.;
RT   "Fibronectin receptors in preimplantation development: cloning,
RT   expression, and localization of the alpha 5 and beta 1 integrin
RT   subunits in bovine trophoblast.";
RL   Biol. Reprod. 53:153-165(1995).
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 (By similarity). Localized in trophoblast
CC       basement membrane and basolateral surfaces of uninucleate cells.
CC       {ECO:0000250|UniProtKB:P05556, ECO:0000269|PubMed:7545439}.
CC   -!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane, sarcolemma
CC       {ECO:0000250}. Cell junction {ECO:0000250}. Note=In cardiac
CC       muscle, isoform 2 is found in costameres and intercalated disks.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Beta-1A;
CC         IsoId=P53712-1; Sequence=Displayed;
CC       Name=2; Synonyms=Beta-1D;
CC         IsoId=P53712-2; Sequence=VSP_019224;
CC         Note=No experimental confirmation available.;
CC   -!- DEVELOPMENTAL STAGE: In the developing placenta, expressed during
CC       the morula (days 6-7) through the attachment stage (day 21).
CC       Expressed in the endoderm of day 14 blastocysts but then is down-
CC       regulated in these cells prior to implantation. Expressed on
CC       lateral surfaces of trophectodermal cells as attachment proceeded
CC       and is particularly intense in migrating binucleate cells at day
CC       24 of development. {ECO:0000269|PubMed:7545439}.
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}.
DR   EMBL; AF468058; AAL78037.1; -; mRNA.
DR   EMBL; DQ871214; ABH07895.1; -; mRNA.
DR   EMBL; BC114107; AAI14108.1; -; mRNA.
DR   EMBL; U10865; AAA80571.1; -; mRNA.
DR   PIR; I46059; I46059.
DR   RefSeq; NP_776793.1; NM_174368.3.
DR   RefSeq; XP_005214205.1; XM_005214148.3.
DR   RefSeq; XP_010809399.1; XM_010811097.2.
DR   UniGene; Bt.9973; -.
DR   SMR; P53712; -.
DR   STRING; 9913.ENSBTAP00000052015; -.
DR   PaxDb; P53712; -.
DR   PeptideAtlas; P53712; -.
DR   PRIDE; P53712; -.
DR   GeneID; 281876; -.
DR   KEGG; bta:281876; -.
DR   CTD; 3688; -.
DR   VGNC; VGNC:30324; ITGB1.
DR   eggNOG; KOG1226; Eukaryota.
DR   eggNOG; ENOG410XP60; LUCA.
DR   HOGENOM; HOG000252936; -.
DR   HOVERGEN; HBG006190; -.
DR   InParanoid; P53712; -.
DR   KO; K05719; -.
DR   OrthoDB; 473040at2759; -.
DR   TreeFam; TF105392; -.
DR   Reactome; R-BTA-1566948; Elastic fibre formation.
DR   Reactome; R-BTA-1566977; Fibronectin matrix formation.
DR   Reactome; R-BTA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR   Reactome; R-BTA-202733; Cell surface interactions at the vascular wall.
DR   Reactome; R-BTA-210991; Basigin interactions.
DR   Reactome; R-BTA-2129379; Molecules associated with elastic fibres.
DR   Reactome; R-BTA-216083; Integrin cell surface interactions.
DR   Reactome; R-BTA-3000157; Laminin interactions.
DR   Reactome; R-BTA-3000170; Syndecan interactions.
DR   Reactome; R-BTA-3000178; ECM proteoglycans.
DR   Reactome; R-BTA-445144; Signal transduction by L1.
DR   Reactome; R-BTA-446343; Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
DR   Reactome; R-BTA-8874081; MET activates PTK2 signaling.
DR   Reactome; R-BTA-8875513; MET interacts with TNS proteins.
DR   Proteomes; UP000009136; Chromosome 13.
DR   Bgee; ENSBTAG00000015910; Expressed in 9 organ(s), highest expression level in lung.
DR   ExpressionAtlas; P53712; baseline and differential.
DR   GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR   GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
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; ISS:UniProtKB.
DR   GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR   GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; IBA:GO_Central.
DR   GO; GO:0001968; F:fibronectin binding; IBA:GO_Central.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR   GO; GO:0001618; F:virus receptor activity; IEA:UniProtKB-KW.
DR   GO; GO:0033627; P:cell adhesion mediated by integrin; ISS:UniProtKB.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR   GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:UniProtKB.
DR   GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR   GO; GO:0010710; P:regulation of collagen catabolic process; ISS:UniProtKB.
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   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cell adhesion; Cell junction;
KW   Cell membrane; Cell projection; Complete proteome; Disulfide bond;
KW   Endosome; Glycoprotein; Host cell receptor for virus entry;
KW   Host-virus interaction; Integrin; Isopeptide bond; Magnesium;
KW   Membrane; Metal-binding; Phosphoprotein; Receptor; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix; Ubl conjugation.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   CHAIN        21    798       Integrin beta-1.
FT                                /FTId=PRO_0000174219.
FT   TOPO_DOM     21    728       Extracellular. {ECO:0000255}.
FT   TRANSMEM    729    749       Helical. {ECO:0000255}.
FT   TOPO_DOM    750    798       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      140    378       VWFA.
FT   REPEAT      466    515       I.
FT   REPEAT      516    559       II.
FT   REPEAT      560    598       III.
FT   REPEAT      599    635       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      466    635       Cysteine-rich tandem repeats.
FT   REGION      762    767       Signal for sorting from recycling
FT                                endosomes; interaction with ACAP1.
FT                                {ECO:0000250}.
FT   REGION      785    792       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   METAL       362    362       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   MOD_RES     777    777       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P05556}.
FT   MOD_RES     783    783       Phosphotyrosine.
FT                                {ECO:0000250|UniProtKB:P05556}.
FT   MOD_RES     785    785       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P05556}.
FT   MOD_RES     789    789       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P05556}.
FT   MOD_RES     794    794       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    481    481       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    520    520       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    584    584       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    669    669       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     27     45       {ECO:0000250}.
FT   DISULFID     35    464       {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    462       {ECO:0000250}.
FT   DISULFID    466    691       {ECO:0000250}.
FT   DISULFID    477    489       {ECO:0000250}.
FT   DISULFID    486    525       {ECO:0000250}.
FT   DISULFID    491    500       {ECO:0000250}.
FT   DISULFID    502    516       {ECO:0000250}.
FT   DISULFID    531    536       {ECO:0000250}.
FT   DISULFID    533    568       {ECO:0000250}.
FT   DISULFID    538    553       {ECO:0000250}.
FT   DISULFID    555    560       {ECO:0000250}.
FT   DISULFID    574    579       {ECO:0000250}.
FT   DISULFID    576    607       {ECO:0000250}.
FT   DISULFID    581    590       {ECO:0000250}.
FT   DISULFID    592    599       {ECO:0000250}.
FT   DISULFID    613    618       {ECO:0000250}.
FT   DISULFID    615    661       {ECO:0000250}.
FT   DISULFID    620    630       {ECO:0000250}.
FT   DISULFID    633    636       {ECO:0000250}.
FT   DISULFID    640    649       {ECO:0000250}.
FT   DISULFID    646    723       {ECO:0000250}.
FT   DISULFID    665    699       {ECO:0000250}.
FT   CROSSLNK    794    794       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO1);
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:P05556}.
FT   VAR_SEQ     786    798       AVTTVVNPKYEGK -> PINNFKNPNYGRKAGL (in
FT                                isoform 2). {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_019224.
FT   CONFLICT    217    217       F -> S (in Ref. 2; ABH07895).
FT                                {ECO:0000305}.
FT   CONFLICT    247    247       S -> P (in Ref. 2; ABH07895).
FT                                {ECO:0000305}.
FT   CONFLICT    268    268       R -> W (in Ref. 1; AAL78037 and 4;
FT                                AAA80571). {ECO:0000305}.
FT   CONFLICT    281    281       G -> V (in Ref. 1; AAL78037 and 4;
FT                                AAA80571). {ECO:0000305}.
FT   CONFLICT    321    321       H -> Y (in Ref. 2; ABH07895).
FT                                {ECO:0000305}.
FT   CONFLICT    390    390       P -> A (in Ref. 4; AAA80571).
FT                                {ECO:0000305}.
FT   CONFLICT    595    595       D -> G (in Ref. 4; AAA80571).
FT                                {ECO:0000305}.
FT   CONFLICT    668    668       F -> L (in Ref. 4; AAA80571).
FT                                {ECO:0000305}.
FT   CONFLICT    691    691       C -> Y (in Ref. 1; AAL78037).
FT                                {ECO:0000305}.
FT   CONFLICT    709    709       G -> V (in Ref. 1; AAL78037).
FT                                {ECO:0000305}.
FT   CONFLICT    778    778       G -> Q (in Ref. 3; AAI14108).
FT                                {ECO:0000305}.
SQ   SEQUENCE   798 AA;  88094 MW;  87D506B5AE5E23CF CRC64;
     MNLQLIFWIG LISSVCCVFG QADENRCLKA NAKSCGECIQ AGPNCGWCTN STFLQEGMPT
     SARCDDLEAL KKKGCHPNDI ENPRGSKDIK KNKNVTNRSK GTAEKLQPED ITQIQPQQLV
     LQLRSGEPQT FTLKFKRAED YPIDLYYLMD LSYSMKDDLE NVKSLGTDLM NEMRRITSDF
     RIGFGSFVEK TVMPYISTTP AKLRNPCTNE QNCTSPFSYK NVLSLTDKGE VFNELVGKQR
     ISGNLDSPEG GFDAIMQVAV CGSLIGWRNV TRLLVFSTDA GFHFAGDGKL GGIVLPNDGQ
     CHLENDVYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN LIPKSAVGTL
     SANSSNVIQL IIDAYNSLSS EVILENSKLP EGVTINYKSY CKNGVNGTGE NGRKCSNISI
     GDEVQFEISI TANKCPNKNS ETIKIKPLGF TEEVEIILQF ICECECQGEG IPGSPKCHDG
     NGTFECGACR CNEGRVGRHC ECSTDEVNSE DMDAYCRKEN SSEICSNNGE CVCGQCVCRK
     RDNTNEIYSG KFCECDNFNC DRSNGLICGG NGVCKCRVCE CNPNYTGSAC DCSLDTTSCM
     AVNGQICNGR GVCECGACKC TDPKFQGPTC EMCQTCLGVC AEHKECVQCR AFNKGEKKDT
     CAQECSHFNI TKVENRDKLP QPGQVDPLSH CKEKDVDDCW FYFTYSVNGN NEATVHVVET
     PECPTGPDII PIVAGVVAGI VLIGLALLLI WKLLMIIHDR REFAKFEKEK MNAKWDTGEN
     PIYKSAVTTV VNPKYEGK
//
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