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Integrin beta-1 (Beta oligodendroglia) (Beta OL) (Fibronectin receptor subunit beta) (VLA-4 subunit beta) (CD antigen CD29)

 ITB1_RAT                Reviewed;         799 AA.
P49134; A2RRT8;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
22-NOV-2017, entry version 166.
RecName: Full=Integrin beta-1;
AltName: Full=Beta oligodendroglia;
Short=Beta OL;
AltName: Full=Fibronectin receptor subunit beta;
AltName: Full=VLA-4 subunit beta;
AltName: CD_antigen=CD29;
Flags: Precursor;
Name=Itgb1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Oligodendrocyte;
PubMed=7541764; DOI=10.1016/0378-1119(94)00911-B;
Malek-Hedayat S., Rome L.H.;
"Cloning and sequence of the cDNA encoding the rat oligodendrocyte
integrin beta 1 subunit.";
Gene 158:287-290(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-
1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-
1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated
sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-
3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-
10/beta-1, alpha-11/beta-1 and alpha-V/beta-1 are receptors for
fibronectin. Alpha-4/beta-1 recognizes one or more domains within
the alternatively spliced CS-1 and CS-5 regions of fibronectin.
Integrin alpha-5/beta-1 is a receptor for fibrinogen. Integrin
alpha-1/beta-1, alpha-2/beta-1, alpha-6/beta-1 and alpha-7/beta-1
are receptors for lamimin. Integrin alpha-4/beta-1 is a receptor
for VCAM1 and recognizes the sequence Q-I-D-S in VCAM1. Integrin
alpha-9/beta-1 is a receptor for VCAM1, cytotactin and
osteopontin. It recognizes the sequence A-E-I-D-G-I-E-L in
cytotactin. Integrin alpha-3/beta-1 is a receptor for epiligrin,
thrombospondin and CSPG4. Integrin alpha-3/beta-1 provides a
docking site for FAP (seprase) at invadopodia plasma membranes in
a collagen-dependent manner and hence may participate in the
adhesion, formation of invadopodia and matrix degradation
processes, promoting cell invasion. Alpha-3/beta-1 may mediate
with LGALS3 the stimulation by CSPG4 of endothelial cells
migration. Integrin alpha-V/beta-1 is a receptor for vitronectin.
Beta-1 integrins recognize the sequence R-G-D in a wide array of
ligands. When associated with alpha-7/beta-1 integrin, regulates
cell adhesion and laminin matrix deposition. Involved in promoting
endothelial cell motility and angiogenesis. Involved in osteoblast
compaction through the fibronectin fibrillogenesis cell-mediated
matrix assembly process and the formation of mineralized bone
nodules. May be involved in up-regulation of the activity of
kinases such as PKC via binding to KRT1. Together with KRT1 and
RACK1, serves as a platform for SRC activation or inactivation.
Plays a mechanistic adhesive role during telophase, required for
the successful completion of cytokinesis. ITGA4:ITGB1 binds to
fractalkine (CX3CL1) and may act as its coreceptor in CX3CR1-
dependent fractalkine signaling. ITGA4:ITGB1 and ITGA5:ITGB1 bind
to PLA2G2A via a site (site 2) which is distinct from the
classical ligand-binding site (site 1) and this induces integrin
conformational changes and enhanced ligand binding to site 1.
ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates
R-G-D-dependent cell adhesion to FBN1.
{ECO:0000250|UniProtKB:P05556}.
-!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-1
associates with either alpha-1, alpha-2, alpha-3, alpha-4, alpha-
5, alpha-6, alpha-7, alpha-8, alpha-9, alpha-10, alpha-11 or
alpha-V. Binds LGALS3BP and NMRK2, when associated with alpha-7,
but not with alpha-5. Interacts with FLNA, FLNB, FLNC and RANBP9.
Interacts with KRT1 in the presence of RACK1 and SRC. Interacts
with JAML; integrin alpha-4/beta-1 may regulate leukocyte to
endothelial cells adhesion by controlling JAML homodimerization.
Interacts with RAB21. Interacts (via the cytoplasmic region) with
RAB25 (via the hypervariable C-terminal region). Interacts with
FGR and HCK. Interacts with MYO10. Interacts with DAB2. Interacts
with ITGB1BP1 (via C-terminal region); the interaction is a
prerequisite for focal adhesion disassembly. Interacts with
FERMT2; the interaction is inhibited in presence of ITGB1BP1.
Interacts with TLN1; the interaction is prevented by competitive
binding of ITGB1BP1. Interacts with ACAP1; required for ITGB1
recycling. Interacts with ASAP3. Interacts with seprase FAP
(seprase); the interaction occurs at the cell surface of
invadopodia membrane in a collagen-dependent manner. Interacts
with EMP2; the interaction may be direct or indirect and ITGB1 has
a heterodimer form (By similarity). ITGA5:ITGB1 interacts with
NOV. ITGA4:ITGB1 is found in a ternary complex with CX3CR1 and
CX3CL1. ITGA5:ITGB1 interacts with FBN1.
{ECO:0000250|UniProtKB:P05556, ECO:0000250|UniProtKB:P09055}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane
protein {ECO:0000255}. Cell projection, invadopodium membrane
{ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane
protein {ECO:0000255}. Cell projection, ruffle membrane
{ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane
protein {ECO:0000255}. Recycling endosome
{ECO:0000250|UniProtKB:P05556}. Melanosome
{ECO:0000250|UniProtKB:P05556}. Cell projection, lamellipodium
{ECO:0000250|UniProtKB:P05556}. Cell projection, ruffle
{ECO:0000250|UniProtKB:P05556}. Cell junction, focal adhesion
{ECO:0000250|UniProtKB:P05556}. Cell surface
{ECO:0000250|UniProtKB:P05556}. Note=Enriched preferentially at
invadopodia, cell membrane protrusions that correspond to sites of
cell invasion, in a collagen-dependent manner. Localized at plasma
and ruffle membranes in a collagen-independent manner. Colocalizes
with ITGB1BP1 and metastatic suppressor protein NME2 at the edge
or peripheral ruffles and lamellipodia during the early stages of
cell spreading on fibronectin or collagen. Translocates from
peripheral focal adhesions to fibrillar adhesions in an ITGB1BP1-
dependent manner. {ECO:0000250|UniProtKB:P05556}.
-!- PTM: The cysteine residues are involved in intrachain disulfide
bonds. {ECO:0000250}.
-!- SIMILARITY: Belongs to the integrin beta chain family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAI31846.1; Type=Frameshift; Positions=442, 443, 447; Evidence={ECO:0000305};
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EMBL; U12309; AAA86669.1; -; mRNA.
EMBL; BC131845; AAI31846.1; ALT_FRAME; mRNA.
PIR; JC4126; JC4126.
RefSeq; NP_058718.2; NM_017022.2.
UniGene; Rn.25733; -.
ProteinModelPortal; P49134; -.
SMR; P49134; -.
BioGrid; 246668; 6.
CORUM; P49134; -.
IntAct; P49134; 4.
MINT; MINT-122445; -.
STRING; 10116.ENSRNOP00000014785; -.
iPTMnet; P49134; -.
PhosphoSitePlus; P49134; -.
PaxDb; P49134; -.
PRIDE; P49134; -.
GeneID; 24511; -.
KEGG; rno:24511; -.
UCSC; RGD:2927; rat.
CTD; 3688; -.
RGD; 2927; Itgb1.
eggNOG; KOG1226; Eukaryota.
eggNOG; ENOG410XP60; LUCA.
HOGENOM; HOG000252936; -.
HOVERGEN; HBG006190; -.
InParanoid; P49134; -.
KO; K05719; -.
PhylomeDB; P49134; -.
TreeFam; TF105392; -.
PRO; PR:P49134; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0001669; C:acrosomal vesicle; IDA:RGD.
GO; GO:0005912; C:adherens junction; IDA:RGD.
GO; GO:0005604; C:basement membrane; IDA:RGD.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0005911; C:cell-cell junction; IDA:RGD.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0043197; C:dendritic spine; IDA:SynGO.
GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0030175; C:filopodium; ISO:RGD.
GO; GO:0005925; C:focal adhesion; IDA:RGD.
GO; GO:0030056; C:hemidesmosome; IDA:RGD.
GO; GO:0034665; C:integrin alpha1-beta1 complex; ISO:RGD.
GO; GO:0034680; C:integrin alpha10-beta1 complex; ISO:RGD.
GO; GO:0034681; C:integrin alpha11-beta1 complex; ISO:RGD.
GO; GO:0034666; C:integrin alpha2-beta1 complex; ISO:RGD.
GO; GO:0034667; C:integrin alpha3-beta1 complex; IDA:RGD.
GO; GO:0034677; C:integrin alpha7-beta1 complex; ISO:RGD.
GO; GO:0034679; C:integrin alpha9-beta1 complex; IDA:RGD.
GO; GO:0008305; C:integrin complex; IDA:RGD.
GO; GO:0014704; C:intercalated disc; ISO:RGD.
GO; GO:0071438; C:invadopodium membrane; ISS:UniProtKB.
GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0035748; C:myelin sheath abaxonal region; ISO:RGD.
GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
GO; GO:0005886; C:plasma membrane; ISO:RGD.
GO; GO:0045211; C:postsynaptic membrane; IDA:SynGO.
GO; GO:0043235; C:receptor complex; ISO:RGD.
GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0042383; C:sarcolemma; ISO:RGD.
GO; GO:0045202; C:synapse; ISO:RGD.
GO; GO:0097060; C:synaptic membrane; ISO:RGD.
GO; GO:0003779; F:actin binding; IDA:RGD.
GO; GO:0051393; F:alpha-actinin binding; IDA:RGD.
GO; GO:0045296; F:cadherin binding; ISO:RGD.
GO; GO:0050839; F:cell adhesion molecule binding; ISO:RGD.
GO; GO:0005518; F:collagen binding; IDA:RGD.
GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; ISO:RGD.
GO; GO:0001968; F:fibronectin binding; IDA:RGD.
GO; GO:0005178; F:integrin binding; IMP:RGD.
GO; GO:0019900; F:kinase binding; IPI:RGD.
GO; GO:0043236; F:laminin binding; IDA:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042277; F:peptide binding; IDA:RGD.
GO; GO:0002020; F:protease binding; IPI:RGD.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0019904; F:protein domain specific binding; IDA:RGD.
GO; GO:0046982; F:protein heterodimerization activity; IMP:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0004872; F:receptor activity; IEA:InterPro.
GO; GO:0005102; F:receptor binding; IPI:RGD.
GO; GO:0048675; P:axon extension; ISO:RGD.
GO; GO:0071711; P:basement membrane organization; ISO:RGD.
GO; GO:0070830; P:bicellular tight junction assembly; IMP:RGD.
GO; GO:0007161; P:calcium-independent cell-matrix adhesion; ISO:RGD.
GO; GO:0055007; P:cardiac muscle cell differentiation; ISO:RGD.
GO; GO:0048738; P:cardiac muscle tissue development; ISO:RGD.
GO; GO:0007155; P:cell adhesion; IDA:RGD.
GO; GO:0033627; P:cell adhesion mediated by integrin; ISS:UniProtKB.
GO; GO:0001708; P:cell fate specification; ISO:RGD.
GO; GO:0016477; P:cell migration; ISO:RGD.
GO; GO:0002042; P:cell migration involved in sprouting angiogenesis; ISO:RGD.
GO; GO:0033631; P:cell-cell adhesion mediated by integrin; ISO:RGD.
GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
GO; GO:0031589; P:cell-substrate adhesion; ISO:RGD.
GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:RGD.
GO; GO:0071479; P:cellular response to ionizing radiation; IEP:RGD.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
GO; GO:0071305; P:cellular response to vitamin D; IEP:RGD.
GO; GO:0048813; P:dendrite morphogenesis; ISO:RGD.
GO; GO:0021943; P:formation of radial glial scaffolds; ISO:RGD.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISO:RGD.
GO; GO:0008354; P:germ cell migration; ISO:RGD.
GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:RGD.
GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
GO; GO:0007229; P:integrin-mediated signaling pathway; IDA:RGD.
GO; GO:0007159; P:leukocyte cell-cell adhesion; ISO:RGD.
GO; GO:0050901; P:leukocyte tethering or rolling; ISO:RGD.
GO; GO:0060135; P:maternal process involved in female pregnancy; IEP:RGD.
GO; GO:0048333; P:mesodermal cell differentiation; ISO:RGD.
GO; GO:2000811; P:negative regulation of anoikis; ISO:RGD.
GO; GO:0045596; P:negative regulation of cell differentiation; ISO:RGD.
GO; GO:0031345; P:negative regulation of cell projection organization; IMP:RGD.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:RGD.
GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:RGD.
GO; GO:0035024; P:negative regulation of Rho protein signal transduction; ISO:RGD.
GO; GO:0031175; P:neuron projection development; ISO:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:RGD.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IMP:RGD.
GO; GO:0045807; P:positive regulation of endocytosis; IMP:RGD.
GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:RGD.
GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:RGD.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:RGD.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISS:UniProtKB.
GO; GO:0032594; P:protein transport within lipid bilayer; IMP:RGD.
GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
GO; GO:0010710; P:regulation of collagen catabolic process; ISS:UniProtKB.
GO; GO:0008277; P:regulation of G-protein coupled receptor protein signaling pathway; IMP:RGD.
GO; GO:0014823; P:response to activity; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0034698; P:response to gonadotropin; IEP:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0071559; P:response to transforming growth factor beta; IEP:RGD.
GO; GO:0045214; P:sarcomere organization; ISO:RGD.
GO; GO:0001894; P:tissue homeostasis; IMP:RGD.
GO; GO:0008542; P:visual learning; ISO:RGD.
Gene3D; 1.20.5.100; -; 1.
Gene3D; 1.20.5.630; -; 1.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
InterPro; IPR013111; EGF_extracell.
InterPro; IPR027071; Integrin_beta-1.
InterPro; IPR033760; Integrin_beta_N.
InterPro; IPR015812; Integrin_bsu.
InterPro; IPR014836; Integrin_bsu_cyt_dom.
InterPro; IPR037076; Integrin_bsu_cyt_dom_sf.
InterPro; IPR012896; Integrin_bsu_tail.
InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
InterPro; IPR002369; Integrin_bsu_VWA.
InterPro; IPR032695; Integrin_dom_sf.
InterPro; IPR016201; PSI.
InterPro; IPR036465; vWFA_dom_sf.
PANTHER; PTHR10082; PTHR10082; 1.
PANTHER; PTHR10082:SF28; PTHR10082:SF28; 1.
Pfam; PF07974; EGF_2; 1.
Pfam; PF08725; Integrin_b_cyt; 1.
Pfam; PF07965; Integrin_B_tail; 1.
Pfam; PF00362; Integrin_beta; 1.
Pfam; PF17205; PSI_integrin; 1.
PIRSF; PIRSF002512; Integrin_B; 1.
PRINTS; PR01186; INTEGRINB.
SMART; SM00187; INB; 1.
SMART; SM01241; Integrin_b_cyt; 1.
SMART; SM01242; Integrin_B_tail; 1.
SMART; SM00423; PSI; 1.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF69179; SSF69179; 1.
SUPFAM; SSF69687; SSF69687; 1.
PROSITE; PS00022; EGF_1; 2.
PROSITE; PS00243; INTEGRIN_BETA; 3.
2: Evidence at transcript level;
Acetylation; Cell adhesion; Cell junction; Cell membrane;
Cell projection; Complete proteome; Disulfide bond; Endosome;
Glycoprotein; Integrin; Isopeptide bond; Magnesium; Membrane;
Metal-binding; Phosphoprotein; Receptor; Reference proteome; Repeat;
Signal; Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 20 {ECO:0000250}.
CHAIN 21 798 Integrin beta-1.
/FTId=PRO_0000016336.
TOPO_DOM 21 729 Extracellular. {ECO:0000255}.
TRANSMEM 730 752 Helical. {ECO:0000255}.
TOPO_DOM 753 799 Cytoplasmic. {ECO:0000255}.
DOMAIN 140 378 VWFA.
REPEAT 467 516 I.
REPEAT 517 560 II.
REPEAT 561 599 III.
REPEAT 600 636 IV.
REGION 207 213 CX3CL1-binding.
{ECO:0000250|UniProtKB:P05556}.
REGION 295 314 CX3CL1-binding.
{ECO:0000250|UniProtKB:P05556}.
REGION 467 636 Cysteine-rich tandem repeats.
REGION 763 768 Signal for sorting from recycling
endosomes; interaction with ACAP1.
{ECO:0000250}.
REGION 786 793 Interaction with ITGB1BP1. {ECO:0000250}.
METAL 152 152 Magnesium. {ECO:0000250}.
METAL 154 154 Calcium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 156 156 Calcium 1. {ECO:0000250}.
METAL 157 157 Calcium 1. {ECO:0000250}.
METAL 189 189 Calcium 2. {ECO:0000250}.
METAL 244 244 Calcium 2. {ECO:0000250}.
METAL 246 246 Calcium 2. {ECO:0000250}.
METAL 248 248 Calcium 2; via carbonyl oxygen.
{ECO:0000250}.
METAL 249 249 Calcium 2. {ECO:0000250}.
METAL 249 249 Magnesium. {ECO:0000250}.
MOD_RES 778 778 Phosphothreonine.
{ECO:0000250|UniProtKB:P05556}.
MOD_RES 784 784 Phosphotyrosine.
{ECO:0000250|UniProtKB:P05556}.
MOD_RES 786 786 Phosphoserine.
{ECO:0000250|UniProtKB:P05556}.
MOD_RES 790 790 Phosphothreonine.
{ECO:0000250|UniProtKB:P05556}.
MOD_RES 795 795 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P05556}.
CARBOHYD 50 50 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 94 94 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 97 97 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 212 212 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 269 269 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 363 363 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 406 406 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 417 417 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 482 482 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 521 521 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 585 585 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 670 670 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 27 45 {ECO:0000250}.
DISULFID 35 465 {ECO:0000250}.
DISULFID 38 75 {ECO:0000250}.
DISULFID 48 64 {ECO:0000250}.
DISULFID 207 213 {ECO:0000250}.
DISULFID 261 301 {ECO:0000250}.
DISULFID 401 415 {ECO:0000250}.
DISULFID 435 463 {ECO:0000250}.
DISULFID 467 692 {ECO:0000250}.
DISULFID 478 490 {ECO:0000250}.
DISULFID 487 526 {ECO:0000250}.
DISULFID 492 501 {ECO:0000250}.
DISULFID 503 517 {ECO:0000250}.
DISULFID 532 537 {ECO:0000250}.
DISULFID 534 569 {ECO:0000250}.
DISULFID 539 554 {ECO:0000250}.
DISULFID 556 561 {ECO:0000250}.
DISULFID 575 580 {ECO:0000250}.
DISULFID 577 608 {ECO:0000250}.
DISULFID 582 591 {ECO:0000250}.
DISULFID 593 600 {ECO:0000250}.
DISULFID 614 619 {ECO:0000250}.
DISULFID 616 662 {ECO:0000250}.
DISULFID 621 631 {ECO:0000250}.
DISULFID 634 637 {ECO:0000250}.
DISULFID 641 650 {ECO:0000250}.
DISULFID 647 724 {ECO:0000250}.
DISULFID 666 700 {ECO:0000250}.
CROSSLNK 795 795 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:P05556}.
CONFLICT 76 76 H -> Q (in Ref. 2; AAI31846).
{ECO:0000305}.
CONFLICT 711 711 K -> N (in Ref. 2; AAI31846).
{ECO:0000305}.
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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