ID ITB1_SHEEP Reviewed; 798 AA.
AC B0FYY4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 100.
DE RecName: Full=Integrin beta-1 {ECO:0000250|UniProtKB:P05556};
DE AltName: Full=Fibronectin receptor subunit beta {ECO:0000250|UniProtKB:P05556};
DE AltName: Full=Integrin subunit beta-1 {ECO:0000312|EMBL:ABY71046.1};
DE AltName: Full=VLA-4 subunit beta;
DE AltName: CD_antigen=CD29 {ECO:0000250|UniProtKB:P05556};
DE Flags: Precursor;
GN Name=ITGB1 {ECO:0000250|UniProtKB:P05556};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1] {ECO:0000312|EMBL:ABY71046.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Du J., Gao S., Chang H., Cai X.;
RT "Molecular cloning and characteristics of cDNA encoding sheep beta-1
RT subunit as FMDV receptor.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and
CC alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1
CC and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-
CC E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-
CC 4/beta-1, alpha-5/beta-1, alpha-8/beta-1, alpha-10/beta-1, alpha-
CC 11/beta-1 and alpha-V/beta-1 are receptors for fibronectin. Alpha-
CC 4/beta-1 recognizes one or more domains within the alternatively
CC spliced CS-1 and CS-5 regions of fibronectin. Integrin alpha-5/beta-1
CC is a receptor for fibrinogen. Integrin alpha-1/beta-1, alpha-2/beta-1,
CC alpha-6/beta-1 and alpha-7/beta-1 are receptors for lamimin. Integrin
CC alpha-6/beta-1 (ITGA6:ITGB1) is present in oocytes and is involved in
CC sperm-egg fusion. Integrin alpha-4/beta-1 is a receptor for VCAM1 and
CC recognizes the sequence Q-I-D-S in VCAM1. Integrin alpha-9/beta-1 is a
CC receptor for VCAM1, cytotactin and osteopontin. It recognizes the
CC sequence 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. Beta-
CC 1 integrins recognize the sequence R-G-D in a wide array of ligands.
CC When associated with alpha-7/beta-1 integrin, regulates cell adhesion
CC and laminin matrix deposition. Involved in promoting endothelial cell
CC motility and angiogenesis. Involved in osteoblast compaction through
CC the fibronectin fibrillogenesis cell-mediated matrix assembly process
CC and the formation of mineralized bone nodules. May be involved in up-
CC regulation of the activity of kinases such as PKC via binding to KRT1.
CC Together with KRT1 and RACK1, serves as a platform for SRC activation
CC or inactivation. Plays a mechanistic adhesive role during telophase,
CC required for the successful completion of cytokinesis (By similarity).
CC ITGA4:ITGB1 binds to fractalkine (CX3CL1) and may act as its coreceptor
CC in CX3CR1-dependent fractalkine signaling. ITGA4:ITGB1 and ITGA5:ITGB1
CC bind to PLA2G2A via a site (site 2) which is distinct from the
CC classical ligand-binding site (site 1) and this induces integrin
CC conformational changes and enhanced ligand binding to site 1.
CC ITGA5:ITGB1 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-
CC D-dependent cell adhesion to FBN1. ITGA5:ITGB1 acts as a receptor for
CC fibronectin FN1 and mediates R-G-D-dependent cell adhesion to FN1 (By
CC similarity). ITGA5:ITGB1 is a receptor for IL1B and binding is
CC essential for IL1B signaling (By similarity). ITGA5:ITGB3 is a receptor
CC for soluble CD40LG and is required for CD40/CD40LG signaling (By
CC similarity). Plays an important role in myoblast differentiation and
CC fusion during skeletal myogenesis (By similarity). ITGA9:ITGB1 may play
CC a crucial role in SVEP1/polydom-mediated myoblast cell adhesion (By
CC similarity). Integrins ITGA9:ITGB1 and ITGA4:ITGB1 repress PRKCA-
CC mediated L-type voltage-gated channel Ca(2+) influx and ROCK-mediated
CC calcium sensitivity in vascular smooth muscle cells via their
CC interaction with SVEP1, thereby inhibit vasocontraction (By
CC similarity). {ECO:0000250|UniProtKB:P05556,
CC ECO:0000250|UniProtKB:P07228, ECO:0000250|UniProtKB:P09055}.
CC -!- SUBUNIT: Interacts with seprase FAP (seprase); the interaction occurs
CC at the cell surface of invadopodia membrane in a collagen-dependent
CC manner (By similarity). Heterodimer of an alpha and a beta subunit.
CC Beta-1 associates with either alpha-1, alpha-2, alpha-3, alpha-4,
CC alpha-5, alpha-6, alpha-7, alpha-8, alpha-9, alpha-10, alpha-11 or
CC alpha-V. ITGA6:ITGB1 is found in a complex with CD9; interaction takes
CC place in oocytes and is involved in sperm-egg fusion. Binds LGALS3BP
CC and NMRK2, when associated with alpha-7, but not with alpha-5.
CC Interacts with FLNA, FLNB, FLNC and RANBP9. Interacts with KRT1 in the
CC presence of RACK1 and SRC. Interacts with JAML; integrin alpha-4/beta-1
CC may regulate leukocyte to endothelial cells adhesion by controlling
CC JAML homodimerization. Interacts with RAB21. Interacts (via the
CC cytoplasmic region) with RAB25 (via the hypervariable C-terminal
CC region). Interacts with MYO10. Interacts with ITGB1BP1 (via C-terminal
CC region); the interaction is a prerequisite for focal adhesion
CC disassembly. Interacts with TLN1; the interaction is prevented by
CC competitive binding of ITGB1BP1. Interacts with ACAP1; required for
CC ITGB1 recycling. Interacts with ASAP3. Interacts with FERMT2; the
CC interaction is inhibited in presence of ITGB1BP1. Interacts with DAB2.
CC Interacts with FGR and HCK. Isoform 2 interacts with alpha-7A and
CC alpha-7B in adult skeletal muscle. Isoform 2 interacts with alpha-7B in
CC cardiomyocytes of adult heart. Interacts with EMP2; the interaction may
CC be direct or indirect and ITGB1 has a heterodimer form (By similarity).
CC ITGA5:ITGB1 interacts with CCN3 (By similarity). ITGA4:ITGB1 is found
CC in a ternary complex with CX3CR1 and CX3CL1 (By similarity).
CC ITGA5:ITGB1 interacts with FBN1 (By similarity). ITGA5:ITGB1 interacts
CC with IL1B. Interacts with MDK. ITGA4:ITGB1 interacts with MDK; this
CC interaction mediates MDK-induced osteoblast cells migration through PXN
CC phosphorylation. ITGA6:ITGB1 interacts with MDK; this interaction
CC mediates MDK-induced neurite-outgrowth (By similarity). ITGA5:ITGB1
CC interacts with ACE2 (By similarity). Interacts with TMEM182 and LAMB1
CC (By similarity). Interacts with tensin TNS3; TNS3 also interacts with
CC PEAK1, thus acting as an adapter molecule to bridge the association of
CC PEAK1 with ITGB1 (By similarity). Interacts with tensin TNS4; the
CC interaction displaces tensin TNS3 from the ITGB1 cytoplasmic tail and
CC promotes ITGB1 stability (By similarity). Integrin ITGA9:ITGB1
CC interacts with SPP1/OPN (via N-terminus) (By similarity). Integrin
CC ITGA9:ITGB1 interacts with TNC/TNFN3 (via the 3rd Fibronectin type-III
CC domain) (By similarity). Integrins ITGA4:ITGB1 and ITGA9:ITGB1 interact
CC with SVEP1 (via Sushi domain 21); thereby inhibit Ca(2+) intracellular
CC signaling and as a result repress vasocontraction (By similarity).
CC {ECO:0000250|UniProtKB:P05556, ECO:0000250|UniProtKB:P07228,
CC ECO:0000250|UniProtKB:P09055}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05556};
CC Single-pass type I membrane protein {ECO:0000255}. Cell projection,
CC invadopodium membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type
CC I membrane protein {ECO:0000255}. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein
CC {ECO:0000255}. Recycling endosome {ECO:0000250|UniProtKB:P05556}.
CC Melanosome {ECO:0000250|UniProtKB:P05556}. Cell projection,
CC lamellipodium {ECO:0000250|UniProtKB:P05556}. Cell projection, ruffle
CC {ECO:0000250|UniProtKB:P05556}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:P05556}. Note=Enriched preferentially at
CC invadopodia, cell membrane protrusions that correspond to sites of cell
CC invasion, in a collagen-dependent manner. Localized at plasma and
CC ruffle membranes in a collagen-independent manner. Colocalizes with
CC ITGB1BP1 and metastatic suppressor protein NME2 at the edge or
CC peripheral ruffles and lamellipodia during the early stages of cell
CC spreading on fibronectin or collagen. Translocates from peripheral
CC focal adhesions to fibrillar adhesions in an ITGB1BP1-dependent manner.
CC {ECO:0000250|UniProtKB:P05556}.
CC -!- DOMAIN: The VWFA domain (or beta I domain) contains three cation-
CC binding sites: the ligand-associated metal ion-binding site (LIMBS or
CC SyMBS), the metal ion-dependent adhesion site (MIDAS), and the adjacent
CC MIDAS site (ADMIDAS). This domain is also part of the ligand-binding
CC site. {ECO:0000250|UniProtKB:P05556}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000255}.
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DR EMBL; EU367988; ABY71046.1; -; mRNA.
DR RefSeq; NP_001107242.1; NM_001113770.1.
DR AlphaFoldDB; B0FYY4; -.
DR BMRB; B0FYY4; -.
DR SMR; B0FYY4; -.
DR STRING; 9940.ENSOARP00000018925; -.
DR GlyCosmos; B0FYY4; 10 sites, No reported glycans.
DR PaxDb; 9940-ENSOARP00000018925; -.
DR GeneID; 443141; -.
DR KEGG; oas:443141; -.
DR CTD; 3688; -.
DR eggNOG; KOG1226; Eukaryota.
DR OrthoDB; 5475862at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0034679; C:integrin alpha9-beta1 complex; 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:0098640; F:integrin binding involved in cell-matrix adhesion; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; ISS:UniProtKB.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0045445; P:myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0007520; P:myoblast fusion; ISS:UniProtKB.
DR GO; GO:0045906; P:negative regulation of vasoconstriction; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
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; 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:SF61; 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; PS00022; EGF_1; 2.
DR PROSITE; PS00243; INTEGRIN_BETA; 3.
PE 2: Evidence at transcript level;
KW Acetylation; Calcium; Cell adhesion; Cell junction; Cell membrane;
KW Cell projection; Disulfide bond; EGF-like domain; Endosome; Glycoprotein;
KW Integrin; Isopeptide bond; Magnesium; Membrane; Metal-binding; Myogenesis;
KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..798
FT /note="Integrin beta-1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000355118"
FT TOPO_DOM 21..246
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..76
FT /note="PSI"
FT /evidence="ECO:0000255"
FT DOMAIN 140..378
FT /note="VWFA"
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DOMAIN 439..501
FT /note="EGF-like 1"
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DOMAIN 502..554
FT /note="EGF-like 2"
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DOMAIN 555..591
FT /note="EGF-like 3"
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT DOMAIN 592..635
FT /note="EGF-like 4"
FT /evidence="ECO:0000250|UniProtKB:P05106"
FT REGION 75..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..213
FT /note="CX3CL1-binding"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT REGION 295..314
FT /note="CX3CL1-binding"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT REGION 383..465
FT /note="Interaction with TMEM182"
FT /evidence="ECO:0000250|UniProtKB:P07228"
FT REGION 762..767
FT /note="Signal for sorting from recycling endosomes;
FT interaction with ACAP1"
FT /evidence="ECO:0000250"
FT REGION 785..792
FT /note="Interaction with ITGB1BP1"
FT /evidence="ECO:0000250"
FT COMPBIAS 75..98
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 152
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="in MIDAS binding site"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /note="in ADMIDAS binding site"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT BINDING 154
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="in MIDAS binding site"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /note="in ADMIDAS binding site"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /note="in ADMIDAS binding site"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="in LIMBS binding site"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="in LIMBS binding site"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="in LIMBS binding site"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="in LIMBS binding site"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /note="in LIMBS binding site"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="in MIDAS binding site"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT BINDING 362
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /note="in ADMIDAS binding site"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT MOD_RES 777
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT MOD_RES 783
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT MOD_RES 789
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT MOD_RES 794
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 520
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..45
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 35..464
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 38..64
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 48..75
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 207..213
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 261..301
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 401..415
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 435..462
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 466..486
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 477..489
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 491..500
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 502..533
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 516..531
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 525..536
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 538..553
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 555..576
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 560..574
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 568..579
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 581..590
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 592..615
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 599..613
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 607..618
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 620..630
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 633..636
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 640..691
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 646..665
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 649..661
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT DISULFID 699..723
FT /evidence="ECO:0000250|UniProtKB:P05556"
FT CROSSLNK 794
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P05556"
SQ SEQUENCE 798 AA; 88110 MW; C8543466755D38BC 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
CHLENDMYTM SHYYDYPSIA HLVQKLSENN IQTIFAVTEE FQPVYKELKN LIPKSAVGTL
SANSGNVIQL IIDAYNSLSS EVILENSKLP EGVTINYKSY CKNGVNGTGE NGRKCSNISI
GDEVQFEISI TANKCPNKNS ETIKIKPLGF TEEVEIILQF ICECECQSEG 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 VLIGPALLLI WKLLMIIHDR REFAKFEKEK MNAKWDTGEN
PIYKSAVTTV VNPKYEGK
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