ID I3N1R0_ICTTR Unreviewed; 1141 AA.
AC I3N1R0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Collagen type XXVIII alpha 1 chain {ECO:0000313|Ensembl:ENSSTOP00000018306.2};
GN Name=COL28A1 {ECO:0000313|Ensembl:ENSSTOP00000018306.2};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000018306.2, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000018306.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AGTP01068069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01068070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01068071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01068072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01068073; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01068074; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01068075; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3N1R0; -.
DR STRING; 43179.ENSSTOP00000018306; -.
DR Ensembl; ENSSTOT00000026598.2; ENSSTOP00000018306.2; ENSSTOG00000023884.2.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000161647; -.
DR HOGENOM; CLU_009158_0_0_1; -.
DR InParanoid; I3N1R0; -.
DR OrthoDB; 2906665at2759; -.
DR TreeFam; TF331207; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd01472; vWA_collagen; 1.
DR CDD; cd01450; vWFA_subfamily_ECM; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 2.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF878; COLLAGEN ALPHA-1(XXVIII) CHAIN; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR Pfam; PF00092; VWA; 2.
DR PRINTS; PR00453; VWFADOMAIN.
DR SMART; SM00131; KU; 1.
DR SMART; SM00327; VWA; 2.
DR SUPFAM; SSF57362; BPTI-like; 1.
DR SUPFAM; SSF53300; vWA-like; 2.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR PROSITE; PS50234; VWFA; 2.
PE 4: Predicted;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1141
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012090592"
FT DOMAIN 48..226
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 797..975
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1088..1138
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT REGION 241..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..599
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..753
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1141 AA; 118409 MW; 7A4123E40D1621B3 CRC64;
MWSRYFAFCL LLLPIFMSQT VYGQRKKGTK SNLLARKNDL QDSVCFIDVL FIVDSSESSK
LVLFDKQKNF VDSLSDKIFQ LTPGHSLKYD IKLAALQFSS SVQIDPPFSS WKDLQTFKQR
VKSMNFIGQG TFSYYAISNA TRLLKREGRK DGVKVVLLMT DGMDHPKNPD VQSISESARN
AGISFITIGL LTVNKTKLHL ISGDAPSEPI LLLSDPTIVD KIRDRLDILF EKKCERKICE
CEKGDPGEPG PPGKHGNPGI KGERGPKGNP GDAQKGETGE RGPGGIPGYK GDKGEPGECG
KPGIKGDKGS PGPSGPKGPK GLQGIGGPPG DPGPKGFQGN KGEPGPPGPY GPPGAPGIGQ
QGIKGERGQE GRTGAPGPIG VGQPGQPGPR GPEGAPGERG LPGEGFPGPK GEKGSEGPIG
PQGLQGLSIK GDKGDLGPVG PQGPMGIPGT GSQGEQGIQG PIGPPGPQGP PGQGLPGSKG
EVGPIGPTGP RGPVGIGAQG PKGEPGSKGS PGQTGEPGED GAAGKKGEAG LPGTRGPEGP
PGKGQPGPKG DEGKKGSKGN QGHMGFPGPA GPKGEQGIMG PFGMPGPSIP GPPGPKGDRG
GPGMPGFKGE PGLFIRGPKG AQGPQGPKGA PGLKGDGYPG VSGPRGLPGP PGPMGLRGVG
DTGAKGEPGV RGPPGPAGPR GIGTQGPKGD IGQKGLPGPP GPPGYGSQGI KGEQGPQGFP
GPKGTRGQGL PGQKGEHGEQ GDVGKKGEKG ELGDPGSPGK QGLQGPKGDA GLTREDIIEL
IIKICGCGRK CKETPLELVF VIDSSESVGL NNFQIIQNFV KSLADRISVD LATARIGIIN
YSHKVEIVAD LRQFSSKDDF KLAVDNMQYL GEGTYTATAL QAANDMFKSA RPGIKKVALV
ITDGQTDSRD KKNLTEVVKE AKDTGVEIFV IGVVKKSDPN FDMFLKEMNL IATDPQHVYH
FDDFLTLLDT LKQKLSTKIC EDFPSYLAKV FGSSSSQPEF GVLGEELGVS TPEPPEEISE
SFSVPGPKHE ENEPPEPTWA HRLVVTSSSE AAATLGPLLS TLESMKTRTP SPGLILHQDN
LVHKDPRCLE DLKPGNCVDY VVRWYYDKQV NSCARFWYSG CSGSGNRFNS EKECQEICIQ
G
//
