ID W5MZ17_LEPOC Unreviewed; 1171 AA.
AC W5MZ17;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Collagen type XXVIII alpha 1 chain {ECO:0000313|Ensembl:ENSLOCP00000013626.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000013626.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000013626.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01004624; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015213641.1; XM_015358155.1.
DR RefSeq; XP_015213642.1; XM_015358156.1.
DR RefSeq; XP_015213643.1; XM_015358157.1.
DR RefSeq; XP_015213644.1; XM_015358158.1.
DR AlphaFoldDB; W5MZ17; -.
DR Ensembl; ENSLOCT00000013655.1; ENSLOCP00000013626.1; ENSLOCG00000011072.1.
DR GeneID; 102691149; -.
DR KEGG; loc:102691149; -.
DR CTD; 340267; -.
DR GeneTree; ENSGT00940000163195; -.
DR HOGENOM; CLU_009158_0_0_1; -.
DR OrthoDB; 2906665at2759; -.
DR Proteomes; UP000018468; Linkage group LG11.
DR Bgee; ENSLOCG00000011072; Expressed in camera-type eye and 11 other cell types or tissues.
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; cd22628; Kunitz_collagen_alpha1_XXVIII; 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; PTHR24020; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24020:SF49; COLLAGEN ALPHA-1(XXVIII) CHAIN; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR Pfam; PF00092; VWA; 2.
DR PRINTS; PR00759; BASICPTASE.
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:UP000018468};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1171
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004866789"
FT DOMAIN 48..231
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 802..985
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1118..1168
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT REGION 239..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..401
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..755
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1171 AA; 121202 MW; C8C1E1D27F03982D CRC64;
MWRGVSVCLL LLAVVSDTAK SQSRKRKGQR ANNLFMKDEV KDMICELDIA FIVDSSESAK
LLLFEKQKTF VESLTERIMQ LQMPLAWKLK VRLAALQYSS TVKIEHNFRD WQDADVFKSR
VSTMAYIGHG TYSSYAITNA TQLFDEQTKP NSVRVAILMT DGVDHPRNPD IMGAASVAKD
RKIRLFTIGL TDLARESVNN AKLRSIATAP AQQYVHSLTD PLLEEKLFRE LSVIANKGCP
QPCSCEKGER GPPGGPGKRG DPGYDGSPGE KGSKGEPGIN GRTGNEGPEG RPGFRGDKGE
RGECGAPGTK GERGMEGPPG LRGPRGVQGI SGPPGETGPE GSPGPKGDRG PLGASGPPGD
AGIGFPGPKG DKGIQGRPGP TGPVGIGEPG LPGPPGPQGI QGNQGPPGEG LPGPKGDRGY
EGPRGSPGPS GASLKGEKGD IGPPGLPGPV GFPGMGIQGE KGNQGPAGPP GPRGTPGIGF
MGPKGDQGFP GESGVPGERG FGEPGPKGDP GPPGAAGIPG IPGEDGVEGP KGESGLPGPR
GPDGAAGKGI PGEKGDKGDR GVRGLPGAQG QQGPTGPKGE PGSIGQIGMP GPPGRGIPGP
KGDTGPVGPA GPVGETGIGI TGPKGERGLP GPTGSPGPKG EGFPGLLGPR GPPGTPGEIG
PEGKGLPGAK GDRGSPGLPG PSGPPGIGQI GPKGSVGQPG LPGLQGIPGE GIQGPKGEPG
FQGSPGPRGP PGEGLPGEKG DRGFPGDRGR KGDKGEFGGP GSPGSPGRIG QKGDPGLTRE
EVIKIIREIC GCGVKCRESP LELVFVIDSS ESVGPDNFNV VKDFVNALID RVSVSRDASR
IGVVLYSHIN VVVASLHQQL SQEEVKAAVR KMTYLGEGTY TGSAIKQANQ IFQASRPGVR
KVAIVITDGQ ADKRDSVKLE VVVRESHATN IEMFVIGVVN KSDTLYQEFK NEMNVIASDP
DEEHVYLIDD FMTLPALESK LLSRICESED GSLFSPIPSS ILPPGIATTS EVFRETERTD
TPRFNGDYNR VYKEPAPPGK SVLTTAPEGP GPVNASRTEQ IHSRKELPVP SFDSETSIAA
ASGPHTPTQK PYSPETGWLP APPPLPLERE SFLSDRGCDE HLDPGPCREY VVKWYYDSTA
NACAQFWYGG CQGNRNRFDT EDSCRNTCVR R
//
