ID W5MN51_LEPOC Unreviewed; 1232 AA.
AC W5MN51;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Collagen, type XXVIII, alpha 2a {ECO:0000313|Ensembl:ENSLOCP00000009810.1};
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:ENSLOCP00000009810.1, 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:ENSLOCP00000009810.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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DR EMBL; AHAT01020077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5MN51; -.
DR STRING; 7918.ENSLOCP00000009810; -.
DR Ensembl; ENSLOCT00000009821.1; ENSLOCP00000009810.1; ENSLOCG00000008066.1.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000163195; -.
DR HOGENOM; CLU_009158_0_0_1; -.
DR InParanoid; W5MN51; -.
DR OMA; KFFTIGI; -.
DR Proteomes; UP000018468; Linkage group LG12.
DR Bgee; ENSLOCG00000008066; Expressed in larva and 5 other cell types or tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
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; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF936; COLLAGEN TYPE VI ALPHA 2 CHAIN; 1.
DR Pfam; PF01391; Collagen; 3.
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 Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1232
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004866516"
FT DOMAIN 58..240
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 813..993
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1173..1223
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT REGION 259..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1057
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..674
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..720
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..768
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1232 AA; 127895 MW; 424D2361FCF3E6EA CRC64;
MYPTFTWLLL VTGLQTISSQ DPYEDKSVAK KVKNKLLSSN AIEKHDGQAI LDEDCTFELA
FLVDSSESAK DNHEREKQFA INVVDKLGGV RLKSGRGLSW KAALLQYSSH VVIEQTFKQW
RGTENFKSRV APVLYIGHGT YTTYAITNLT QIYLEESNQG SVKIAVLFTD GVFHPRNPDI
FSATADAKNQ GVKFFTIGIT RAANEPSNVA KLRLLASSPA SRFLYNLQDT GIVDKVVKEM
AELADEGCPL AQKCVCEKGE RGPSGPPGKK GRPGDDGAPG IKGYKGESGL SGLPGREGAE
GKPGYKGEKG ERGECGTPGI KGDRGPEGPS GIRGARGLQG LPGSQGDIGT EGPQGKKGER
GPAGPPGIQG ETGIGLPGPK GDMGFQGRPG PSGPPGIGEP GLPGPQGPQG VQGEKGPIGE
GFPGPKGDRG LEGPRGSRGP PGAGIKGEKG ELGPLGPPGL VGLPGVGIQG EKGVEGPRGP
PGSRGQPGEG FPGPKGDQGL PGELGAPGER GIGEPGPKGE PGSSGLAGLP GLPGEDGAPG
QKGEPGLIGL RGPEGTPGIG TQGEKGDQGQ RGIRGLPGPP GIAGPSGAKG EPGTPGRLGM
PGLPGRPITG PKGEIGPPGP QGPIGETGYG LPGPKGDRGN HGPPGPFGPK GDGYPGPPGQ
PGLPGLPGEP GPEGIGLPGP KGDIGFRGLP GLPGPSGEGL PGPKGVIGRP GPPGPPGPQG
EGLQGPKGEH GPQGVTGPRG PPGEGLAGSK GDRGSQGERG RKGEKGDFGD PGTPGQSGRP
GIKGEAGLTR EDIIKLIKEI CGCGVKCKER PMELVFVIDS SESVGPDNFE IIKDFVTALV
DRITVGRNAT RIGLVLYSLD VHLEFNLARY MTKQDIKQAI RKMPYMGEGT YTGTAIRKAT
QEAFYSARTG VRKVAIVMTD GQTDKREPVK LDIAVREAHA ANIEMYAIGI VNTTDPTQAE
FLRELNLIAS DPDSEHMYLI DDFNTLPALE SKLVSQFCED ENGALVYNRI VNGYGTNGNV
FQEEFRVGTR LTTSHSESSS VGRGDVPAVS VSTGRPSQQV ASQNSEFLTF VKKTSCANFL
VQVEEIDEDL EDPYEVTVKE VLSHSSSVNA KGSGTSVISR PVPSPQPKPV APGRDSSSST
VVVSSSSSSS SVQFLPAPRP VLPKEFIPLD PRCALVLDQG PCRDYNIRWY YDKQANACAQ
FWYGGCSGND NRFDTEEECK KICVLTRTGD RS
//