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Database: UniProt
Entry: W5MN51_LEPOC
LinkDB: W5MN51_LEPOC
Original site: W5MN51_LEPOC 
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
//
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