ID A0A3Q1J4B1_ANATE Unreviewed; 1114 AA.
AC A0A3Q1J4B1;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Collagen, type XXVIII, alpha 2a {ECO:0000313|Ensembl:ENSATEP00000025048.2};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000025048.2, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000025048.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3Q1J4B1; -.
DR STRING; 64144.ENSATEP00000025048; -.
DR Ensembl; ENSATET00000025452.2; ENSATEP00000025048.2; ENSATEG00000017277.2.
DR GeneTree; ENSGT00940000163195; -.
DR InParanoid; A0A3Q1J4B1; -.
DR Proteomes; UP000265040; Unplaced.
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:SF70; PH DOMAIN-CONTAINING PROTEIN; 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:UP000265040};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1114
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030080214"
FT DOMAIN 58..240
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 703..887
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1029..1079
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT REGION 281..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..569
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..622
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..676
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1114 AA; 117044 MW; FDB231961836244F CRC64;
GARMLPPFPL VLLITALASV WAQDFYEDRK TIKNSKVKPL TASIYNGQAI LDEDCSLELS
FLLDSSESAK DNHEQEKQFV INVVERFQRI RLQTGRSLSL RVAVLQYSSH VITEQTFRDW
RGTESFKSQI SPITYIGHGT YTTYAITNMT KIYLEESNPG SIKVAVLLTD GISHPRNPDI
FSAVADAKNQ GITFFILGIT RAAKEPANVA QLSLLASTPT SNYLLNLQDE DIVEKVVNQM
CPLAERCTCE KGERGPSGPA VSVHLPTQLF KISYSQRAVS FEGERGPAGP PGIQGETGIG
LPGPKGDMGF QGRSGPPGPP GVGEPGPSGP QGPQGVQGEK GPQGEGFPGP KGEMGPPGSP
GPIGLTGVGI QGEKGIEGPR GPPGPRGIPG EGFPGPKGDQ GLPGEQGAPG EGGIGEPGSK
GEPGAVGLAG VPGLPGEDGA PGQKGEPGLP GLRGPEGAQG IGIQGEKGDQ GLRGIRGLHG
PPGIAGPSGP KGERGIPGQQ GMPGLPGRSI SGPKGDVGPA GPPGPIGETG LGLPGPKGNH
GHPGLPGPSG PKGEGIPGPM GPPGMPGLPG EPGSEGIGVP GPKGDVGFRG LPGLPGSPGE
GLPGPPGHIG RPGPPGPAGP PGEGIQGPKG EPGSQGMTGP RGPQGDGFPG AKGDRGLQGE
RGMKGAKGDM GDHGVPGEAR EDIIKLIREI CGCGIKCKER PMELVFVIDS SESVGPENFE
IIKDFVTRLV DRITVGRNAT RIGLVLYSLD VQLEFNLARY MSKQDVKQAI RKMPYMGEGT
HTGTAIRKAN QEAFFGARPG VRKVAIVITD GQTDKREPVK LDIAVREAHA ANIEMYALGI
VNSSDPTQAE FLRELNLIAS DPDSEHMYLI DDFNTLPALE SKLVNQFCED ENGALIYNHI
TNGHWNGNNG PGHGISGHNG QAVNANGYNA HGNNGYGNNI NGYNYQEERN PNQNERLTNS
RSRGDTFTLP ISANPLPVQV VEDEDGEDLD SRAHVRGSST GSIVSRITLK MCISHTISPS
VVALLDPRCG LNLDQGTCRD YGIRWYYDKQ ANACAQFWYG GCGGNDNRFE TETECKKTCV
QFRTGNCRFI LQNIYIFFSR LLFPYYYSFF SPAG
//
