ID A0A3P8P1G6_ASTCA Unreviewed; 1603 AA.
AC A0A3P8P1G6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Collagen type XX alpha 1 chain {ECO:0000313|Ensembl:ENSACLP00000010857.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000010857.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000010857.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000010857.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR STRING; 8154.ENSACLP00000010857; -.
DR Ensembl; ENSACLT00000011122.1; ENSACLP00000010857.1; ENSACLG00000007430.1.
DR GeneTree; ENSGT00940000153769; -.
DR OMA; DISGCYG; -.
DR OrthoDB; 5353225at2759; -.
DR Proteomes; UP000265100; Chromosome 20.
DR Bgee; ENSACLG00000007430; Expressed in anal fin and 3 other cell types or tissues.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 7.
DR CDD; cd01482; vWA_collagen_alphaI-XII-like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 7.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR24020; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24020:SF39; COLLAGEN ALPHA-1(XX) CHAIN; 1.
DR Pfam; PF01391; Collagen; 4.
DR Pfam; PF00041; fn3; 7.
DR Pfam; PF00092; VWA; 1.
DR PRINTS; PR00453; VWFADOMAIN.
DR SMART; SM00060; FN3; 7.
DR SMART; SM00210; TSPN; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 5.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS50853; FN3; 6.
DR PROSITE; PS50234; VWFA; 1.
PE 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 55..145
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 278..450
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 481..570
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 571..662
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 663..751
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 752..842
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 843..936
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 148..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1468..1603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1471..1488
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1587..1603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1603 AA; 172287 MW; F78FCD3F5A4C8A93 CRC64;
MLTSRLWNAV RNKLDSPNRQ TPLMSPHLLA TSLSSSWLMP FFLLSVLLLS AAVHGQGRLK
LTVLSEDRLQ MKWKEADGPV QGYKVRVRPI SEVPQPELML TTTRGRATVA GLDSSQEYYL
QVLVLNGTTE KLLAKRRFTM QTLREEEMIR SGTREHRKKL LPGGSGSGEL EDATEALLDV
PTVLYPEPTT TTPASASTTE PPVTDTPSEL PDKTSEKSGK EKRKKKKERD RSKMENKEEQ
GTTQGEPAQE KPRKSPFPTQ PGMSSRKPFE CASDAAADIV LLVDGSWSIG RINFRRVRDF
LEGLVTPFHI GPNHIQIGLT QYSGDPRTEW HLNNFTSKEQ LLEAVRNFRY KGGNTFTGQA
LLHVMEENMR SSAGARSDTP FFLVLLTDGK SQDDAIAAAT RLKNAGIEII AVGVKNADEA
ELRQVASEPV DLNVYNVNDF PLLSKLVARL VHILCGRIEE RGITKRMEPG STADPTLSYP
SPTDLRFSEL GSREVKLHWT NPVKPVQQYR VVYHSAESQS PQEVVLPGSE SVVLLEGLSS
QTLYHVSIFP VYEDNVGLAL RGTVTTLPLA MPANLKVTPS SYSTLQVSWG AAPGATQYLI
LYSALSHGEP DDAKEEKFGA EQTVVELAGL LPATDYSVTL YALYEEEPSD PVTAVTTTFP
LPTPLSVQFP MVTHSMMKVS WVPGAGDVPG HRITYSTNHG SDVKQVEVTG VNSVLVQNLS
SLSRYLISVQ SHYAQGLSAA LTSNVTTLKV PPPSDLRVTN FSDSDIMVRW EAAADDVVSY
LIKWISLSGG DLRQLRMSGD SEGAVLGGVE DDKEYQISLS ALYGDGAQSE AVAIRYSTLS
GGGPTSLTVS DETAVSMVIS WVPPNAHVLQ YRVSYTALTG TDSQDHTVLV PGGEKQVMLE
SLQPDTRYSI LVTAEYHNRE GGSGSAQGKT ATLRVSSASV VRSDHSSICV SWRPVSAVDG
YRIVIQDVKD KQSKQEVVSK SSRSHCFTDL EPETLYRISV HSLLGSAEGP AVSILHPTAA
APARIAIHPR MYPIHNEVCP EVTIRNSIVK GFNMMEAFGL TQRAHSSVEG VAAEPFVFNT
LPTYTLYRDV QLTQSTKFIH PAGFSPEHTI SIAFRMLQDT PREPFALWQL TDNDFQPKMG
VVIDPTTKHL LYFSLDYRGE VQELTFDQPQ VHRLFYGSFH KVHLSVSQVS VSLSVDCQHV
GERPARPLGN LPTDGFEMLG KLVKTRGPNS GSAPFQLQSF EIVCNTTWAS EDTCCDLPGV
RDEESCPAPA YTCTCSSDVP GAPGPPGPPG KPGPRGEKGE KGEHGQKGEV GPPGNPGLEG
GLGPVGSIGP RGITMQGKKG PPGARGEKGD PGRPGVQGVP GPPGQKGEEG IAGAKGIRGV
EGNMGAPGIT GPRGFQGMPG YPGPIGERGP PGPVGPTGLP GNKGERGEKG EPQSMAMIYQ
LVTQACEQLV HKEVLKLDMF INEIGRKPVP IEEPVGPPGE PGIPGPKGPP GERGSQGRVG
PRGTPGRPGY PGEQGRKGVP GDKGDAGSNV QGHPGVKGLA GPPGESKLGI PGPKGENGML
GPSGIPGTPG QPGEIGPPGV CDNSGGCHML PQQTEDSYDD YQP
//
