ID A0A6P4ZQI3_BRABE Unreviewed; 1385 AA.
AC A0A6P4ZQI3;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 28-JAN-2026, entry version 22.
DE SubName: Full=Collagen alpha-1(I) chain-like isoform X7 {ECO:0000313|RefSeq:XP_019636314.1};
GN Name=LOC109478941 {ECO:0000313|RefSeq:XP_019636314.1};
OS Branchiostoma belcheri (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7741 {ECO:0000313|Proteomes:UP000515135, ECO:0000313|RefSeq:XP_019636314.1};
RN [1] {ECO:0000313|RefSeq:XP_019636314.1}
RP IDENTIFICATION.
RC TISSUE=Gonad {ECO:0000313|RefSeq:XP_019636314.1};
RG RefSeq;
RL Submitted (AUG-2025) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
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DR RefSeq; XP_019636314.1; XM_019780755.1.
DR GeneID; 109478941; -.
DR OrthoDB; 10060752at2759; -.
DR Proteomes; UP000515135; Unplaced.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
DR FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR050149; Collagen_superfamily.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF01391; Collagen; 5.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
PE 3: Inferred from homology;
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000515135};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1385
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5028410699"
FT DOMAIN 41..235
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 237..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..274
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..443
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..487
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..534
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..582
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..615
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..636
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 709..720
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..758
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..778
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 789..807
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..901
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..935
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 944..953
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 997..1006
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1044
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1385 AA; 137901 MW; AE5BC857DA608460 CRC64;
MVCLFAGEQG RLVWLVALVA VIATPPGHGQ EIIGESGGQQ DIDLLQMIGV PLPTPIRFVS
GYDGFPAFEF GSEANIGRLA RTFFPNMFYK DFSILVTTRP NFQEGGILFA VTNSFQTVIQ
LGLKIADAGK GRSGEELQNL TFIYTDTRNS EVTQEVAKFT IPTTAGEWLR FSLSIRGNAV
TLYYNCEERE TQFFDRTVSQ LEFAPAAAVF VGQAGAAEEG KYLGSIQELL IRKDPNAAEQ
QCSGDAGEEG AVSGSGDGGE EGTIITIPGT VIPGRPNTPH ATQETPVDGP DVNEPYPDTS
NMERHDGDTT GWPELPEGGG NTPGLPGLPG VPGPKGATGP QGPPGLRGQK GEPGDTTLVE
GPIGIPGERG LQGLPGTPGE AGPVGPPGER GPKGERGEAG LKGDPGVGLT GPPGPPGPPG
VVTVGEDDQV ISGTPGSKGA PGAPGLPGLP GPAGITGAKG EPGESIAGVA GPPGPPGPPG
LPGPPGPSNG FVPETAIIGL EGSGYEFAGQ GVSGPPGPPG PPGIPGLPGP PGLPGLPGKP
GTFGTGNITN GIQGPPGRDG LDGLTGPPGL PGLPGQDGLI GPKGEAGAPG IQGSAGSKGE
PGQPGLPGPP GPPGPSGGGG GIFGFGGSSG GPGPAGEPGI PGNPGQKGEQ GTAGPEGPQG
SPGLPGPVGP RGPKGDAGEA GIVGPQGPKG DMGPRGPPGE AGRDGVGLPG PPGPPGPPGL
PGTISVLPGD DEMTVSPGFP PVGGEGEMTD GFTGGVIGPA GPEGPRGPPG IAGPPGPIGR
PGEPGLPGER GEKGDSGEAG RKGDRGEPGP AVTVDGDVLQ IKGAKGEPGL EGVAGFPGKK
GEPGDAGVRG PEGPVGPKGM IGEVGFPGRM GIPGVRGQKG ERGDTGTGLP GPPGPPGPPG
LPSGASFPAG SFPVLQKGEK GDIGPSGPPG PPGPPGSLAS GPGLSFGGAG VIGPAGPKGE
KGMMGIRGPL GRQGRKGEIG LPGRKGDTGL PGPPGAPGGG FFGGSGQVVQ GPTGPPGPQG
PRGPPGFPGR GPSGPPGPRG PPGPAGIGAP GLPGPPGRPG QPGASIGSGI MGPPGPPGPP
GRAAGIITFN SESQLLRSPP SSSGTLAFIA DTEQLYLRVR DGWQIILTQP LRPTVQVGKI
MSIPERPPIQ PEASAENPGH ANNGFNNGFF GSEVDAPTVQ LVGSPDDGGL GKATGKMLHL
IALNEPMTGN MYGIRGADFK CFQQARQAGL RGTYRAFLSS KVQDLSSVVS RGDRDGIPIV
NLKDEILFPS WNSIFEGERQ TNKYKGGAFD INTAIYTFNG TQPLLNPTWP HKRIWHGTNM
DGQRLGDHFC SAWRENDVSY VGMASSLQTG LLLGQEQYSC SSSYIVLCIE NTHKRHHRLY
NFRRK
//
