ID A0A9J7KJN1_BRAFL Unreviewed; 1369 AA.
AC A0A9J7KJN1;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 28-JAN-2026, entry version 14.
DE SubName: Full=Collagen alpha-1(I) chain-like isoform X9 {ECO:0000313|RefSeq:XP_035662023.1};
GN Name=LOC118406220 {ECO:0000313|RefSeq:XP_035662023.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554, ECO:0000313|RefSeq:XP_035662023.1};
RN [1] {ECO:0000313|Proteomes:UP000001554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|Proteomes:UP000001554};
RX PubMed=32313176;
RA Simakov O., Marletaz F., Yue J.X., O'Connell B., Jenkins J., Brandt A.,
RA Calef R., Tung C.H., Huang T.K., Schmutz J., Satoh N., Yu J.K.,
RA Putnam N.H., Green R.E., Rokhsar D.S.;
RT "Deeply conserved synteny resolves early events in vertebrate evolution.";
RL Nat. Ecol. Evol. 0:0-0(2020).
RN [2] {ECO:0000313|RefSeq:XP_035662023.1}
RP IDENTIFICATION.
RC STRAIN=S238N-H82 {ECO:0000313|RefSeq:XP_035662023.1};
RC TISSUE=Testes {ECO:0000313|RefSeq:XP_035662023.1};
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_035662023.1; XM_035806130.1.
DR GeneID; 118406220; -.
DR Proteomes; UP000001554; Chromosome 18.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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:SF1112; COL_CUTICLE_N DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01391; Collagen; 3.
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:UP000001554};
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..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1369
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039942898"
FT DOMAIN 40..234
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 236..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..273
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..341
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..402
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..459
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..488
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..520
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..539
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..568
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..604
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..625
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..709
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..747
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..767
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..796
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..890
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..939
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1026
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1369 AA; 136063 MW; 6B6E83ED2FBC56D3 CRC64;
MMCLFAGEQG RLVCLLALVA VIATPGHGQE IIGESGGQQD IDLLQMIGVP LPTPIRFVSG
YDGFPAFEFG SEANIGRLAR TFFPNMFYKD FSILVTTRPN FQEGGILFAV TNSFQTVIQL
GLKIADAGKG RSGEALQNIT FIYTDTRNSE VTQEVARFTI PTTAGEWLRF SLSVRGNAVT
LYYDCEERET QFFDRTVSQL EFAPAAAVFV GQAGAAEEGK YLGSIQELLI RKDPNAAEQQ
CSGDAGEEGT VSGSGDGGEE GTIITIPGTV IPGRPNTPLA TQETPVDGPD VNEPYPDTSN
MERHDGDTTG WPELPEGGAN TGLAGLPGLP GVPGPKGDTG PQGPPGPRGE KGEPGDTTLV
EGPIGIPGDP GLPGLPGPKG DTGPVGPPGE RGLQGERGEA GLKGDPGVGL TGPPGPPGPP
GVVTVGDTDQ VISGTPGSKG EAGAPGLPGL PGPAGITGAK GEPGESIAGV AGPPGPPGPP
GLPGPPGPSN GFVPETGVAG PPGPPGPPGI PGLPGPPGLP GLPGKPGTFG TGNITNGIQG
PPGRDGVDGS AGPPGIPGIP GQDGPIGPKG EAGVPGIEGP AGTKGEPGLT GAPGLPGPPG
PPGPSGGGGG IFGFGGSSGG PGPAGEPGIP GNPGQKGEQG TAGPEGPQGT PGLPGPVGPR
GQKGDPGEAG IVGPQGPKGD MGPRGPAGEA GRDGVGLPGP PGPPGPPGLP GTISVLPGDD
EMTVSPGFRP TGGEGEMTGG FPGGLIGPAG PEGPRGPPGI AGPPGPIGRP GDDGAPGLKG
DRGDSGEAGR KGDRGEPGPA VTVDGDVLQI KGSKGEPGLD GVEGLPGIKG EPGEAGIQGP
EGPIGPKGMI GEVGFPGRMG LPGVRGQKGE KGDTGTGLPG PPGPPGPPGL PSGASFPAGS
FPVLQKGEKG DIGPSGPPGP PGALASGPGL SFGGAGLVGP AGPKGEKGMM GIRGPLGRQG
RKGEIGLPGR KGDRGEAGPP GAPGGFFGGS GQVVQGPTGP PGPQGPRGPP GFPGRGPSGP
PGPRGPAGPA GIGAPGLPGP PGRPGQPGAS IGSGIMGPPG PPGPPGRAAG IVTFNSESHL
LRSPPSSPGT LAFVADTEQL YLRVGGGWQI ILTQPLRPTV QVGKIMSIPE RPPVQPEASA
ENPGHANNGF NNGFFGSEVD APTVQLVGSP DSNLGKATGK RLHLIALNEP MTGNMYGIRG
ADFKCFQQAR QAGLRGTFRA FLSSKVQDLS SVVSRGDRDG IPIVNLKDEI LFPSWNSIFE
GERETNEYKG GAFDINTAIY TFNGTQPLLN PTWPHKRIWH GTNMDGQRLG DHFCNAWREN
DVSFVGMASS LQTGMLLGQE QYSCSSSYIV LCIENTHKRH HRVYNYRRK
//
