ID A0A7M7LNC9_APIME Unreviewed; 1148 AA.
AC A0A7M7LNC9; A0A8B6YZN7;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE SubName: Full=Collagen alpha-1(IX) chain isoform X7 {ECO:0000313|RefSeq:XP_006564403.1};
GN Name=LOC412865 {ECO:0000313|RefSeq:XP_006564403.1};
OS Apis mellifera (Honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Apis.
OX NCBI_TaxID=7460 {ECO:0000313|EnsemblMetazoa:XP_006564403};
RN [1] {ECO:0000313|EnsemblMetazoa:XP_006564403}
RP IDENTIFICATION.
RC STRAIN=DH4 {ECO:0000313|EnsemblMetazoa:XP_006564403};
RG EnsemblMetazoa;
RL Submitted (JAN-2021) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_006564403.1}
RP IDENTIFICATION.
RC STRAIN=DH4 {ECO:0000313|RefSeq:XP_006564403.1};
RC TISSUE=Whole body {ECO:0000313|RefSeq:XP_006564403.1};
RG RefSeq;
RL Submitted (APR-2025) to UniProtKB.
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DR RefSeq; XP_006564403.1; XM_006564340.3.
DR AlphaFoldDB; A0A7M7LNC9; -.
DR EnsemblMetazoa; XM_006564340; XP_006564403; LOC412865.
DR GeneID; 412865; -.
DR CTD; 104327; -.
DR OrthoDB; 5983381at2759; -.
DR Proteomes; UP000005203; Linkage group LG11.
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:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR CDD; cd00247; Endostatin-like; 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:SF914; OTOLIN-1; 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 4: Predicted;
KW Collagen {ECO:0000256|ARBA:ARBA00023119,
KW ECO:0000313|RefSeq:XP_006564403.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005203};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1148
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5044660314"
FT DOMAIN 47..222
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT REGION 234..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 321..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..260
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..529
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..574
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 650..661
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..714
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..748
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..769
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1135
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1148 AA; 120438 MW; C502A1CC9EE07BD6 CRC64;
MRSRLQSLIF ALFCVTRVNA DFFAEKKEIN YDLIEAAVAS ADTDDTNLYI DDGLDGFPSF
GFRPGSEVKQ PYRLYLPEKL PAEFTLVATF KPMSFRTSYL FAVLNPFETV VQLGIRISDG
PGTNQNVSLI YTNSDLHSHS EEVAKFTVPK LSRKWSKIVI RVSTTDVTLY LNCHEMARQR
VTRIPLELVF DTASTLYIAQ AGPHIQEKYD GLLQSLKLYP GHPADLVKCT ADFNIGRDDD
EDRSEESNPP PFITPPPPNP DYKGPKGEKG DKGDKGESVR GPPGPPGPPG QDEGPPGKKG
EPGTCTCNAT ALMASFTMPK MIQGPKGEQG VPGQEGKQGQ MGLTGVAGPP GERGLEGPQG
PKGDKGDVGI PGPEGPQGQK GEPGRDGIPG EKGAQGPPGP PGKGEFSGYD PSWKPRGIYR
TEGITMRPGL PGQKGEAGLP GSPGPKGETG IAGAKGNKGE PGHKGAKGDH GNEGARGIQG
SKGEPGAPGA PGLPGAPGEN GRPAEKGDKG DTGPEGKPGP PGAPGPPGLP GLSGPGGVNV
GESMLREKGD KGEGGARGYK GDKGTKGEKG DKGDSGPAGI PGVNGIQGPQ GNKGEPGKDG
VAGVQGIAGA KGEKGERGPP GATAIASSGD YITIKGEKGA EGKRGRRGRP GPPGPVGPPG
KPGAMGEIGL PGWVNTMKGR PGTPGLPGPV GPAGPKGEKG EPGTPSPYGV SVGVKGDKGD
DGFPGIPGQP GREGQRGPPG PPGPPGPPSQ GNYIPVPGPP GPPGPPGPPG LSLIGQKGEP
GIGRSHIFGE RDYYGVRQVQ SVKKKHIPYP TLQGPRTSLD ELKALRELKQ LKELKEHLGA
GTTATRGPLE STTKIVPGAV TFQNTEAMTK MSAVSPVGTL AYIIDEQALL VRVNNGWQYI
ALGSLLPITT PAPPTTSPPP VNPPFEASNL INQIPVKADG TGWYPRMLRM AALNEPFTGD
MHGVRGADYA CYRQAKRAGL RGTFRAFLSS RVQNVDSIVR LGDRDLPIVN IKGDVLFNSW
KEMFNGNGAY FSQNPRIYSF NGKNILTDFA WPEKVAWHGS HKLGDRAMDT YCDAWHSSSS
DRYGLGSPLT GGRLLEQVRY SCDNKFALLC IEVTSETTRR RRNAEIAEDE DEMSENDYKE
YLDSLMED
//
