ID A0A7K6YD81_ALCTO Unreviewed; 1356 AA.
AC A0A7K6YD81;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 17.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
DE Flags: Fragment;
GN Name=Col15a1 {ECO:0000313|EMBL:NWX69446.1};
GN ORFNames=ALCTOR_R07381 {ECO:0000313|EMBL:NWX69446.1};
OS Alca torda (Razorbill).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Charadriiformes; Alcidae; Alca.
OX NCBI_TaxID=28689 {ECO:0000313|EMBL:NWX69446.1, ECO:0000313|Proteomes:UP000536033};
RN [1] {ECO:0000313|EMBL:NWX69446.1, ECO:0000313|Proteomes:UP000536033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OUT-0003 {ECO:0000313|EMBL:NWX69446.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:NWX69446.1};
RA Zhang G.;
RT "Bird 10,000 Genomes (B10K) Project - Family phase.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Restin potently inhibits angiogenesis.
CC {ECO:0000256|ARBA:ARBA00058706}.
CC -!- FUNCTION: Structural protein that stabilizes microvessels and muscle
CC cells, both in heart and in skeletal muscle.
CC {ECO:0000256|ARBA:ARBA00058695}.
CC -!- SUBUNIT: Interacts moderately with EFEMP2.
CC {ECO:0000256|ARBA:ARBA00065596}.
CC -!- SUBUNIT: Trimer; disulfide-linked. {ECO:0000256|ARBA:ARBA00061770}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:NWX69446.1}.
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DR EMBL; VZSD01002695; NWX69446.1; -; Genomic_DNA.
DR Proteomes; UP000536033; Unassembled WGS sequence.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-ARBA.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
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 CDD; cd00247; Endostatin-like; 1.
DR FunFam; 3.40.1620.70:FF:000002; Collagen alpha 1 (XV) chain; 1.
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; IPR001791; Laminin_G.
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; SM00282; LamG; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
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:UP000536033};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 8..196
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 57..195
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 193..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1098
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..634
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..692
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..715
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..748
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..758
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..801
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..884
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 900..910
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..971
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1074
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1093
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:NWX69446.1"
FT NON_TER 1356
FT /evidence="ECO:0000313|EMBL:NWX69446.1"
SQ SEQUENCE 1356 AA; 141845 MW; 6066A0FBA5DCDE39 CRC64;
TERGSKGHLD LTELIGVPLP PSVYFVTGYG GFPAYSFGPD ANIGRLTSAI IPLPFYRDFS
IAVTVKPNSD RGGVLFAITD AFQKTIYLGM RISPVDDSTQ RIITYYTEPG SHVSREAASF
KVPVMTDRWN RFTVTIQGNY VALFMDCEEY QKVQFQRSAQ ALVFESGSGI FVGNAGATGL
EKFTGSIQHL TIKSDPRATE DHCEDDDPYA SGDTSGNGSI QEHEGISETQ EVLAPSHLPI
RPEDTLAEPV EAPPTILSYL EENDFSGNHR AEEISGAAKL KEQGTASFFI WLGTVMESGQ
SNSESTTATQ EILREEDGSG ASVLPGVSRE EVCIMAVSIC SSGTLEFSKY LSLVLCSPVG
ILSNPNAACQ VLPSLCPKQA LLPLCCGQSR CVCPTWTQGQ RMVPSLILLM RIGSKKKTLW
QQEKQLSRSE LRLHLEGKDS CSLFLITYMA ILVKTLLEAE ESGSGDIDGE TEILRHNKDC
RRSIFIDSSI ISQCKFCTCL IHHIQKCFVG NTGGFISISK KDLCESGRGR SSCPSSLPCQ
VLTMSTSSQC SCNPMEKPFE TSKEKTNHFP LFSDPLISFW LSPPGLPGLP GKPAPNSGVG
PPGSPGEDGA SGERGPEGPQ GPPGLDGVVG PPGQKGEKGD QGLPGSVGPK GDTGVAGSIG
PKGQAGAVGS PGKPGPPGPP GPPGPPGPPG PPGLSYTLGF EDMEGSGSAG LLSESRIPGS
RGPKGPKGEK GDPGPQGEPG QDGNSIVGPP GPPGPPGPII AIPELLLNDT DGIFNFTGIK
GLLGPPGPDG KPGLPGFPGP RGPKGDTGLP GLQGRKGQQG EKGEPGAIIA SNGSLTELLG
RKGEKGEAGV VGPVGPMGPI GPTGPKGELG FPGRPGRPGL NGVRGVKGDK GEAFNGLPGL
PGPPGPPGPP GRIVYIKGVI FPVSPRPHCK MPVSPPYPEN QEALNVHGAK ANRDSWGLHR
SADLKGEKGD KGAPGPPGPP LPPSYFSHFI NSIKGEKGDN GVTGVKGEKG EPNGGFFLTG
PPGPPGRPGL VGPKGDSVVG PRGPPGLPGL PGLPGYGKIG PPGPPGPPGP PGPPAIYGSA
ATMPGPPGPP GEPGSPATRN LVTTFQNIEG MLEKVHLVAE GTLIYLSETS EVFIRVRNGW
RKLQLGELIP IPADSLPPPA ISSHGFQSLP APNPVSNMNN GRPALHLVAL NSPFSGDVRA
DFQCFQQAQL AGLSATYRAF LSSHLQDLAT VVTKTDRYHL PIVNLKGETL FNNWEFIFNG
NGGQFNVHVP IYSFDGRNVM TDPSWPQKVI WHGSTANGIR LVSNYCEAWH TADMAAMGQA
SPLKMGKLLD QKVFSCNNKF IVLCIEISFV SDPQGK
//
