ID A0A7J7UNF6_MYOMY Unreviewed; 1373 AA.
AC A0A7J7UNF6;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE RecName: Full=Collagen alpha-1(XV) chain {ECO:0000256|ARBA:ARBA00074723};
GN ORFNames=mMyoMyo1_003128 {ECO:0000313|EMBL:KAF6314332.1};
OS Myotis myotis (Greater mouse-eared bat) (Vespertilio myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=51298 {ECO:0000313|EMBL:KAF6314332.1, ECO:0000313|Proteomes:UP000527355};
RN [1] {ECO:0000313|EMBL:KAF6314332.1, ECO:0000313|Proteomes:UP000527355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMyoMyo1 {ECO:0000313|EMBL:KAF6314332.1};
RC TISSUE=Flight muscle {ECO:0000313|EMBL:KAF6314332.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
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:KAF6314332.1}.
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DR EMBL; JABWUV010000012; KAF6314332.1; -; Genomic_DNA.
DR VEuPathDB; HostDB:GeneID_118667264; -.
DR Proteomes; UP000527355; 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; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 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, ECO:0000313|EMBL:KAF6314332.1};
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:UP000527355};
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..1373
FT /note="Collagen alpha-1(XV) chain"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5029755011"
FT DOMAIN 39..227
FT /note="Thrombospondin-like N-terminal"
FT /evidence="ECO:0000259|SMART:SM00210"
FT DOMAIN 88..226
FT /note="Laminin G"
FT /evidence="ECO:0000259|SMART:SM00282"
FT REGION 225..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 973..1117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..250
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..562
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..577
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..596
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..617
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..718
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..903
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1029
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1091
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1110
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1373 AA; 141378 MW; D17FEA7A2E357FD6 CRC64;
MEPRKNEQSR FLLWLLWVSA LLSAAARTRA ETEPASQATV DLMEIIGLPL SPSVSFVPGY
GGFPAYSFGP GANVGRPASV LIPPTFFRDF AISVTVKPSS DRGGMLFAIM DTGRTVIHLG
LQLSAVEDGH QRVILYYTEP GSPVSREAAA FSVPAMTHRW NRFAVMVEGE EVILLVDCEE
HSHAPFQRSS RALVFEPRTG LFVGSAGDRK LEKFIGSIQQ LTIHSDPRAP EKRCEAEESS
ASGEASGLLE TDGVTDGVAE ILEADTYTQA PPKEAKVEPI NTPPTPTFPS EDSELSGEPI
PEGTLETTNL SAILNSSAEQ GSGDILNDTL EEVDAMNGVP VTDPGSGDGA FLHVTEESPH
TEEDLATTVA AREADVTVST AWDAEVAIST AGEAEGGSVP TGAPALSMST QDPGERDTPS
PDTEEGSAAI SMEEAEMPTS TDREAEASTV PTGEPALFMS TQEPEEGVSL GPVSEGSLTT
AAAAAEMPLS TCEDEEEEEE TSKAPTGGPP PGTPTAAPEQ AVTFGPSDED LVAATTEEPL
SRAEAEESGS APPEGPPLPI PTVTPATTVP PVTSVGAEAE GSGLGWGSEI GSGSGDLGHS
EELLRGPPGP PGPPGLPGNP GKPGTDVFMG PPGSPGKNGA AGEPGPRGPK GQPGLDGASG
RPGTKGEKGA RGPNGSVGEK GDPGNRGSPG RPGKNGQVGT PGIMGPPGPP GPPGPPGPEC
TMEPEFEYIE GSGTIRPRHE PRISGPNASN GLKGEKGDPG LKGERGMDGT SIVGPPGPRG
PPGRIEVLPS SLINMTHGFM NLSDIPELTG PPGPDGMPGL PGFPGPRGPK GDTGVPGFPG
LKGEQGEKGE PGAILTGDIP LERLRGEKGE PGVHGAPGPM GPKGPPGHKG EFGLPGRPGR
PGLNGFKGAK GDRGVMMPGP PGVPGPPGPP GPPGAVINIK GAVFPIPARP HCKMPVGAAH
PGNSELITFH GVKGEKGTWG LPGSKGEKGD QGAQGPPGPP MDPAYLRHFI NSLKGENGDR
GFKGEKGDSL GDFSVSGPPG RPGSPGLAGQ KGETIVGPQG PPGVPGLPGP PGFGRPGSPG
PPGPPGPPGP PAILGAAVAL PGPPGPPGQP GLPGSRNLVT ALRSMDDMLQ NAHLVIEGTF
IYLRDSTEFF IRVRDGWKKL QLGELIPIPA DSPPPPALSS NNPHPLRPPL TSVSSVNYGR
PALHLVALNM PFSGDVRADF QCFQQARHAG LLSTYRAFLS SHLQDLSTVV RKVERYSLPI
VNLKGQVLFN NWDSIFSGHG GQFSTHVPIY SFDGRDVMTD PSWPQKVVWH GSNPHGVRLE
DNYCEAWRTA STAVTGLASP LSTGKILDQK AYSCASRLIV LCIENSFMTD ARK
//
