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Database: UniProt
Entry: W5M0R9_LEPOC
LinkDB: W5M0R9_LEPOC
Original site: W5M0R9_LEPOC 
ID   W5M0R9_LEPOC            Unreviewed;      3022 AA.
AC   W5M0R9;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Collagen, type VI, alpha 4a {ECO:0000313|Ensembl:ENSLOCP00000001976.1};
GN   Name=COL6A6 {ECO:0000313|Ensembl:ENSLOCP00000001976.1};
OS   Lepisosteus oculatus (Spotted gar).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC   Lepisosteus.
OX   NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000001976.1, ECO:0000313|Proteomes:UP000018468};
RN   [1] {ECO:0000313|Proteomes:UP000018468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA   MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT   "The Draft Genome of Lepisosteus oculatus.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLOCP00000001976.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AHAT01012312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01012313; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01012314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01012315; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01012316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01012317; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AHAT01012318; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 7918.ENSLOCP00000001976; -.
DR   Ensembl; ENSLOCT00000001981.1; ENSLOCP00000001976.1; ENSLOCG00000001668.1.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00940000155619; -.
DR   InParanoid; W5M0R9; -.
DR   Proteomes; UP000018468; Linkage group LG11.
DR   Bgee; ENSLOCG00000001668; Expressed in larva and 12 other cell types or tissues.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   CDD; cd22630; Kunitz_collagen_alpha6_VI; 1.
DR   CDD; cd01472; vWA_collagen; 4.
DR   CDD; cd01450; vWFA_subfamily_ECM; 2.
DR   Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 10.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR24020; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24020:SF70; PH DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01391; Collagen; 3.
DR   Pfam; PF00014; Kunitz_BPTI; 1.
DR   Pfam; PF00092; VWA; 10.
DR   PRINTS; PR00759; BASICPTASE.
DR   PRINTS; PR00453; VWFADOMAIN.
DR   SMART; SM00131; KU; 1.
DR   SMART; SM00327; VWA; 10.
DR   SUPFAM; SSF57362; BPTI-like; 1.
DR   SUPFAM; SSF53300; vWA-like; 11.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR   PROSITE; PS50234; VWFA; 10.
PE   4: Predicted;
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW   Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..3022
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004865386"
FT   TRANSMEM        1294..1319
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1331..1361
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          35..209
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          238..411
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          443..618
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          633..807
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          840..1014
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          1034..1207
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          1369..1542
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          1571..1742
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          2322..2465
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          2531..2732
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          2972..3022
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
FT   REGION          1971..2280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2788..2815
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2025..2040
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2121..2135
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2788..2805
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   3022 AA;  333091 MW;  660D9A60C22CB293 CRC64;
     SSMEMIQFLS AFLFAFCLPV NNAQKTVCTE ETAADIVFLV DGSWSIGTEN FQQIRDFLYA
     LIDSFDVGAD KVQIGLIQYS NSPRTEFTLN QYQNKQDILT YIQSLPYKGG GTRTGLGLSY
     MLDNHFTEAA GSRVREGVPQ VAIVITDGQS QDTVKQAAEE VKNSGITLYA IGIKEAVLEE
     LNEIASDPDD KFVYNVDDFA ALQGISKNFV QVLCTTVEES KRQTLQVSKE CRQATAADIV
     FLVDGSTSIG ETNFNEVRNF LYTFVEGLDV GLNKVRVGLA QYSDEVYQEF LLNKYSDKQD
     ILEQMQNLQY RTGGTNTGKA LEFLRTQYFT EEAGSRATLG IPQVVIVITD GVSADEVREP
     AKKLRENVTV FVVGIGVAAY DELQEIANRP SDKFLFNIDN FEALNQLSSS LLPNVCTSIG
     TQKEENQLTP FLVVVIQKPM VLYIVFLVGG STLLGSPAFQ QIRSFISRIV NQLDVGINQH
     RVGMAQFSGD TKTEFLLNTY EKRGEVLNHL KNNFRLKGGA QRLGQALNYV HRTFYKESAG
     SRIAEGFRQF LIVFTSAKSE DEIQRAARII KAEGVTVISI GLPRAPITEL EVVATKPYVY
     QLNSQVFSKT VQEVSGIIES KEAHPCKSAT VADIVFIVDE SASIGTQNFR SVRNFVYKII
     DGLDVDLNKV RTGVIMYSDA PRAEVYLNSF REKAEVLRYI KTLPYRGGGT NTGAALDFAR
     QNMFVKGRGS RRSQGVQQIA IVITDGESQD NVSGPAVSLQ RAGVTVFALG IKEANMKQLK
     QIASYPSRKF VFNVDSFAKL ASVEKSLQKL LCSEIINIAF AAPRVIYSLK EGCVETEEAD
     IYFLIDHSGS IDPLGFVDMK KFIKEMIRMF RIGPQSVRIG VVKYANTPTV EFTVTEHTNK
     KDLERAVERV QQLGGGTQTG DALRSMSALF QKAASSRNRK TPQFLIVITD GKSQDAVVDA
     AKELRAQSIM IYAIGVGDAN EDELLEMSGS PDKKFYVSNF DSLRLIKNEV AQELCSEEAF
     FSFFLLVCKT MEADIIFLID SSGSIHPDDY SKMKTFMESM VDRSDIGADK VQVGVLQFSS
     VQQEEFPLNK YEDKSGIKQA IYNIQQLGGG TLTGEALKFT SQYFDAARGG RSTVKQFLIV
     ITDGEAQDEV AKPAQNLRNK GIIIHTIGVM NANDTQLVEI SGSQDKVHSA KNFDGLQFLE
     KNILFQICNP DTGEESGVTL QQNIVESNML KCHCRVHPKS GSMRVLLLEM PEQFQTNLNF
     SRLHQYLQNI AKHITGRTEH LLNLPLTVLS QIQYPLYCII FNALLVSICA YFCFTPIYFE
     FISLTNKVFK LLTFLLHIIS CYYTVPIIIH FPLYLITFLY IECRTEVADM IFLVDESTTI
     DSSEFVSMQK FMIAMVNNSD VGKNRVRFGA IKYSTTPTEM FRLNQFDSKQ QVRDAIAAMT
     ADGGDTYTAK ALQFSQTFFT EAYGGRKSAG VPQILLVITD GEATDRYELP KSSMRVREDG
     ISIYGIGVEN ATEEELKIMT EDETKVFYVN NFKGLEELQK NITKKLCNDT KPGRQACLLD
     YTYSCETKEA DIVMLIDGSG SINPGQFQTM QNFMKDIVGS FRISKTSVQV GVAQFSTEPQ
     KEFYLSEFDS EDAIKERILQ MKQMKQSTYI GKALRFIRSF FEPSAGSRIR QFVPQNLIVI
     TDGKSIDPVE EAAAELRALN IHIFVISIGY VDALKLQQIA GSNDRLFTVK NFNELETIKK
     RVVKNICDPG DEPSTSNCTI DIAVGFDISR RGRFPGLLSS QRKLEAQLLG LIRQMSYLDN
     LNCVSASQVI IQIGFLISEN GRIIFDSNFE KYNEEIVRKV MVTLQTMEAT YFTTKLLQSF
     LDKFKGKSTA NVKVLLVFSD GLDENVELLE TESENLRRGG INALLTVALE GVTNANDLQM
     VEFGRGFGYK VPLAIDMHNI NSAMAKELDT IAERVCCNVM CKCMGQEGLR GPRGPLGIKG
     SPGTKGPPGH PGDEGGFGER GTPGLNGTQG IEGCPGKRGI KGPRGYRGNR GEDGDHGIDG
     VDGEQGMAGL PGALGERGDP GSPGRSGVRG EPGERGQPGL RGDPGDSGTD NNIRGPKGEK
     GNPGIQVAPQ GDAGEDGTPG DAGVDGKRGE RGEPGTPGLR GDPGASGPQG ERGTRGLPGP
     PGTLGLPGRQ GELGLQGPKG SVGNEGPKGQ KGQPGDPGVK GSVGPNGPRG LPGIDGRDGY
     GSPGQKGEKG ESGFPGYPGP QGEEGDLGTP GSRGPKGSRG RRGNSGSSGV PGDPGIPGAS
     GHKVTVVPQF SLFHYFVGDK YWHKSNCFYR IHMTDCPVYP TELVVALDMS EDVTPQVFER
     MRNIAVNLLQ DLTISESNCP TGARVAVVSY SSTTKYLIRF SDYHRKKQLI EAIKNIPPKR
     TTSRRNIGAA MRFVARNVFK RVRQGVLMRK VAIFISNGAS QEATPIVTAA LEFKALDITP
     VVIAFRNVPN VRRAFQVDET GSFLVSVVDR PQNQRTEVQR IQQCALCLDV CNPSEACRIN
     LIPAPLQADV DLALVVDSSR NVPTDQYDGV KELLSSILDQ LDVSSQPGTS NRGARVALVQ
     HSTLNYPPRR GQAPVRTEFD LLKFKSRNLM KRHISESMQQ LGGSSSTGHA VEWAINNLLL
     KAVRPRKAKA VFAFVGGETS YWDRARLGYV ARRAMCQGVA VLAFSVGSDY NDTQVEDLAS
     IPLEQHMVHL GQAKLGEIEF AQRFARAFFR VLSTGVNSYP PPALRRECAN IQEPVQQAEI
     LETPPIDRIK PKTPPPAEEY YEYTEESESI VEEESEPEEE ITAGPELSQE ETVSQYEETG
     RAVEEILFGG ENYLCNTVSQ RQNISDCVNV LCVVLHVNSQ TNACWMWISV AFVGTICKDG
     IIIGQSVHAP LSGMAVVAVM RIDLIRNKSH TIQTLAETLQ CKNIRHFSKP QVPSLTPLYR
     QDLRLCLKIY FCHKVTLCTV QASPQFFSTD ACTLPKDEGD CRNFTLKWFF DGQQNECSRF
     WYGGCGGNRN KFETQEECEA VC
//
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