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HPLN3_MOUSE
ID   HPLN3_MOUSE             Reviewed;         359 AA.
AC   Q80WM5; Q3UVT2; Q80XX3;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Hyaluronan and proteoglycan link protein 3;
DE   Flags: Precursor;
GN   Name=Hapln3; Synonyms=Lpr3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000312|EMBL:AAP22049.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAP22049.1};
RX   PubMed=12663660; DOI=10.1074/jbc.m213100200;
RA   Spicer A.P., Joo A., Bowling R.A. Jr.;
RT   "A hyaluronan binding link protein gene family whose members are physically
RT   linked adjacent to chondroitin sulfate proteoglycan core protein genes: the
RT   missing links.";
RL   J. Biol. Chem. 278:21083-21091(2003).
RN   [2] {ECO:0000312|EMBL:AAP12624.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/cJ {ECO:0000312|EMBL:AAP12624.1};
RC   TISSUE=Brain {ECO:0000312|EMBL:AAP12624.1};
RA   Czipri M., Nesterovitch A.B., Glant T.T.;
RT   "Discoordinate expression of link proteins and skeletal tissue
RT   proteoglycans (aggrecan and versican) in different organs from early
RT   embryonic to adult age of mice.";
RL   Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4] {ECO:0000312|EMBL:AAP12624.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May function in hyaluronic acid binding.
CC       {ECO:0000303|PubMed:12663660}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the HAPLN family. {ECO:0000305}.
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DR   EMBL; AY262757; AAP22049.1; -; mRNA.
DR   EMBL; AY269788; AAP12624.1; -; mRNA.
DR   EMBL; AK136956; BAE23187.1; -; mRNA.
DR   EMBL; CH466543; EDL07078.1; -; Genomic_DNA.
DR   CCDS; CCDS21378.1; -.
DR   RefSeq; NP_839986.2; NM_178255.3.
DR   RefSeq; XP_006541190.1; XM_006541127.3.
DR   RefSeq; XP_006541191.1; XM_006541128.3.
DR   AlphaFoldDB; Q80WM5; -.
DR   SMR; Q80WM5; -.
DR   STRING; 10090.ENSMUSP00000032827; -.
DR   PhosphoSitePlus; Q80WM5; -.
DR   PaxDb; Q80WM5; -.
DR   PRIDE; Q80WM5; -.
DR   ProteomicsDB; 273271; -.
DR   Antibodypedia; 28522; 115 antibodies from 21 providers.
DR   DNASU; 67666; -.
DR   Ensembl; ENSMUST00000206092; ENSMUSP00000146090; ENSMUSG00000030606.
DR   GeneID; 67666; -.
DR   KEGG; mmu:67666; -.
DR   UCSC; uc009hxy.1; mouse.
DR   CTD; 145864; -.
DR   MGI; MGI:1914916; Hapln3.
DR   VEuPathDB; HostDB:ENSMUSG00000030606; -.
DR   eggNOG; ENOG502QWFF; Eukaryota.
DR   GeneTree; ENSGT00940000159628; -.
DR   HOGENOM; CLU_052285_1_0_1; -.
DR   InParanoid; Q80WM5; -.
DR   OMA; RPNCGSL; -.
DR   OrthoDB; 743812at2759; -.
DR   PhylomeDB; Q80WM5; -.
DR   TreeFam; TF332134; -.
DR   BioGRID-ORCS; 67666; 0 hits in 73 CRISPR screens.
DR   PRO; PR:Q80WM5; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; Q80WM5; protein.
DR   Bgee; ENSMUSG00000030606; Expressed in yolk sac and 59 other tissues.
DR   ExpressionAtlas; Q80WM5; baseline and differential.
DR   Genevisible; Q80WM5; MM.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005540; F:hyaluronic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR   GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 3.10.100.10; -; 2.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR000538; Link_dom.
DR   Pfam; PF07686; V-set; 1.
DR   Pfam; PF00193; Xlink; 2.
DR   PRINTS; PR01265; LINKMODULE.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00406; IGv; 1.
DR   SMART; SM00445; LINK; 2.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   SUPFAM; SSF56436; SSF56436; 2.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS01241; LINK_1; 2.
DR   PROSITE; PS50963; LINK_2; 2.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Extracellular matrix; Hyaluronic acid;
KW   Immunoglobulin domain; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..359
FT                   /note="Hyaluronan and proteoglycan link protein 3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000013191"
FT   DOMAIN          48..164
FT                   /note="Ig-like V-type"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          166..261
FT                   /note="Link 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00323,
FT                   ECO:0000305"
FT   DOMAIN          266..357
FT                   /note="Link 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00323,
FT                   ECO:0000305"
FT   DISULFID        70..146
FT                   /evidence="ECO:0000250|UniProtKB:P03994"
FT   DISULFID        188..259
FT                   /evidence="ECO:0000250|UniProtKB:P03994"
FT   DISULFID        212..233
FT                   /evidence="ECO:0000250|UniProtKB:P03994"
FT   DISULFID        286..355
FT                   /evidence="ECO:0000250|UniProtKB:P03994"
FT   DISULFID        311..332
FT                   /evidence="ECO:0000250|UniProtKB:P03994"
FT   CONFLICT        12
FT                   /note="F -> L (in Ref. 2; AAP12624)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        29..31
FT                   /note="DLS -> GLR (in Ref. 2; AAP12624)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   359 AA;  40740 MW;  81E8F78DA76BB1E3 CRC64;
     MSLLFLVLLS PFPCVLGLPF YNGFYYSNDL SGRTLGNGYG EGLFNGVKLV VETTEESLFS
     HQGASVTLPC HYHYEPALAS PRHVRVKWWK LSENGAPEQD VLVVIGQRHR SFGDYQGRVQ
     LRQDKQQEVS LELRDLRLED SGRYRCEVID GLEDESGLVE LELRGVVFPY QSREGRYQLN
     FHEAQQACQE QGAMVATFEQ LFRAWEEGLD WCNAGWLQDA SVQYPIVLPR QPCGGLGLAP
     GVRSYGQRHH RLHRYDVFCF AAALKGRVYY LENPKKLTLL EAREACQEDG AQISTVGQLF
     AAWKFRGLDR CDAGWLADGS ARYPIVHPRL NCGPPEPGVR TFGFPDPHTR YGVYCYVQH
 
 
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