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O35206

- COFA1_MOUSE

UniProt

O35206 - COFA1_MOUSE

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Protein

Collagen alpha-1(XV) chain

Gene

Col15a1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Structural protein that stabilizes microvessels and muscle cells, both in heart and in skeletal muscle.
Restin potently inhibits angiogenesis.

GO - Molecular functioni

  1. structural molecule activity Source: InterPro

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199055. Collagen degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(XV) chain
Cleaved into the following chain:
Alternative name(s):
Endostatin-XV
Gene namesi
Name:Col15a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:88449. Col15a1.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: MGI
  2. collagen trimer Source: UniProtKB-KW
  3. extracellular space Source: Ensembl
  4. extracellular vesicular exosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence AnalysisAdd
BLAST
Chaini32 – 13671336Collagen alpha-1(XV) chainPRO_0000005790Add
BLAST
Chaini1177 – 1365189RestinPRO_0000005791Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi305 – 3051N-linked (GlcNAc...)Sequence Analysis
Glycosylationi323 – 3231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi348 – 3481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi375 – 3751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi402 – 4021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi673 – 6731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi792 – 7921N-linked (GlcNAc...)Sequence Analysis
Glycosylationi795 – 7951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi799 – 7991N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1216 ↔ 13561 Publication
Disulfide bondi1318 ↔ 13481 Publication

Post-translational modificationi

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.By similarity
O-glycosylated; contains chondroitin sulfate.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

MaxQBiO35206.
PaxDbiO35206.
PRIDEiO35206.

PTM databases

PhosphoSiteiO35206.

Expressioni

Tissue specificityi

Detected in testis, brain, heart, kidney, skeletal muscle and skin (at protein level). Detected in heart and skeletal muscle.1 Publication

Developmental stagei

Detected at low levels from day 7 to 11 of embryonic development. Levels are much increased and remain high from day 15 to 17.

Gene expression databases

BgeeiO35206.
CleanExiMM_COL15A1.
ExpressionAtlasiO35206. baseline and differential.
GenevestigatoriO35206.

Interactioni

Subunit structurei

Trimer; disulfide-linked.By similarity

Protein-protein interaction databases

IntActiO35206. 1 interaction.
MINTiMINT-4104642.

Structurei

Secondary structure

1
1367
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1197 – 12015Combined sources
Helixi1212 – 122211Combined sources
Beta strandi1229 – 12335Combined sources
Helixi1240 – 12423Combined sources
Helixi1246 – 12483Combined sources
Beta strandi1249 – 12513Combined sources
Beta strandi1261 – 12644Combined sources
Helixi1267 – 12704Combined sources
Beta strandi1271 – 12733Combined sources
Turni1291 – 12933Combined sources
Beta strandi1301 – 13033Combined sources
Helixi1318 – 13214Combined sources
Beta strandi1329 – 13346Combined sources
Helixi1335 – 13373Combined sources
Beta strandi1339 – 13413Combined sources
Beta strandi1344 – 13474Combined sources
Beta strandi1355 – 13584Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DY2X-ray2.00A1192-1367[»]
ProteinModelPortaliO35206.
SMRiO35206. Positions 1112-1165, 1194-1361.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35206.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini54 – 249196Laminin G-likeAdd
BLAST
Domaini605 – 66561Collagen-like 1Add
BLAST
Domaini666 – 71752Collagen-like 2Add
BLAST
Domaini808 – 85043Collagen-like 3Add
BLAST
Domaini863 – 91250Collagen-like 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni229 – 604376Nonhelical region 1 (NC1)Add
BLAST
Regioni605 – 718114Triple-helical region 1 (COL1)Add
BLAST
Regioni719 – 74830Nonhelical region 2 (NC2)Add
BLAST
Regioni749 – 78335Triple-helical region 2 (COL2)Add
BLAST
Regioni784 – 80724Nonhelical region 3 (NC3)Add
BLAST
Regioni808 – 85245Triple-helical region 3 (COL3)Add
BLAST
Regioni853 – 86311Nonhelical region 4 (NC4)Add
BLAST
Regioni864 – 93471Triple-helical region 4 (COL4)Add
BLAST
Regioni935 – 96834Nonhelical region 5 (NC5)Add
BLAST
Regioni969 – 99830Triple-helical region 5 (COL5)Add
BLAST
Regioni999 – 103133Nonhelical region 6 (NC6)Add
BLAST
Regioni1032 – 108655Triple-helical region 6 (COL6)Add
BLAST
Regioni1087 – 109610Nonhelical region 7 (NC7)
Regioni1097 – 111115Triple-helical region 7 (COL7)Add
BLAST
Regioni1112 – 1367256Nonhelical region 8 (NC8)Add
BLAST

Sequence similaritiesi

Belongs to the multiplexin collagen family.Curated
Contains 4 collagen-like domains.Curated
Contains 1 laminin G-like domain.Curated

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00710000106713.
HOGENOMiHOG000231591.
HOVERGENiHBG080337.
InParanoidiO35206.
KOiK08135.
OMAiPELITFH.
PhylomeDBiO35206.
TreeFamiTF315821.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
3.10.100.10. 1 hit.
InterProiIPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR010515. Collagenase_NC10/endostatin.
IPR013320. ConA-like_dom.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF01391. Collagen. 4 hits.
PF06482. Endostatin. 2 hits.
[Graphical view]
SMARTiSM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF56436. SSF56436. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O35206-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTHRRTAQGR RPRWLLSIIS ALLSAVLQTR AATGSASQVH LDLTVLIGVP
60 70 80 90 100
LPSSVSFTTG YGGFPAYSFG PGANVGRPAR TLIPPTFFRD FAIGVAVKPN
110 120 130 140 150
SAQGGVLFAI TDAFQKVIYL GLRLSSVEDG RQRVILYYTE PGSHVSREAA
160 170 180 190 200
VFSVPVMTNR WNRFAVTVQG EEVALFMDCE EQSQVRFQRS SWPLTFEPSA
210 220 230 240 250
GIFVGNAGAM GLERFTGSIQ QLTIYSDPRT PEELCEAQES SASGEASGFQ
260 270 280 290 300
EMDEVAEIME AVTYTQAPPK ESHVDPISVP PTSSSPAEDS ELSGEPVPEG
310 320 330 340 350
TPETNLSIIG HSSPEQGSGE ILNDTLEVHA MDGDPGTDDG SGDGALLNVT
360 370 380 390 400
DGQGLSATAT GEASVPVTTV LEAENGSMPT GSPTLAMFTQ SIREVDTPDP
410 420 430 440 450
ENLTTTASGD GEVPTSTDGD TEADSSPTGG PTLKPREEAT LGSHGEEWLT
460 470 480 490 500
PAVSKMPLKA FEEEEASGTA IDSLDVIFTP TVVLEQVSRR PTDIQATFTP
510 520 530 540 550
TVVLEETSGA PTDTQDALTP TVAPEQMFTA EPTDGGDLVA STEEAEEEGS
560 570 580 590 600
GSMPPSGPPL PTPTVTPKRQ VTLVGVEAEG SGPVGGLDEG SGSGDIVGNE
610 620 630 640 650
DLLRGPPGPP GPPGSPGIPG KPGTDVFMGP PGSPGEDGAP GEPGPQGPEG
660 670 680 690 700
QPGLDGASGQ QGMKGEKGAR GPNGSAGEKG DPGNRGLPGP PGKNGEVGTP
710 720 730 740 750
GVMGPPGPPG PPGPPGPGCT TELGFEIEGS GDVRLLSKPT ISGPTSPSGP
760 770 780 790 800
KGEKGEQGAK GERGADGTST MGPPGPRGPP GHVEVLSSSL INITNGSMNF
810 820 830 840 850
SDIPELMGPP GPDGVPGLPG FPGPRGPKGD TGVPGFPGLK GEQGEKGEPG
860 870 880 890 900
AILTGDVPLE MMKGRKGEPG IHGAPGPMGP KGPPGHKGEF GLPGRPGRPG
910 920 930 940 950
LNGLKGAKGD RGVTLPGPPG LPGPPGPPGP PGAVVNIKGA VFPIPARPHC
960 970 980 990 1000
KTPVGTAHPG DPELVTFHGV KGEKGSWGLP GSKGEKGDQG AQGPPGPPVD
1010 1020 1030 1040 1050
PAYLRHFLNS LKGENEDASF RGESSNNLFV SGPPGLPGYP GLVGQKGEAV
1060 1070 1080 1090 1100
VGPQGPPGIP GLPGPPGFGR PGVPGPPGPP GPPGPPAILG AAVALPGPPG
1110 1120 1130 1140 1150
PPGQPGLPGS RNLVTALSDM GDMLQKAHLV IEGTFIYLRD SGEFFIRVRD
1160 1170 1180 1190 1200
GWKKLQLGEL IPIPADSPPP PALSSNPYQP QPPLNPILSA NYERPVLHLV
1210 1220 1230 1240 1250
ALNTPVAGDI RADFQCFQQA RAAGLLSTFR AFLSSHLQDL STVVRKAERF
1260 1270 1280 1290 1300
GLPIVNLKGQ VLFNNWDSIF SGDGGQFNTH IPIYSFDGRD VMTDPSWPQK
1310 1320 1330 1340 1350
VVWHGSNPHG VRLVDKYCEA WRTTDMAVTG FASPLSTGKI LDQKAYSCAN
1360
RLIVLCIENS FMTDTRK
Length:1,367
Mass (Da):140,472
Last modified:April 3, 2007 - v2
Checksum:iBD92E26B5E99B607
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti380 – 3801T → L in AAC53387. (PubMed:9339358)Curated
Sequence conflicti499 – 4991T → K in BAE21987. (PubMed:16141072)Curated
Sequence conflicti569 – 5691R → K in AAG27545. (PubMed:11068203)Curated
Sequence conflicti593 – 5931S → A in AAG27545. (PubMed:11068203)Curated
Sequence conflicti699 – 6991T → P in AAC53387. (PubMed:9339358)Curated
Sequence conflicti699 – 6991T → P in AAG27545. (PubMed:11068203)Curated
Sequence conflicti736 – 7361L → M in AAG27545. (PubMed:11068203)Curated
Sequence conflicti779 – 7791P → R in AAC53387. (PubMed:9339358)Curated
Sequence conflicti1116 – 11161A → G in AAC53387. (PubMed:9339358)Curated
Sequence conflicti1116 – 11161A → G in AAG27545. (PubMed:11068203)Curated
Sequence conflicti1309 – 13091H → Y in AAG27545. (PubMed:11068203)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF011450 mRNA. Translation: AAC53387.1.
AF261131
, AF261109, AF261110, AF261111, AF261112, AF261113, AF261114, AF261115, AF261116, AF261117, AF261118, AF261119, AF261120, AF261121, AF261122, AF261123, AF261124, AF261125, AF261126, AF261127, AF261128, AF261129, AF261130 Genomic DNA. Translation: AAG27545.1.
AK134030 mRNA. Translation: BAE21987.1.
AL772232, AL928652 Genomic DNA. Translation: CAM13891.1.
AL928652, AL772232 Genomic DNA. Translation: CAM20188.1.
CCDSiCCDS18159.1.
RefSeqiNP_034058.2. NM_009928.3.
UniGeneiMm.233547.

Genome annotation databases

EnsembliENSMUST00000102917; ENSMUSP00000099981; ENSMUSG00000028339.
GeneIDi12819.
KEGGimmu:12819.
UCSCiuc008sum.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF011450 mRNA. Translation: AAC53387.1 .
AF261131
, AF261109 , AF261110 , AF261111 , AF261112 , AF261113 , AF261114 , AF261115 , AF261116 , AF261117 , AF261118 , AF261119 , AF261120 , AF261121 , AF261122 , AF261123 , AF261124 , AF261125 , AF261126 , AF261127 , AF261128 , AF261129 , AF261130 Genomic DNA. Translation: AAG27545.1 .
AK134030 mRNA. Translation: BAE21987.1 .
AL772232 , AL928652 Genomic DNA. Translation: CAM13891.1 .
AL928652 , AL772232 Genomic DNA. Translation: CAM20188.1 .
CCDSi CCDS18159.1.
RefSeqi NP_034058.2. NM_009928.3.
UniGenei Mm.233547.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DY2 X-ray 2.00 A 1192-1367 [» ]
ProteinModelPortali O35206.
SMRi O35206. Positions 1112-1165, 1194-1361.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O35206. 1 interaction.
MINTi MINT-4104642.

PTM databases

PhosphoSitei O35206.

Proteomic databases

MaxQBi O35206.
PaxDbi O35206.
PRIDEi O35206.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000102917 ; ENSMUSP00000099981 ; ENSMUSG00000028339 .
GeneIDi 12819.
KEGGi mmu:12819.
UCSCi uc008sum.1. mouse.

Organism-specific databases

CTDi 1306.
MGIi MGI:88449. Col15a1.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00710000106713.
HOGENOMi HOG000231591.
HOVERGENi HBG080337.
InParanoidi O35206.
KOi K08135.
OMAi PELITFH.
PhylomeDBi O35206.
TreeFami TF315821.

Enzyme and pathway databases

Reactomei REACT_198984. Collagen biosynthesis and modifying enzymes.
REACT_199046. Assembly of collagen fibrils and other multimeric structures.
REACT_199055. Collagen degradation.

Miscellaneous databases

ChiTaRSi Col15a1. mouse.
EvolutionaryTracei O35206.
NextBioi 282290.
PROi O35206.
SOURCEi Search...

Gene expression databases

Bgeei O35206.
CleanExi MM_COL15A1.
ExpressionAtlasi O35206. baseline and differential.
Genevestigatori O35206.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
3.10.100.10. 1 hit.
InterProi IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR010515. Collagenase_NC10/endostatin.
IPR013320. ConA-like_dom.
IPR001791. Laminin_G.
[Graphical view ]
Pfami PF01391. Collagen. 4 hits.
PF06482. Endostatin. 2 hits.
[Graphical view ]
SMARTi SM00282. LamG. 1 hit.
SM00210. TSPN. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
SSF56436. SSF56436. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of mouse type XV collagen sequences and mapping of the corresponding gene to 4B1-3. Comparison of mouse and human alpha 1 (XV) collagen sequences indicates divergence in the number of small collagenous domains."
    Haegg P.M., Horelli-Kuitunen N., Eklund L., Palotie A., Pihlajaniemi T.
    Genomics 45:31-41(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: 129/Sv.
    Tissue: Kidney.
  2. "Structure of the mouse type XV collagen gene, Col15a1, comparison with the human COL15A1 gene and functional analysis of the promoters of both genes."
    Eklund L., Muona A., Lietard J., Pihlajaniemi T.
    Matrix Biol. 19:489-500(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Thymus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "Endostatins derived from collagens XV and XVIII differ in structural and binding properties, tissue distribution and anti-angiogenic activity."
    Sasaki T., Larsson H., Tisi D., Claesson-Welsh L., Hohenester E., Timpl R.
    J. Mol. Biol. 301:1179-1190(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: FUNCTION.
  7. "Crystal structure of the angiogenesis inhibitor endostatin at 1.5-A resolution."
    Hohenester E., Sasaki T., Olsen B.R., Timpl R.
    EMBO J. 17:1656-1664(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1192-1367, DISULFIDE BONDS.

Entry informationi

Entry nameiCOFA1_MOUSE
AccessioniPrimary (citable) accession number: O35206
Secondary accession number(s): A2AJY3, Q3UZ71, Q9EQD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: April 3, 2007
Last modified: November 26, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

The name Restin has also been used for CAP-Gly domain-containing linker protein 1 the product of the CLIP1 gene.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3