Full text data of SCAMP4
SCAMP4
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Secretory carrier-associated membrane protein 4; Secretory carrier membrane protein 4
Secretory carrier-associated membrane protein 4; Secretory carrier membrane protein 4
hRBCD
IPI00056310
IPI00056310 Secretory carrier-associated membrane protein 4 Secretory carrier-associated membrane protein 4 membrane n/a n/a n/a n/a 1 n/a n/a 1 n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a integral membrane protein n/a found at its expected molecular weight found at molecular weight
IPI00056310 Secretory carrier-associated membrane protein 4 Secretory carrier-associated membrane protein 4 membrane n/a n/a n/a n/a 1 n/a n/a 1 n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a integral membrane protein n/a found at its expected molecular weight found at molecular weight
UniProt
Q969E2
ID SCAM4_HUMAN Reviewed; 229 AA.
AC Q969E2; Q8N2N1; Q8NAV0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 77.
DE RecName: Full=Secretory carrier-associated membrane protein 4;
DE Short=Secretory carrier membrane protein 4;
GN Name=SCAMP4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Probably involved in membrane protein trafficking (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q969E2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q969E2-2; Sequence=VSP_026446;
CC Name=3;
CC IsoId=Q969E2-3; Sequence=VSP_026447;
CC -!- SIMILARITY: Belongs to the SCAMP family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK074586; BAC11075.1; -; mRNA.
DR EMBL; AK074967; BAC11322.1; -; mRNA.
DR EMBL; AK092056; BAC03797.1; -; mRNA.
DR EMBL; BC011747; AAH11747.1; -; mRNA.
DR EMBL; BC016509; AAH16509.1; -; mRNA.
DR EMBL; BC062598; AAH62598.1; -; mRNA.
DR RefSeq; NP_524558.1; NM_079834.2.
DR RefSeq; XP_005259538.1; XM_005259481.1.
DR UniGene; Hs.144980; -.
DR ProteinModelPortal; Q969E2; -.
DR PhosphoSite; Q969E2; -.
DR DMDM; 47117277; -.
DR PaxDb; Q969E2; -.
DR PRIDE; Q969E2; -.
DR DNASU; 113178; -.
DR Ensembl; ENST00000316097; ENSP00000316007; ENSG00000227500.
DR Ensembl; ENST00000409472; ENSP00000386865; ENSG00000227500.
DR GeneID; 113178; -.
DR KEGG; hsa:113178; -.
DR UCSC; uc002luj.4; human.
DR CTD; 113178; -.
DR GeneCards; GC19P001905; -.
DR HGNC; HGNC:30385; SCAMP4.
DR HPA; HPA043284; -.
DR MIM; 613764; gene.
DR neXtProt; NX_Q969E2; -.
DR PharmGKB; PA134983341; -.
DR eggNOG; NOG243140; -.
DR HOGENOM; HOG000294221; -.
DR HOVERGEN; HBG071938; -.
DR InParanoid; Q969E2; -.
DR OMA; CATLGVN; -.
DR OrthoDB; EOG7FZ009; -.
DR ChiTaRS; SCAMP4; human.
DR GenomeRNAi; 113178; -.
DR NextBio; 78773; -.
DR PRO; PR:Q969E2; -.
DR ArrayExpress; Q969E2; -.
DR Bgee; Q969E2; -.
DR CleanEx; HS_SCAMP4; -.
DR Genevestigator; Q969E2; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR007273; SCAMP.
DR PANTHER; PTHR10687; PTHR10687; 1.
DR Pfam; PF04144; SCAMP; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Complete proteome; Membrane; Polymorphism;
KW Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1 229 Secretory carrier-associated membrane
FT protein 4.
FT /FTId=PRO_0000191259.
FT TOPO_DOM 1 39 Cytoplasmic (Potential).
FT TRANSMEM 40 60 Helical; (Potential).
FT TRANSMEM 61 81 Helical; (Potential).
FT TRANSMEM 105 125 Helical; (Potential).
FT TRANSMEM 149 169 Helical; (Potential).
FT TOPO_DOM 170 229 Cytoplasmic (Potential).
FT VAR_SEQ 99 132 Missing (in isoform 2).
FT /FTId=VSP_026446.
FT VAR_SEQ 132 229 CGWLSAIGFFQYSPGAAVVMLLPAIMFSVSAAMMAIAIMKV
FT HRIYRGAGGSFQKAQTEWNTGTWRNPPSREAQYNNFSGNSL
FT PEYPTVPSYPGSGQWP -> G (in isoform 3).
FT /FTId=VSP_026447.
FT VARIANT 49 49 A -> T (in dbSNP:rs45562539).
FT /FTId=VAR_061783.
SQ SEQUENCE 229 AA; 25728 MW; FA3EB084B3970334 CRC64;
MSEKENNFPP LPKFIPVKPC FYQNFSDEIP VEHQVLVKRI YRLWMFYCAT LGVNLIACLA
WWIGGGSGTN FGLAFVWLLL FTPCGYVCWF RPVYKAFRAD SSFNFMAFFF IFGAQFVLTV
IQAIGFSGWG ACGWLSAIGF FQYSPGAAVV MLLPAIMFSV SAAMMAIAIM KVHRIYRGAG
GSFQKAQTEW NTGTWRNPPS REAQYNNFSG NSLPEYPTVP SYPGSGQWP
//
ID SCAM4_HUMAN Reviewed; 229 AA.
AC Q969E2; Q8N2N1; Q8NAV0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-DEC-2001, sequence version 1.
DT 22-JAN-2014, entry version 77.
DE RecName: Full=Secretory carrier-associated membrane protein 4;
DE Short=Secretory carrier membrane protein 4;
GN Name=SCAMP4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Probably involved in membrane protein trafficking (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q969E2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q969E2-2; Sequence=VSP_026446;
CC Name=3;
CC IsoId=Q969E2-3; Sequence=VSP_026447;
CC -!- SIMILARITY: Belongs to the SCAMP family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AK074586; BAC11075.1; -; mRNA.
DR EMBL; AK074967; BAC11322.1; -; mRNA.
DR EMBL; AK092056; BAC03797.1; -; mRNA.
DR EMBL; BC011747; AAH11747.1; -; mRNA.
DR EMBL; BC016509; AAH16509.1; -; mRNA.
DR EMBL; BC062598; AAH62598.1; -; mRNA.
DR RefSeq; NP_524558.1; NM_079834.2.
DR RefSeq; XP_005259538.1; XM_005259481.1.
DR UniGene; Hs.144980; -.
DR ProteinModelPortal; Q969E2; -.
DR PhosphoSite; Q969E2; -.
DR DMDM; 47117277; -.
DR PaxDb; Q969E2; -.
DR PRIDE; Q969E2; -.
DR DNASU; 113178; -.
DR Ensembl; ENST00000316097; ENSP00000316007; ENSG00000227500.
DR Ensembl; ENST00000409472; ENSP00000386865; ENSG00000227500.
DR GeneID; 113178; -.
DR KEGG; hsa:113178; -.
DR UCSC; uc002luj.4; human.
DR CTD; 113178; -.
DR GeneCards; GC19P001905; -.
DR HGNC; HGNC:30385; SCAMP4.
DR HPA; HPA043284; -.
DR MIM; 613764; gene.
DR neXtProt; NX_Q969E2; -.
DR PharmGKB; PA134983341; -.
DR eggNOG; NOG243140; -.
DR HOGENOM; HOG000294221; -.
DR HOVERGEN; HBG071938; -.
DR InParanoid; Q969E2; -.
DR OMA; CATLGVN; -.
DR OrthoDB; EOG7FZ009; -.
DR ChiTaRS; SCAMP4; human.
DR GenomeRNAi; 113178; -.
DR NextBio; 78773; -.
DR PRO; PR:Q969E2; -.
DR ArrayExpress; Q969E2; -.
DR Bgee; Q969E2; -.
DR CleanEx; HS_SCAMP4; -.
DR Genevestigator; Q969E2; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR007273; SCAMP.
DR PANTHER; PTHR10687; PTHR10687; 1.
DR Pfam; PF04144; SCAMP; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Complete proteome; Membrane; Polymorphism;
KW Protein transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1 229 Secretory carrier-associated membrane
FT protein 4.
FT /FTId=PRO_0000191259.
FT TOPO_DOM 1 39 Cytoplasmic (Potential).
FT TRANSMEM 40 60 Helical; (Potential).
FT TRANSMEM 61 81 Helical; (Potential).
FT TRANSMEM 105 125 Helical; (Potential).
FT TRANSMEM 149 169 Helical; (Potential).
FT TOPO_DOM 170 229 Cytoplasmic (Potential).
FT VAR_SEQ 99 132 Missing (in isoform 2).
FT /FTId=VSP_026446.
FT VAR_SEQ 132 229 CGWLSAIGFFQYSPGAAVVMLLPAIMFSVSAAMMAIAIMKV
FT HRIYRGAGGSFQKAQTEWNTGTWRNPPSREAQYNNFSGNSL
FT PEYPTVPSYPGSGQWP -> G (in isoform 3).
FT /FTId=VSP_026447.
FT VARIANT 49 49 A -> T (in dbSNP:rs45562539).
FT /FTId=VAR_061783.
SQ SEQUENCE 229 AA; 25728 MW; FA3EB084B3970334 CRC64;
MSEKENNFPP LPKFIPVKPC FYQNFSDEIP VEHQVLVKRI YRLWMFYCAT LGVNLIACLA
WWIGGGSGTN FGLAFVWLLL FTPCGYVCWF RPVYKAFRAD SSFNFMAFFF IFGAQFVLTV
IQAIGFSGWG ACGWLSAIGF FQYSPGAAVV MLLPAIMFSV SAAMMAIAIM KVHRIYRGAG
GSFQKAQTEW NTGTWRNPPS REAQYNNFSG NSLPEYPTVP SYPGSGQWP
//
MIM
613764
*RECORD*
*FIELD* NO
613764
*FIELD* TI
*613764 SECRETORY CARRIER MEMBRANE PROTEIN 4; SCAMP4
*FIELD* TX
DESCRIPTION
Secretory carrier membrane proteins (SCAMPs) are widely distributed
read moreintegral membrane proteins implicated in membrane trafficking. Most
SCAMPs (e.g., SCAMP1; 606911) have N-terminal cytoplasmic NPF
(arg-pro-phe) repeats, 4 central transmembrane regions, and a short
C-terminal cytoplasmic tail. These SCAMPs likely have a role in
endocytosis that is mediated by their NPF repeats. Other SCAMPs, such as
SCAMP4, lack the NPF repeats and are therefore unlikely to function in
endocytosis (summary by Fernandez-Chacon and Sudhof, 2000).
CLONING
By searching EST databases, Fernandez-Chacon and Sudhof (2000)
identified mouse Scamp4. The deduced 230-amino acid mouse protein
contains 4 transmembrane domains that are highly conserved among other
SCAMPs, with little conservation at the N- and C-terminal ends. Scamp4
lacks the N-terminal NPF repeats found in several other SCAMPs. Northern
blot analysis revealed variable expression of Scamp4 in all rat tissues
examined, with highest expression in testis and liver.
Krebs and Pfaff (2001) cloned rat Scamp4. The deduced protein lacks the
calcium-binding, leucine zipper, and NPF motifs found in other SCAMPs,
but it has a putative protein kinase C (PKC; see 176960) phosphorylation
site. In situ hybridization showed that Scamp4 mRNA was relatively low
in female rat forebrain, with highest levels in ventromedial
hypothalamus, habenula, and hippocampus.
GENE FUNCTION
Using differential display PCR, Krebs and Pfaff (2001) found reduced
expression of Scamp4 mRNA in the ventromedial hypothalamus of female rat
brains after progesterone treatment, following estrogen priming. In situ
hybridization showed that Scamp4 mRNA was less abundant in habenula and
ventromedial hypothalamus during proestrus, when circulating levels of
estrogen and progesterone are at their peak, than during diestrus-1,
when circulating hormone levels are low. Krebs and Pfaff (2001) noted
that Scamp4 mRNA levels are high in habenula, a brain area rich in mast
cells that may be involved in courtship behavior. They suggested that
SCAMP4 may be involved in reproductive behaviors associated with mast
cell activity in the central nervous system.
MAPPING
Gross (2011) mapped the SCAMP4 gene to chromosome 19p13.3 based on an
alignment of the SCAMP4 sequence (GenBank GENBANK BC011747) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Fernandez-Chacon, R.; Sudhof, T. C.: Novel SCAMPs lacking NPF
repeats: ubiquitous and synaptic vesicle-specific forms implicate
SCAMPs in multiple membrane-trafficking functions. J. Neurosci. 20:
7941-7950, 2000.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 3/25/2011.
3. Krebs, C. J.; Pfaff, D. W.: Expression of the SCAMP-4 gene, a
new member of the secretory carrier membrane protein family, is repressed
by progesterone in brain regions associated with female sexual behavior. Molec.
Brain Res. 88: 144-154, 2001.
*FIELD* CN
Matthew B. Gross - updated: 03/25/2011
*FIELD* CD
Paul J. Converse: 2/22/2011
*FIELD* ED
mgross: 03/25/2011
mgross: 2/22/2011
*RECORD*
*FIELD* NO
613764
*FIELD* TI
*613764 SECRETORY CARRIER MEMBRANE PROTEIN 4; SCAMP4
*FIELD* TX
DESCRIPTION
Secretory carrier membrane proteins (SCAMPs) are widely distributed
read moreintegral membrane proteins implicated in membrane trafficking. Most
SCAMPs (e.g., SCAMP1; 606911) have N-terminal cytoplasmic NPF
(arg-pro-phe) repeats, 4 central transmembrane regions, and a short
C-terminal cytoplasmic tail. These SCAMPs likely have a role in
endocytosis that is mediated by their NPF repeats. Other SCAMPs, such as
SCAMP4, lack the NPF repeats and are therefore unlikely to function in
endocytosis (summary by Fernandez-Chacon and Sudhof, 2000).
CLONING
By searching EST databases, Fernandez-Chacon and Sudhof (2000)
identified mouse Scamp4. The deduced 230-amino acid mouse protein
contains 4 transmembrane domains that are highly conserved among other
SCAMPs, with little conservation at the N- and C-terminal ends. Scamp4
lacks the N-terminal NPF repeats found in several other SCAMPs. Northern
blot analysis revealed variable expression of Scamp4 in all rat tissues
examined, with highest expression in testis and liver.
Krebs and Pfaff (2001) cloned rat Scamp4. The deduced protein lacks the
calcium-binding, leucine zipper, and NPF motifs found in other SCAMPs,
but it has a putative protein kinase C (PKC; see 176960) phosphorylation
site. In situ hybridization showed that Scamp4 mRNA was relatively low
in female rat forebrain, with highest levels in ventromedial
hypothalamus, habenula, and hippocampus.
GENE FUNCTION
Using differential display PCR, Krebs and Pfaff (2001) found reduced
expression of Scamp4 mRNA in the ventromedial hypothalamus of female rat
brains after progesterone treatment, following estrogen priming. In situ
hybridization showed that Scamp4 mRNA was less abundant in habenula and
ventromedial hypothalamus during proestrus, when circulating levels of
estrogen and progesterone are at their peak, than during diestrus-1,
when circulating hormone levels are low. Krebs and Pfaff (2001) noted
that Scamp4 mRNA levels are high in habenula, a brain area rich in mast
cells that may be involved in courtship behavior. They suggested that
SCAMP4 may be involved in reproductive behaviors associated with mast
cell activity in the central nervous system.
MAPPING
Gross (2011) mapped the SCAMP4 gene to chromosome 19p13.3 based on an
alignment of the SCAMP4 sequence (GenBank GENBANK BC011747) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Fernandez-Chacon, R.; Sudhof, T. C.: Novel SCAMPs lacking NPF
repeats: ubiquitous and synaptic vesicle-specific forms implicate
SCAMPs in multiple membrane-trafficking functions. J. Neurosci. 20:
7941-7950, 2000.
2. Gross, M. B.: Personal Communication. Baltimore, Md. 3/25/2011.
3. Krebs, C. J.; Pfaff, D. W.: Expression of the SCAMP-4 gene, a
new member of the secretory carrier membrane protein family, is repressed
by progesterone in brain regions associated with female sexual behavior. Molec.
Brain Res. 88: 144-154, 2001.
*FIELD* CN
Matthew B. Gross - updated: 03/25/2011
*FIELD* CD
Paul J. Converse: 2/22/2011
*FIELD* ED
mgross: 03/25/2011
mgross: 2/22/2011